ID CPXB_PRIM2 Reviewed; 1049 AA. AC P14779; A0A0B6AQ66; Q9AE23; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000305}; DE AltName: Full=Cytochrome P450(BM-3) {ECO:0000303|PubMed:15299332}; DE AltName: Full=Cytochrome P450BM-3 {ECO:0000303|PubMed:8342039, ECO:0000312|EMBL:AAK19020.1}; DE AltName: Full=Fatty acid monooxygenase {ECO:0000303|PubMed:3106359}; DE AltName: Full=Flavocytochrome P450 BM3 {ECO:0000303|PubMed:11695889, ECO:0000303|PubMed:14653735}; DE Includes: DE RecName: Full=Cytochrome P450 102A1; DE EC=1.14.14.1 {ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081}; DE Includes: DE RecName: Full=NADPH--cytochrome P450 reductase; DE EC=1.6.2.4 {ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081}; GN Name=cyp102A1 {ECO:0000312|EMBL:AJI21949.1}; Synonyms=cyp102; GN ORFNames=BG04_163 {ECO:0000312|EMBL:AJI21949.1}; OS Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / OS NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19) OS (Bacillus megaterium). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia. OX NCBI_TaxID=1348623; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB RC 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19 RC {ECO:0000303|PubMed:2544578}; RX PubMed=2544578; DOI=10.1016/s0021-9258(18)60416-8; RA Ruettinger R.T., Wen L.-P., Fulco A.J.; RT "Coding nucleotide, 5' regulatory, and deduced amino acid sequences of P- RT 450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from RT Bacillus megaterium."; RL J. Biol. Chem. 264:10987-10995(1989). RN [2] {ECO:0000312|EMBL:AJI21949.1, ECO:0000312|Proteomes:UP000031829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB RC 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19 RC {ECO:0000312|EMBL:AJI21949.1}; RX PubMed=25931591; DOI=10.1128/genomea.00151-15; RA Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G., RA Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Gibbons H.S., RA Coyne S.R., Lo C.C., Meincke L., Munk A.C., Koroleva G.I., Rosenzweig C.N., RA Palacios G.F., Redden C.L., Minogue T.D., Chain P.S.; RT "Complete genome sequences for 35 biothreat assay-relevant bacillus RT species."; RL Genome Announc. 3:0-0(2015). RN [3] {ECO:0000312|EMBL:AAK19020.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29, AND INDUCTION. RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB RC 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19 RC {ECO:0000303|PubMed:1544926}; RX PubMed=1544926; DOI=10.1016/s0021-9258(18)42797-4; RA Shaw G.C., Fulco A.J.; RT "Barbiturate-mediated regulation of expression of the cytochrome P450BM-3 RT gene of Bacillus megaterium by Bm3R1 protein."; RL J. Biol. Chem. 267:5515-5526(1992). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION. RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB RC 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19 RC {ECO:0000303|PubMed:3106359}; RX PubMed=3106359; DOI=10.1016/s0021-9258(18)48295-6; RA Wen L.P., Fulco A.J.; RT "Cloning of the gene encoding a catalytically self-sufficient cytochrome P- RT 450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium RT and its functional expression and regulation in heterologous (Escherichia RT coli) and homologous (Bacillus megaterium) hosts."; RL J. Biol. Chem. 262:6676-6682(1987). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=1727637; DOI=10.1016/0003-9861(92)90045-x; RA Boddupalli S.S., Pramanik B.C., Slaughter C.A., Estabrook R.W., RA Peterson J.A.; RT "Fatty acid monooxygenation by P450BM-3: product identification and RT proposed mechanisms for the sequential hydroxylation reactions."; RL Arch. Biochem. Biophys. 292:20-28(1992). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-75; PHE-88 AND RP LEU-189. RX PubMed=16566047; DOI=10.1002/cbic.200500444; RA Budde M., Morr M., Schmid R.D., Urlacher V.B.; RT "Selective hydroxylation of highly branched fatty acids and their RT derivatives by CYP102A1 from Bacillus megaterium."; RL ChemBioChem 7:789-794(2006). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18020460; DOI=10.1021/bi701945j; RA Chowdhary P.K., Keshavan N., Nguyen H.Q., Peterson J.A., Gonzalez J.E., RA Haines D.C.; RT "Bacillus megaterium CYP102A1 oxidation of acyl homoserine lactones and RT acyl homoserines."; RL Biochemistry 46:14429-14437(2007). RN [8] {ECO:0007744|PDB:2HPD} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-472 IN COMPLEX WITH HEME. RX PubMed=8342039; DOI=10.1126/science.8342039; RA Ravichandran K.G., Boddupalli S.S., Hasemann C.A., Peterson J.A., RA Deisenhofer J.; RT "Crystal structure of hemoprotein domain of P450BM-3, a prototype for RT microsomal P450's."; RL Science 261:731-736(1993). RN [9] {ECO:0007744|PDB:2BMH} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 IN COMPLEX WITH HEME. RX PubMed=15299332; DOI=10.1107/s0907444994009194; RA Li H., Poulos T.L.; RT "Modeling protein-substrate interactions in the heme domain of cytochrome RT P450(BM-3)."; RL Acta Crystallogr. D 51:21-32(1995). RN [10] {ECO:0007744|PDB:1FAH} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-472 OF MUTANT ALA-269 IN COMPLEX RP WITH HEME, CATALYTIC ACTIVITY, COFACTOR, SITE, AND MUTAGENESIS OF THR-269. RX PubMed=7578081; DOI=10.1021/bi00045a014; RA Yeom H., Sligar S.G., Li H., Poulos T.L., Fulco A.J.; RT "The role of Thr268 in oxygen activation of cytochrome P450BM-3."; RL Biochemistry 34:14733-14740(1995). RN [11] {ECO:0007744|PDB:1FAG} RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-472 IN COMPLEX WITH HEME AND RP PALMITOLEIC ACID. RX PubMed=9033595; DOI=10.1038/nsb0297-140; RA Li H.Y., Poulos T.L.; RT "The structure of the cytochrome p450BM-3 haem domain complexed with the RT fatty acid substrate, palmitoleic acid."; RL Nat. Struct. Biol. 4:140-146(1997). RN [12] {ECO:0007744|PDB:1BU7, ECO:0007744|PDB:1BVY} RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-650 IN COMPLEX WITH FMN AND RP HEME. RX PubMed=10051560; DOI=10.1073/pnas.96.5.1863; RA Sevrioukova I.F., Li H., Zhang H., Peterson J.A., Poulos T.L.; RT "Structure of a cytochrome P450-redox partner electron-transfer complex."; RL Proc. Natl. Acad. Sci. U.S.A. 96:1863-1868(1999). RN [13] {ECO:0007744|PDB:1JME} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 OF MUTANT HIS-394 IN COMPLEX RP WITH HEME, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-394. RX PubMed=11695889; DOI=10.1021/bi010717e; RA Ost T.W., Munro A.W., Mowat C.G., Taylor P.R., Pesseguiero A., Fulco A.J., RA Cho A.K., Cheesman M.A., Walkinshaw M.D., Chapman S.K.; RT "Structural and spectroscopic analysis of the F393H mutant of RT flavocytochrome P450 BM3."; RL Biochemistry 40:13430-13438(2001). RN [14] {ECO:0007744|PDB:1JPZ} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471 IN COMPLEX WITH HEME AND RP N-PALMITOYLGLYCINE, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11695892; DOI=10.1021/bi011197q; RA Haines D.C., Tomchick D.R., Machius M., Peterson J.A.; RT "Pivotal role of water in the mechanism of P450BM-3."; RL Biochemistry 40:13456-13465(2001). RN [15] {ECO:0007744|PDB:1P0V, ECO:0007744|PDB:1P0W, ECO:0007744|PDB:1P0X} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 OF MUTANTS ALA/TRP/TYR-394 RP IN COMPLEXES WITH HEME, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF RP PHE-394. RX PubMed=14653735; DOI=10.1021/ja035731o; RA Ost T.W., Clark J., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A., RA Chapman S.K., Daff S.; RT "Oxygen activation and electron transfer in flavocytochrome P450 BM3."; RL J. Am. Chem. Soc. 125:15010-15020(2003). RN [16] {ECO:0007744|PDB:1SMI, ECO:0007744|PDB:1SMJ} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-472 OF MUTANT GLU-265 IN RP COMPLEXES WITH HEME AND PALMITOLEIC ACID. RX PubMed=15020590; DOI=10.1074/jbc.m401717200; RA Joyce M.G., Girvan H.M., Munro A.W., Leys D.; RT "A single mutation in cytochrome P450 BM3 induces the conformational RT rearrangement seen upon substrate binding in the wild-type enzyme."; RL J. Biol. Chem. 279:23287-23293(2004). RN [17] {ECO:0007744|PDB:1YQO, ECO:0007744|PDB:1YQP} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-456 OF MUTANTS ALA/ASN-269 IN RP COMPLEXES WITH HEME, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL RP PROPERTIES, ENZYME KINETICS, ABSORPTION SPECTROSCOPY, REDOX POTENTIOMETRY RP OF HEME, AND MUTAGENESIS OF THR-269 AND PHE-394. RX PubMed=16403573; DOI=10.1016/j.jinorgbio.2005.11.020; RA Clark J.P., Miles C.S., Mowat C.G., Walkinshaw M.D., Reid G.A., Daff S.N., RA Chapman S.K.; RT "The role of Thr268 and Phe393 in cytochrome P450 BM3."; RL J. Inorg. Biochem. 100:1075-1090(2006). RN [18] {ECO:0007744|PDB:1ZO9} RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-471 IN COMPLEX WITH HEME AND RP N-PALMITOYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF ARG-48. RX PubMed=18004886; DOI=10.1021/bi701667m; RA Hegde A., Haines D.C., Bondlela M., Chen B., Schaffer N., Tomchick D.R., RA Machius M., Nguyen H., Chowdhary P.K., Stewart L., Lopez C., Peterson J.A.; RT "Interactions of substrates at the surface of P450s can greatly enhance RT substrate potency."; RL Biochemistry 46:14010-14017(2007). RN [19] {ECO:0007744|PDB:2J1M, ECO:0007744|PDB:2J4S} RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-456 IN COMPLEXES WITH HEME. RX PubMed=17429965; DOI=10.1021/ja067036x; RA Kuper J., Wong T.S., Roccatano D., Wilmanns M., Schwaneberg U.; RT "Understanding a mechanism of organic cosolvent inactivation in heme RT monooxygenase P450 BM-3."; RL J. Am. Chem. Soc. 129:5786-5787(2007). RN [20] {ECO:0007744|PDB:2IJ2, ECO:0007744|PDB:2IJ3, ECO:0007744|PDB:2IJ4} RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 2-471 OF WILD-TYPE AND MUTANTS RP HIS/LYS-265 IN COMPLEXES WITH HEME, FUNCTION, CATALYTIC ACTIVITY, AND RP MUTAGENESIS OF ALA-265. RX PubMed=17077084; DOI=10.1074/jbc.m607949200; RA Girvan H.M., Seward H.E., Toogood H.S., Cheesman M.R., Leys D., Munro A.W.; RT "Structural and spectroscopic characterization of P450 BM3 mutants with RT unprecedented P450 heme iron ligand sets. New heme ligation states RT influence conformational equilibria in P450 BM3."; RL J. Biol. Chem. 282:564-572(2007). RN [21] {ECO:0007744|PDB:2UWH} RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-459 OF MUTANT PHE-83 IN COMPLEX RP WITH HEME AND PALMITIC ACID, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, AND MUTAGENESIS OF ALA-83. RX PubMed=17868686; DOI=10.1016/j.jmb.2007.08.015; RA Huang W.C., Westlake A.C., Marechal J.D., Joyce M.G., Moody P.C., RA Roberts G.C.; RT "Filling a hole in cytochrome P450 BM3 improves substrate binding and RT catalytic efficiency."; RL J. Mol. Biol. 373:633-651(2007). RN [22] {ECO:0007744|PDB:3BEN} RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-470 IN COMPLEX WITH HEME AND RP SUBSTRATE INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=18298086; DOI=10.1021/bi7023964; RA Haines D.C., Chen B., Tomchick D.R., Bondlela M., Hegde A., Machius M., RA Peterson J.A.; RT "Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of RT substrate access channel."; RL Biochemistry 47:3662-3670(2008). RN [23] {ECO:0007744|PDB:3CBD} RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-456 OF MUTANT RP ALA-79/TYR-139/ILE-176/ILE-179/VAL-185/GLN-237/GLY-253/SER-256/VAL-291/THR-296/VAL-354 RP IN COMPLEX WITH HEME AND N-PALMITOYLGLYCINE, FUNCTION, CATALYTIC ACTIVITY, RP AND BIOTECHNOLOGY. RX PubMed=18619466; DOI=10.1016/j.jmb.2008.06.060; RA Fasan R., Meharenna Y.T., Snow C.D., Poulos T.L., Arnold F.H.; RT "Evolutionary history of a specialized p450 propane monooxygenase."; RL J. Mol. Biol. 383:1069-1080(2008). RN [24] {ECO:0007744|PDB:3EKB, ECO:0007744|PDB:3EKD, ECO:0007744|PDB:3EKF} RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-471 OF MUTANTS CYS/MET/GLN-265 RP IN COMPLEXES WITH HEME AND PALMITOLEIC ACID, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SPECTROSCOPIC STUDIES, REDOX RP POTENTIOMETRY OF HEME, AND MUTAGENESIS OF ALA-265. RX PubMed=18721129; DOI=10.1042/bj20081133; RA Girvan H.M., Toogood H.S., Littleford R.E., Seward H.E., Smith W.E., RA Ekanem I.S., Leys D., Cheesman M.R., Munro A.W.; RT "Novel haem co-ordination variants of flavocytochrome P450BM3."; RL Biochem. J. 417:65-76(2009). RN [25] {ECO:0007744|PDB:3HF2} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-482 OF MUTANT PRO-402 IN COMPLEX RP WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL RP PROPERTIES, REDOX POTENTIOMETRY OF HEME, BIOTECHNOLOGY, AND MUTAGENESIS OF RP ILE-402. RX PubMed=19492389; DOI=10.1002/cbic.200900279; RA Whitehouse C.J., Bell S.G., Yang W., Yorke J.A., Blanford C.F., RA Strong A.J., Morse E.J., Bartlam M., Rao Z., Wong L.L.; RT "A highly active single-mutation variant of P450BM3 (CYP102A1)."; RL ChemBioChem 10:1654-1656(2009). RN [26] {ECO:0007744|PDB:3KX3, ECO:0007744|PDB:3KX4, ECO:0007744|PDB:3KX5} RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-471 OF MUTANTS GLU-87; GLU-262 RP AND GLU-402 IN COMPLEXES WITH HEME AND N-PALMITOYLGLYCINE, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, REDOX RP POTENTIOMETRY OF HEME, AND MUTAGENESIS OF LEU-87; PHE-262 AND ILE-402. RX PubMed=20180779; DOI=10.1042/bj20091603; RA Girvan H.M., Levy C.W., Williams P., Fisher K., Cheesman M.R., Rigby S.E., RA Leys D., Munro A.W.; RT "Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 RT BM3: characterization of glutamate substitution mutants at the haem site of RT P450 BM3."; RL Biochem. J. 427:455-466(2010). RN [27] {ECO:0007744|PDB:3M4V} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-482 OF MUTANT PRO-331 IN COMPLEX RP WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL RP PROPERTIES, REDOX POTENTIOMETRY OF HEME, BIOTECHNOLOGY, AND MUTAGENESIS OF RP ALA-331. RX PubMed=21110374; DOI=10.1002/cbic.201000421; RA Whitehouse C.J., Yang W., Yorke J.A., Rowlatt B.C., Strong A.J., RA Blanford C.F., Bell S.G., Bartlam M., Wong L.L., Rao Z.; RT "Structural basis for the properties of two single-site proline mutants of RT CYP102A1 (P450BM3)."; RL ChemBioChem 11:2549-2556(2010). RN [28] {ECO:0007744|PDB:3NPL} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-464 OF MUTANT RP ALA-63/CYS-98/CYS-157 IN COMPLEX WITH HEME, AND REACTION MECHANISM. RX PubMed=20947800; DOI=10.1073/pnas.1012381107; RA Ener M.E., Lee Y.T., Winkler J.R., Gray H.B., Cheruzel L.; RT "Photooxidation of cytochrome P450-BM3."; RL Proc. Natl. Acad. Sci. U.S.A. 107:18783-18786(2010). RN [29] {ECO:0007744|PDB:1ZO4, ECO:0007744|PDB:1ZOA} RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-471 IN COMPLEXES WITH HEME AND RP N-PALMITOYLGLYCINE, FUNCTION, CATALYTIC ACTIVITY, ENZYME KINETICS, AND RP MUTAGENESIS OF ALA-329. RX PubMed=21875028; DOI=10.1021/bi201099j; RA Haines D.C., Hegde A., Chen B., Zhao W., Bondlela M., Humphreys J.M., RA Mullin D.A., Tomchick D.R., Machius M., Peterson J.A.; RT "A single active-site mutation of P450BM-3 dramatically enhances substrate RT binding and rate of product formation."; RL Biochemistry 50:8333-8341(2011). CC -!- FUNCTION: Functions as a fatty acid monooxygenase (PubMed:3106359, CC PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, CC PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, CC PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, CC PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). CC Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 CC positions (PubMed:1727637, PubMed:21875028). Shows activity toward CC medium and long-chain fatty acids, with optimum chain lengths of 12, 14 CC and 16 carbons (lauric, myristic, and palmitic acids). Able to CC metabolize some of these primary metabolites to secondary and tertiary CC products (PubMed:1727637). Marginal activity towards short chain CC lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates CC highly branched fatty acids, which play an essential role in membrane CC fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent CC reductase activity in the C-terminal domain, which allows electron CC transfer from NADPH to the heme iron of the cytochrome P450 N-terminal CC domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, CC PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, CC PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, CC PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, CC PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum CC sensing signals of other competing bacteria by oxidazing efficiently CC acyl homoserine lactones (AHLs), molecules involved in quorum sensing CC signaling pathways, and their lactonolysis products acyl homoserines CC (AHs) (PubMed:18020460). {ECO:0000269|PubMed:11695892, CC ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573, CC ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084, CC ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686, CC ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460, CC ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, CC ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, CC ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374, CC ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359, CC ECO:0000269|PubMed:7578081}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA- CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:11695889, CC ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735, CC ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:16566047, CC ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:1727637, CC ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, CC ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:18298086, CC ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129, CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, CC ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, CC ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:142491; EC=1.14.14.1; CC Evidence={ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, CC ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573, CC ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084, CC ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686, CC ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460, CC ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, CC ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, CC ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374, CC ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359, CC ECO:0000269|PubMed:7578081}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:7578081}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:10051560}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:18721129, CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, CC ECO:0000269|PubMed:21110374}; CC -!- ACTIVITY REGULATION: Inhibited by N-(12-imidazolyl-dodecanoyl)-L- CC leucine. {ECO:0000269|PubMed:18298086}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=250 uM for lauric acid at pH 7.4 at room temperature CC {ECO:0000269|PubMed:18020460}; CC KM=34 uM for N-beta-oxolauroyl-DL-homoserine lactone CC {ECO:0000269|PubMed:18020460}; CC KM=210 uM for N-beta-oxolauroyl-DL-homoserine CC {ECO:0000269|PubMed:18020460}; CC KM=140 uM for N-lauroyl-DL-homoserine {ECO:0000269|PubMed:18020460}; CC KM=322 uM for lauric acid at pH 7.5 and 15 degrees Celsius CC {ECO:0000269|PubMed:16403573}; CC KM=265 uM for lauric acid {ECO:0000269|PubMed:17868686}; CC KM=16 mM for indole {ECO:0000269|PubMed:17868686}; CC KM=87.4 uM for laurate/dodecanoate at pH 7.0 and 25 degrees Celsius CC {ECO:0000269|PubMed:18721129}; CC KM=230 uM for lauric acid at pH 7.4 {ECO:0000269|PubMed:19492389}; CC KM=87.4 uM for laurate/dodecanoate at 25 degrees Celsius CC {ECO:0000269|PubMed:20180779}; CC KM=5.1 uM for arachidonate at 25 degrees Celsius CC {ECO:0000269|PubMed:20180779}; CC KM=42.4 uM for palmitic acid at pH 7.4 and 30 degrees Celsius CC {ECO:0000269|PubMed:21110374}; CC Note=kcat is 84.1 sec(-1) for lauric acid (PubMed:16403573). kcat is CC 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for CC N-palmitoylglycine. kcat is 1690 min(-1) for CC N-palmitoyl-L-methionine. kcat is 610 min(-1) for CC N-palmitoyl-L-glutamine. kcat is 485 min(-1) for CC N-palmitoyl-L-glutamic acid. kcat is 1160 min(-1) for CC N-palmitoyl-L-leucine (PubMed:18004886). kcat is 28 sec(-1) for CC lauric acid (PubMed:17868686). kcat is 2770 min(-1) for CC laurate/dodecanoate (PubMed:18721129). kcat is 77 for lauric acid CC (PubMed:19492389). kcat is 2770 min(-1) for laurate/dodecanoate CC (PubMed:20180779). kcat is 16400 min(-1) for arachidonate CC (PubMed:20180779). kcat is 91.4 for palmitic acid (PubMed:21110374). CC {ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:17868686, CC ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18721129, CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, CC ECO:0000269|PubMed:21110374}; CC -!- INTERACTION: CC P14779; P14779: cyp102A1; NbExp=2; IntAct=EBI-7701704, EBI-7701704; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- INDUCTION: By pentobarbital (PubMed:1544926, PubMed:3106359). CC Expression is negatively regulated by repressor bm3R1 at the CC transcriptional level (PubMed:1544926). {ECO:0000269|PubMed:1544926, CC ECO:0000269|PubMed:3106359}. CC -!- BIOTECHNOLOGY: This protein is a target of protein engineering. Its CC selectivity-directing and activity-enhancing mutations have been CC extensively studied and the designed mutations allow this enzyme to act CC on non-native substrates and/or in order to enhance production of CC synthetically desirable end-products. {ECO:0000269|PubMed:18619466, CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:21110374, ECO:0000305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450 CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04832; AAA87602.1; -; Genomic_DNA. DR EMBL; CP009920; AJI21949.1; -; Genomic_DNA. DR EMBL; S87512; AAK19020.1; -; Genomic_DNA. DR PIR; A34286; A34286. DR RefSeq; WP_034650526.1; NZ_CP035094.1. DR PDB; 1BU7; X-ray; 1.65 A; A/B=2-456. DR PDB; 1BVY; X-ray; 2.03 A; A/B=2-459, F=460-650. DR PDB; 1FAG; X-ray; 2.70 A; A/B/C/D=2-472. DR PDB; 1FAH; X-ray; 2.30 A; A/B=2-472. DR PDB; 1JME; X-ray; 2.00 A; A/B=2-456. DR PDB; 1JPZ; X-ray; 1.65 A; A/B=2-471. DR PDB; 1P0V; X-ray; 2.05 A; A/B=2-456. DR PDB; 1P0W; X-ray; 2.00 A; A/B=2-456. DR PDB; 1P0X; X-ray; 2.00 A; A/B=2-456. DR PDB; 1SMI; X-ray; 2.00 A; A/B=2-472. DR PDB; 1SMJ; X-ray; 2.75 A; A/B/C/D=2-472. DR PDB; 1YQO; X-ray; 1.90 A; A/B=2-456. DR PDB; 1YQP; X-ray; 1.80 A; A/B=2-456. DR PDB; 1ZO4; X-ray; 1.46 A; A/B=2-471. DR PDB; 1ZO9; X-ray; 1.70 A; A/B=2-471. DR PDB; 1ZOA; X-ray; 1.74 A; A/B=2-471. DR PDB; 2BMH; X-ray; 2.00 A; A/B=2-456. DR PDB; 2HPD; X-ray; 2.00 A; A/B=2-472. DR PDB; 2IJ2; X-ray; 1.20 A; A/B=2-471. DR PDB; 2IJ3; X-ray; 1.90 A; A/B=2-471. DR PDB; 2IJ4; X-ray; 2.40 A; A/B=2-471. DR PDB; 2J1M; X-ray; 1.70 A; A/B=2-456. DR PDB; 2J4S; X-ray; 2.10 A; A/B=2-456. DR PDB; 2NNB; X-ray; 1.90 A; A/B=2-472. DR PDB; 2UWH; X-ray; 2.80 A; A/B/C/D/E/F=2-459. DR PDB; 2X7Y; X-ray; 2.10 A; A/B=2-456. DR PDB; 2X80; X-ray; 2.30 A; A/B=2-456. DR PDB; 3BEN; X-ray; 1.65 A; A/B=1-470. DR PDB; 3CBD; X-ray; 2.65 A; A/B=2-456. DR PDB; 3DGI; X-ray; 1.95 A; A/B=2-456. DR PDB; 3EKB; X-ray; 2.30 A; A/B=2-471. DR PDB; 3EKD; X-ray; 2.50 A; A/B=2-471. DR PDB; 3EKF; X-ray; 2.10 A; A/B=2-471. DR PDB; 3HF2; X-ray; 2.20 A; A/B=1-482. DR PDB; 3KX3; X-ray; 1.80 A; A/B=2-471. DR PDB; 3KX4; X-ray; 1.95 A; A/B=2-471. DR PDB; 3KX5; X-ray; 1.69 A; A/B=2-471. DR PDB; 3M4V; X-ray; 1.90 A; A/B=1-482. DR PDB; 3NPL; X-ray; 2.40 A; A/B=1-464. DR PDB; 3PSX; X-ray; 1.90 A; A/B=1-482. DR PDB; 3WSP; X-ray; 1.80 A; A/B=1-456. DR PDB; 4DQK; X-ray; 2.40 A; A/B=659-1049. DR PDB; 4DQL; X-ray; 2.15 A; A/B=657-1049. DR PDB; 4DTW; X-ray; 1.80 A; A/B=2-464. DR PDB; 4DTY; X-ray; 1.45 A; A/B=2-464. DR PDB; 4DTZ; X-ray; 1.55 A; A/B=2-464. DR PDB; 4DU2; X-ray; 1.90 A; A/B=1-464. DR PDB; 4DUA; X-ray; 2.00 A; A/B=2-464. DR PDB; 4DUB; X-ray; 1.70 A; A/B=1-464. DR PDB; 4DUC; X-ray; 1.92 A; A/B=1-464. DR PDB; 4DUD; X-ray; 1.85 A; A/B=2-464. DR PDB; 4DUE; X-ray; 1.70 A; A/B=2-464. DR PDB; 4DUF; X-ray; 1.80 A; A/B/C/D=2-464. DR PDB; 4H23; X-ray; 3.30 A; A/B=1-464. DR PDB; 4H24; X-ray; 2.50 A; A/B/C/D=1-464. DR PDB; 4HGF; X-ray; 1.70 A; A/B=2-456. DR PDB; 4HGG; X-ray; 1.70 A; A/B=2-456. DR PDB; 4HGH; X-ray; 1.40 A; A/B=2-456. DR PDB; 4HGI; X-ray; 1.50 A; A/B=2-456. DR PDB; 4HGJ; X-ray; 1.90 A; A/B=2-456. DR PDB; 4KEW; X-ray; 1.89 A; A/B=2-456. DR PDB; 4KEY; X-ray; 2.05 A; A/B=2-456. DR PDB; 4KF0; X-ray; 1.45 A; A/B=2-458. DR PDB; 4KF2; X-ray; 1.82 A; A/B=2-458. DR PDB; 4KPA; X-ray; 2.00 A; A=1-471. DR PDB; 4KPB; X-ray; 2.10 A; A/B=1-471. DR PDB; 4O4P; X-ray; 1.83 A; A/B=2-456. DR PDB; 4RSN; X-ray; 2.70 A; A/B=1-456. DR PDB; 4WG2; X-ray; 2.66 A; A/B/C=2-464. DR PDB; 4ZF6; X-ray; 2.77 A; A=1-461. DR PDB; 4ZF8; X-ray; 2.77 A; A=1-461. DR PDB; 4ZFA; X-ray; 2.77 A; A=1-461. DR PDB; 4ZFB; X-ray; 2.84 A; A=1-461. DR PDB; 5B2U; X-ray; 1.90 A; A/B=1-456. DR PDB; 5B2V; X-ray; 2.30 A; A/B=1-456. DR PDB; 5B2W; X-ray; 1.65 A; A/B=1-456. DR PDB; 5B2X; X-ray; 1.90 A; A/B=1-456. DR PDB; 5B2Y; X-ray; 2.01 A; A/B=1-456. DR PDB; 5DYP; X-ray; 2.40 A; A/C=2-471. DR PDB; 5DYZ; X-ray; 1.97 A; A/C=2-471. DR PDB; 5E78; X-ray; 2.00 A; A/B=2-456. DR PDB; 5E7Y; X-ray; 2.00 A; A/B=2-472. DR PDB; 5E9Z; X-ray; 2.23 A; A/B/C/D=1-468. DR PDB; 5JQ2; X-ray; 2.00 A; A/B=2-464. DR PDB; 5JQU; X-ray; 2.16 A; A/B/C/D/E/F/G/H=2-464. DR PDB; 5JQV; X-ray; 2.34 A; A/B/C/D/E/F/G/H=2-464. DR PDB; 5JTD; X-ray; 1.50 A; A/B=2-464. DR PDB; 5OG9; X-ray; 2.09 A; A/B=2-474. DR PDB; 5UCW; X-ray; 1.70 A; A/B=1-464. DR PDB; 5XA3; X-ray; 2.20 A; A/B/C/D=1-456. DR PDB; 5XHJ; X-ray; 2.00 A; A/B=1-456. DR PDB; 5ZIS; X-ray; 3.10 A; A/B/C/D=2-456. DR PDB; 5ZLH; X-ray; 3.40 A; A/B/C/D=2-456. DR PDB; 6H1O; X-ray; 1.73 A; A/B=2-458. DR PDB; 6H1S; X-ray; 1.95 A; A/B=2-458. DR PDB; 6HN8; X-ray; 2.00 A; A/B=1-456. DR PDB; 6IAO; X-ray; 2.16 A; A/B/C/D=1-473. DR PDB; 6JLV; X-ray; 1.22 A; A/B=1-456. DR PDB; 6JMH; X-ray; 1.46 A; A/B=1-456. DR PDB; 6JMW; X-ray; 1.85 A; A/B=1-457. DR PDB; 6JO1; X-ray; 2.10 A; A/B=1-456. DR PDB; 6JS8; X-ray; 1.36 A; A/B=1-456. DR PDB; 6JVC; X-ray; 1.75 A; A/C=1-456. DR PDB; 6JZS; X-ray; 1.68 A; A/C=1-457. DR PDB; 6K24; X-ray; 2.10 A; A/B=2-457. DR PDB; 6K3Q; X-ray; 2.06 A; A/B=1-456. DR PDB; 6K58; X-ray; 1.41 A; A/B=1-456. DR PDB; 6K9S; X-ray; 1.55 A; A/B=1-456. DR PDB; 6L1A; X-ray; 1.84 A; A/B=1-456. DR PDB; 6L1B; X-ray; 1.74 A; A/B=1-456. DR PDB; 6LY4; X-ray; 1.68 A; A=3-457. DR PDB; 7CKN; X-ray; 1.55 A; A/B=1-456. DR PDB; 7CON; X-ray; 1.46 A; A/B=1-456. DR PDB; 7COO; X-ray; 1.49 A; A/B=1-456. DR PDB; 7CP8; X-ray; 1.68 A; A/B=1-456. DR PDB; 7CVR; X-ray; 1.60 A; A/B=1-456. DR PDB; 7CX6; X-ray; 1.69 A; A/B=1-456. DR PDB; 7CX8; X-ray; 1.70 A; A/B=1-456. DR PDB; 7CZI; X-ray; 1.64 A; A/B=1-456. DR PDB; 7D0T; X-ray; 1.74 A; A/B=1-456. DR PDB; 7D0U; X-ray; 1.68 A; A/B=1-456. DR PDB; 7D1F; X-ray; 1.45 A; A/B=1-456. DR PDB; 7E46; X-ray; 1.91 A; A/B=1-456. DR PDB; 7EGN; X-ray; 2.70 A; A/B=1-456. DR PDB; 7W97; X-ray; 1.40 A; A/B=1-456. DR PDB; 7W9D; X-ray; 1.55 A; A/B=1-456. DR PDB; 7W9J; X-ray; 1.75 A; A/B=1-456. DR PDB; 7WDD; X-ray; 2.21 A; A/B=1-456. DR PDB; 7WDE; X-ray; 2.11 A; A/B=1-456. DR PDB; 7WDG; X-ray; 2.07 A; A/B=1-456. DR PDB; 7WDH; X-ray; 1.68 A; A/B=1-456. DR PDB; 7WDI; X-ray; 2.10 A; A/B=1-456. DR PDB; 7WG0; X-ray; 2.20 A; A/B=1-457. DR PDB; 7WY1; X-ray; 1.60 A; A/B=1-456. DR PDB; 7WY2; X-ray; 1.45 A; A/B=1-456. DR PDB; 7WY3; X-ray; 1.60 A; A/B=1-456. DR PDB; 7WY4; X-ray; 1.45 A; A/B=1-456. DR PDB; 7XZK; X-ray; 1.54 A; A/B=1-456. DR PDB; 7Y0P; X-ray; 1.99 A; A/B=1-456. DR PDB; 7Y0Q; X-ray; 2.31 A; A/B=1-456. DR PDB; 7Y0R; X-ray; 2.09 A; A/B=1-456. DR PDB; 7Y0S; X-ray; 2.06 A; A/B=1-456. DR PDB; 7Y0T; X-ray; 1.89 A; A/B=1-456. DR PDB; 7Y0U; X-ray; 2.00 A; A/B=1-456. DR PDB; 7Y9J; X-ray; 1.83 A; A/B=3-465. DR PDB; 7Y9K; X-ray; 2.23 A; A/B=3-465. DR PDB; 7Y9L; X-ray; 1.76 A; A/B=3-458. DR PDB; 7Y9M; X-ray; 2.16 A; A/B=3-458. DR PDB; 7YD9; X-ray; 1.75 A; A/B=1-456. DR PDB; 7YDA; X-ray; 1.56 A; A/B=1-456. DR PDB; 7YDB; X-ray; 1.47 A; A/B=1-456. DR PDB; 7YDC; X-ray; 1.61 A; A/B=1-456. DR PDB; 7YDD; X-ray; 1.66 A; A/B=1-456. DR PDB; 7YDE; X-ray; 1.79 A; A/B=1-456. DR PDB; 7YDL; X-ray; 1.58 A; A/B=1-456. DR PDB; 7YFT; X-ray; 2.00 A; A/B=1-456. DR PDB; 7YJD; X-ray; 1.90 A; A/B=1-456. DR PDB; 7YJE; X-ray; 1.85 A; A/B=1-456. DR PDB; 7YJF; X-ray; 1.51 A; A/B=1-456. DR PDB; 7YJG; X-ray; 1.68 A; A/B=1-456. DR PDB; 7YJH; X-ray; 1.79 A; A/B=1-456. DR PDB; 8DME; EM; 6.50 A; A/B=4-1049. DR PDB; 8DMG; EM; 4.40 A; A/B=1-1049. DR PDB; 8DSG; X-ray; 1.87 A; A/B/C/D=1-464. DR PDBsum; 1BU7; -. DR PDBsum; 1BVY; -. DR PDBsum; 1FAG; -. DR PDBsum; 1FAH; -. DR PDBsum; 1JME; -. DR PDBsum; 1JPZ; -. DR PDBsum; 1P0V; -. DR PDBsum; 1P0W; -. DR PDBsum; 1P0X; -. DR PDBsum; 1SMI; -. DR PDBsum; 1SMJ; -. DR PDBsum; 1YQO; -. DR PDBsum; 1YQP; -. DR PDBsum; 1ZO4; -. DR PDBsum; 1ZO9; -. DR PDBsum; 1ZOA; -. DR PDBsum; 2BMH; -. DR PDBsum; 2HPD; -. DR PDBsum; 2IJ2; -. DR PDBsum; 2IJ3; -. DR PDBsum; 2IJ4; -. DR PDBsum; 2J1M; -. DR PDBsum; 2J4S; -. DR PDBsum; 2NNB; -. DR PDBsum; 2UWH; -. DR PDBsum; 2X7Y; -. DR PDBsum; 2X80; -. DR PDBsum; 3BEN; -. DR PDBsum; 3CBD; -. DR PDBsum; 3DGI; -. DR PDBsum; 3EKB; -. DR PDBsum; 3EKD; -. DR PDBsum; 3EKF; -. DR PDBsum; 3HF2; -. DR PDBsum; 3KX3; -. DR PDBsum; 3KX4; -. DR PDBsum; 3KX5; -. DR PDBsum; 3M4V; -. DR PDBsum; 3NPL; -. DR PDBsum; 3PSX; -. DR PDBsum; 3WSP; -. DR PDBsum; 4DQK; -. DR PDBsum; 4DQL; -. DR PDBsum; 4DTW; -. DR PDBsum; 4DTY; -. DR PDBsum; 4DTZ; -. DR PDBsum; 4DU2; -. DR PDBsum; 4DUA; -. DR PDBsum; 4DUB; -. DR PDBsum; 4DUC; -. DR PDBsum; 4DUD; -. DR PDBsum; 4DUE; -. DR PDBsum; 4DUF; -. DR PDBsum; 4H23; -. DR PDBsum; 4H24; -. DR PDBsum; 4HGF; -. DR PDBsum; 4HGG; -. DR PDBsum; 4HGH; -. DR PDBsum; 4HGI; -. DR PDBsum; 4HGJ; -. DR PDBsum; 4KEW; -. DR PDBsum; 4KEY; -. DR PDBsum; 4KF0; -. DR PDBsum; 4KF2; -. DR PDBsum; 4KPA; -. DR PDBsum; 4KPB; -. DR PDBsum; 4O4P; -. DR PDBsum; 4RSN; -. DR PDBsum; 4WG2; -. DR PDBsum; 4ZF6; -. DR PDBsum; 4ZF8; -. DR PDBsum; 4ZFA; -. DR PDBsum; 4ZFB; -. DR PDBsum; 5B2U; -. DR PDBsum; 5B2V; -. DR PDBsum; 5B2W; -. DR PDBsum; 5B2X; -. DR PDBsum; 5B2Y; -. DR PDBsum; 5DYP; -. DR PDBsum; 5DYZ; -. DR PDBsum; 5E78; -. DR PDBsum; 5E7Y; -. DR PDBsum; 5E9Z; -. DR PDBsum; 5JQ2; -. DR PDBsum; 5JQU; -. DR PDBsum; 5JQV; -. DR PDBsum; 5JTD; -. DR PDBsum; 5OG9; -. DR PDBsum; 5UCW; -. DR PDBsum; 5XA3; -. DR PDBsum; 5XHJ; -. DR PDBsum; 5ZIS; -. DR PDBsum; 5ZLH; -. DR PDBsum; 6H1O; -. DR PDBsum; 6H1S; -. DR PDBsum; 6HN8; -. DR PDBsum; 6IAO; -. DR PDBsum; 6JLV; -. DR PDBsum; 6JMH; -. DR PDBsum; 6JMW; -. DR PDBsum; 6JO1; -. DR PDBsum; 6JS8; -. DR PDBsum; 6JVC; -. DR PDBsum; 6JZS; -. DR PDBsum; 6K24; -. DR PDBsum; 6K3Q; -. DR PDBsum; 6K58; -. DR PDBsum; 6K9S; -. DR PDBsum; 6L1A; -. DR PDBsum; 6L1B; -. DR PDBsum; 6LY4; -. DR PDBsum; 7CKN; -. DR PDBsum; 7CON; -. DR PDBsum; 7COO; -. DR PDBsum; 7CP8; -. DR PDBsum; 7CVR; -. DR PDBsum; 7CX6; -. DR PDBsum; 7CX8; -. DR PDBsum; 7CZI; -. DR PDBsum; 7D0T; -. DR PDBsum; 7D0U; -. DR PDBsum; 7D1F; -. DR PDBsum; 7E46; -. DR PDBsum; 7EGN; -. DR PDBsum; 7W97; -. DR PDBsum; 7W9D; -. DR PDBsum; 7W9J; -. DR PDBsum; 7WDD; -. DR PDBsum; 7WDE; -. DR PDBsum; 7WDG; -. DR PDBsum; 7WDH; -. DR PDBsum; 7WDI; -. DR PDBsum; 7WG0; -. DR PDBsum; 7WY1; -. DR PDBsum; 7WY2; -. DR PDBsum; 7WY3; -. DR PDBsum; 7WY4; -. DR PDBsum; 7XZK; -. DR PDBsum; 7Y0P; -. DR PDBsum; 7Y0Q; -. DR PDBsum; 7Y0R; -. DR PDBsum; 7Y0S; -. DR PDBsum; 7Y0T; -. DR PDBsum; 7Y0U; -. DR PDBsum; 7Y9J; -. DR PDBsum; 7Y9K; -. DR PDBsum; 7Y9L; -. DR PDBsum; 7Y9M; -. DR PDBsum; 7YD9; -. DR PDBsum; 7YDA; -. DR PDBsum; 7YDB; -. DR PDBsum; 7YDC; -. DR PDBsum; 7YDD; -. DR PDBsum; 7YDE; -. DR PDBsum; 7YDL; -. DR PDBsum; 7YFT; -. DR PDBsum; 7YJD; -. DR PDBsum; 7YJE; -. DR PDBsum; 7YJF; -. DR PDBsum; 7YJG; -. DR PDBsum; 7YJH; -. DR PDBsum; 8DME; -. DR PDBsum; 8DMG; -. DR PDBsum; 8DSG; -. DR AlphaFoldDB; P14779; -. DR EMDB; EMD-27534; -. DR EMDB; EMD-27536; -. DR SMR; P14779; -. DR MINT; P14779; -. DR BindingDB; P14779; -. DR ChEMBL; CHEMBL4630872; -. DR DrugBank; DB08086; N-[12-(1H-imidazol-1-yl)dodecanoyl]-L-leucine. DR DrugBank; DB03440; N-hexadecanoylglycine. DR DrugBank; DB04257; Palmitoleic Acid. DR KEGG; bmeg:BG04_163; -. DR HOGENOM; CLU_001570_7_0_9; -. DR BioCyc; MetaCyc:MONOMER-17698; -. DR BRENDA; 1.1.1.B57; 656. DR BRENDA; 1.14.14.1; 656. DR BRENDA; 1.6.2.4; 656. DR SABIO-RK; P14779; -. DR EvolutionaryTrace; P14779; -. DR Proteomes; UP000031829; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IDA:UniProtKB. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR CDD; cd06206; bifunctional_CYPOR; 1. DR CDD; cd11068; CYP120A1; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR023206; Bifunctional_P450_P450_red. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR036396; Cyt_P450_sf. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Electron transport; FAD; Flavoprotein; FMN; Heme; KW Iron; Metal-binding; Monooxygenase; Multifunctional enzyme; NADP; KW Oxidoreductase; Transport. FT CHAIN 1..1049 FT /note="Bifunctional cytochrome P450/NADPH--P450 reductase" FT /id="PRO_0000052205" FT DOMAIN 483..622 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088" FT DOMAIN 660..892 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 2..472 FT /note="Cytochrome P450" FT REGION 473..1049 FT /note="NADPH--P450 reductase" FT BINDING 52 FT /ligand="(9Z)-hexadecenoate" FT /ligand_id="ChEBI:CHEBI:32372" FT /evidence="ECO:0000269|PubMed:15020590, FT ECO:0007744|PDB:1SMJ" FT BINDING 401 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:10051560, FT ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, FT ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:15020590, FT ECO:0000269|PubMed:15299332, ECO:0000269|PubMed:16403573, FT ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:17429965, FT ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, FT ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, FT ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, FT ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:20947800, FT ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, FT ECO:0000269|PubMed:7578081, ECO:0000269|PubMed:8342039, FT ECO:0000269|PubMed:9033595, ECO:0007744|PDB:1BU7, FT ECO:0007744|PDB:1BVY, ECO:0007744|PDB:1FAG, FT ECO:0007744|PDB:1FAH, ECO:0007744|PDB:1JME, FT ECO:0007744|PDB:1JPZ, ECO:0007744|PDB:1P0V, FT ECO:0007744|PDB:1P0W, ECO:0007744|PDB:1P0X, FT ECO:0007744|PDB:1SMI, ECO:0007744|PDB:1SMJ, FT ECO:0007744|PDB:1YQO, ECO:0007744|PDB:1YQP, FT ECO:0007744|PDB:1ZO4, ECO:0007744|PDB:1ZO9, FT ECO:0007744|PDB:1ZOA, ECO:0007744|PDB:2BMH, FT ECO:0007744|PDB:2HPD, ECO:0007744|PDB:2IJ2, FT ECO:0007744|PDB:2IJ3, ECO:0007744|PDB:2IJ4, FT ECO:0007744|PDB:2J1M, ECO:0007744|PDB:2J4S, FT ECO:0007744|PDB:2UWH, ECO:0007744|PDB:3BEN, FT ECO:0007744|PDB:3CBD, ECO:0007744|PDB:3EKB, FT ECO:0007744|PDB:3EKD, ECO:0007744|PDB:3EKF, FT ECO:0007744|PDB:3HF2, ECO:0007744|PDB:3KX3, FT ECO:0007744|PDB:3KX4, ECO:0007744|PDB:3KX5, FT ECO:0007744|PDB:3M4V, ECO:0007744|PDB:3NPL" FT BINDING 489..494 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:10051560, FT ECO:0007744|PDB:1BVY" FT BINDING 536..539 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:10051560, FT ECO:0007744|PDB:1BVY" FT BINDING 570..572 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:10051560, FT ECO:0007744|PDB:1BVY" FT BINDING 578..580 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:10051560, FT ECO:0007744|PDB:1BVY" FT SITE 269 FT /note="Important for catalytic activity" FT /evidence="ECO:0000305|PubMed:16403573, FT ECO:0000305|PubMed:7578081" FT MUTAGEN 48 FT /note="R->Q,S: 2-3-fold decrease in binding affinity for FT N-myristoyl-L-methionine as substrate." FT /evidence="ECO:0000269|PubMed:18004886" FT MUTAGEN 75 FT /note="A->G: Higher activity in the hydroxylation of highly FT branched fatty acids; when associated with V-88 and Q-189." FT /evidence="ECO:0000269|PubMed:16566047" FT MUTAGEN 83 FT /note="A->F: 800-fold binding affinity for laurate as FT substrate. High coupling of NADPH consumption to laurate FT formation. Very much more effective in indole FT hydroxylation. Favors omega-2 hydroxylation. Significantly FT higher rates of NADPH consumption in the absence of FT substrate. No temperature-dependent shifts to low-spin in FT complex with palmitate." FT /evidence="ECO:0000269|PubMed:17868686" FT MUTAGEN 83 FT /note="A->I: No effect in binding affinity for laurate as FT substrate. High coupling of NADPH consumption to laurate FT formation. No indole hydroxylation. Favors omega-2 FT hydroxylation. Similarly to wild-type, shows significant FT shifts to low-spin in complex with palmitate as the FT temperature decreases." FT /evidence="ECO:0000269|PubMed:17868686" FT MUTAGEN 83 FT /note="A->W: 800-fold binding affinity for laurate as FT substrate. Low coupling of NADPH consumption to laurate FT formation. Very much more effective in indole FT hydroxylation. Favors omega-1 hydroxylation. Significantly FT higher rates of NADPH consumption in the absence of FT substrate. No temperature-dependent shifts to low-spin in FT complex with palmitate." FT /evidence="ECO:0000269|PubMed:17868686" FT MUTAGEN 87 FT /note="L->E: Ineffective covalent modification of the heme FT macrocycle. Extensive formation of Fe(II)CO complex in the FT substrate-free form. Has more positive potential in both FT substrate-free and arachidonate-bound forms and some FT high-spin content in the ferric substrate-free form of the FT enzyme." FT /evidence="ECO:0000269|PubMed:20180779" FT MUTAGEN 88 FT /note="F->V: Higher activity in the hydroxylation of highly FT branched fatty acids; when associated with G-75 and Q-189." FT /evidence="ECO:0000269|PubMed:16566047" FT MUTAGEN 189 FT /note="L->Q: Higher activity in the hydroxylation of highly FT branched fatty acids; when associated with G-75 and V-88." FT /evidence="ECO:0000269|PubMed:16566047" FT MUTAGEN 262 FT /note="F->E: Ineffective covalent modification of the heme FT macrocycle. Substantially slower FMN to heme electron FT transfer for the arachidonate-bound enzyme. Product FT distribution biased towards omega-3." FT /evidence="ECO:0000269|PubMed:20180779" FT MUTAGEN 265 FT /note="A->C: No effective fatty acid oxidation. No effect FT on electron transport from NADPH to FMN. Substantially FT lower high-spin conversion with arachidonate and FT palmitoleate, and negligible change is observed with FT palmitate, myristate and laurate/dodecanoate. 20% of FT omega-1, omega-2 and omega-3 laurate/dodecanoate FT hydroxylation products." FT /evidence="ECO:0000269|PubMed:18721129" FT MUTAGEN 265 FT /note="A->H,K: No significant stimulation of NADPH FT oxidation induced by addition of fatty acids and no FT hydroxylated products, but cytochrome c reductase activity FT levels are identical to wild-type enzyme. More negative FT reduction potential with dithionite. Unable to form FT Fe(2+)CO complexes on reduction with dithionite and FT bubbling with carbon monoxide." FT /evidence="ECO:0000269|PubMed:17077084" FT MUTAGEN 265 FT /note="A->M: No effective fatty acid oxidation. No effect FT on electron transport from NADPH to FMN. Slightly lower FT high-spin conversion with arachidonate, palmitoleate, FT palmitate, myristate and laurate/dodecanoate. 5% of FT omega-1, omega-2 and omega-3 laurate/dodecanoate FT hydroxylation products." FT /evidence="ECO:0000269|PubMed:18721129" FT MUTAGEN 265 FT /note="A->Q: No effective fatty acid oxidation. No effect FT on electron transport from NADPH to FMN. Nearly wild-type FT level of high-spin conversion with laurate/dodecanoate, FT palmitoleate and arachidonate. 5% of omega-1, omega-2 and FT omega-3 laurate/dodecanoate hydroxylation products." FT /evidence="ECO:0000269|PubMed:18721129" FT MUTAGEN 269 FT /note="T->A: Contrary to wild-type, significant decrease in FT the formation of the high-spin complex via substrate FT binding, and decreased substrate-induced reduction FT potential shift with saturating concentrations of FT arachidonate; when associated with H-394. Considerably FT lower proportion of high-spin protein and decreased FT substrate-induced heme reduction-potential shift on FT addition of saturating concentrations of arachidonate. FT Leads to destabilization of the oxy-ferrous complex. FT Exhibits slower rates of O(2) and NADPH consumption using FT sodium laurate as the substrate. Greater production of FT water and peroxide compared to wild-type indicating FT uncoupled electron transfer from sodium laurate FT hydroxylation. Only 16% yield of product after 5 min of FT reaction relative to the amount of NADPH used compared to FT 100% of wild-type." FT /evidence="ECO:0000269|PubMed:16403573, FT ECO:0000269|PubMed:7578081" FT MUTAGEN 269 FT /note="T->N: High substrate-free turnover rate constant. FT Negligible substrate-induced spin-state and FT substrate-induced heme reduction-potential shifts on FT addition of saturating concentrations of arachidonate. FT Induces a positive shift in the substrate-free heme FT reduction potential. 10-fold greater rate constants for the FT first electron transfer in the absence of substrate; when FT associated with H-394. Turnover rate constants diminished. FT Significantly smaller degrees of coupling to product. FT Negligible amounts of high-spin protein on addition of FT saturating concentration of arachidonate. Negligible FT substrate-induced spin-state and substrate-induced heme FT reduction-potential shifts on addition of saturating FT concentrations of arachidonate. Induces a 60 mV positive FT shift in the substrate-free heme reduction potential. The FT apparent rate constant for heme reduction is smaller than FT the overall turnover rate constant. Leads to FT destabilization of the oxy-ferrous complex." FT /evidence="ECO:0000269|PubMed:16403573" FT MUTAGEN 329 FT /note="A->V: Substrate binding affinity increases 5-10 fold FT and the turnover number increases 2-8-fold for palmitate as FT substrate compared to the wild-type. Has a very different FT product distribution favoring greatly oxidation at the FT omega-1 position and shows almost no oxidation at the FT omega-3 position." FT /evidence="ECO:0000269|PubMed:21875028" FT MUTAGEN 331 FT /note="A->P: Enhanced activity with small non-natural FT substrates with altered product profiles compared to FT wild-type." FT /evidence="ECO:0000269|PubMed:21110374" FT MUTAGEN 394 FT /note="F->H: High substrate-free turnover rate constant. FT Negligible substrate-induced spin-state and FT substrate-induced heme reduction-potential shifts on FT addition of saturating concentrations of arachidonate. FT Induces a positive shift in the substrate-free heme FT reduction potential. 10-fold greater rate constants for the FT first electron transfer in the absence of substrate; when FT associated with N-269. Significant decrease in the FT formation of the high-spin complex via substrate binding, FT and decreased substrate-induced reduction potential shift FT with saturating concentrations of arachidonate; when FT associated with A-269. No change in product profile using FT myristate as substrate, but slightly higher amount of FT unreacted myristate indicating lower overall catalytic FT activity relative to wild-type." FT /evidence="ECO:0000269|PubMed:11695889, FT ECO:0000269|PubMed:16403573" FT MUTAGEN 394 FT /note="F->W: Large decrease in the heme reduction potential FT in the presence and absence of substrate arachidonate. 10% FT reduction in efficiency to couple NADPH consumption to FT substrate monooxygenation. Half of the turn over rate and FT four times faster decay of the oxy-ferrous complex to the FT ferric form than that of wild-type." FT /evidence="ECO:0000269|PubMed:14653735" FT MUTAGEN 402 FT /note="I->E: Ineffective covalent modification of the heme FT macrocycle. 2-fold apparent limiting rate of flavin to heme FT electron transfer for arachidonate-bound enzyme. FT Substrate-free enzyme is converted rapidly and completely FT into its Fe(II)CO complex and has much more positive FT potential. 8-fold decrease in overall catalytic rate with FT arachidonic acid. More efficient NADPH oxidase in absence FT of fatty acids. Product distribution biased towards FT omega-1." FT /evidence="ECO:0000269|PubMed:20180779" FT MUTAGEN 402 FT /note="I->P: 10-fold increase in binding affinity for FT lauric acid. Catalytic activity rates accelerate across a FT range of hydrophobic non-natural substrates, including FT (+)-alpha-pinene, fluorene, 3-methylpentane and FT propylbenzene, while product distributions of them are FT broadly similar to the wild-type enzyme exept for FT (+)-alpha-pinene which is not metabolized by wild-type." FT /evidence="ECO:0000269|PubMed:19492389" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:6K24" FT HELIX 26..37 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 39..45 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 56..62 FT /evidence="ECO:0007829|PDB:2IJ2" FT TURN 65..67 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 74..83 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:5JQU" FT HELIX 95..104 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:2IJ2" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 113..132 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 142..159 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:5JQV" FT HELIX 173..187 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:6JLV" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:4HGJ" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 200..227 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 234..240 FT /evidence="ECO:0007829|PDB:2IJ2" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 252..283 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 285..298 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 306..310 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 313..325 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 331..338 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:2IJ2" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 353..357 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 365..368 FT /evidence="ECO:0007829|PDB:2IJ2" FT TURN 370..373 FT /evidence="ECO:0007829|PDB:6JLV" FT HELIX 377..380 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:4ZFB" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 404..421 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 434..442 FT /evidence="ECO:0007829|PDB:2IJ2" FT STRAND 446..451 FT /evidence="ECO:0007829|PDB:2IJ2" FT HELIX 462..464 FT /evidence="ECO:0007829|PDB:4WG2" FT STRAND 483..488 FT /evidence="ECO:0007829|PDB:1BVY" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:1BVY" FT HELIX 493..506 FT /evidence="ECO:0007829|PDB:1BVY" FT TURN 507..509 FT /evidence="ECO:0007829|PDB:1BVY" FT STRAND 513..516 FT /evidence="ECO:0007829|PDB:1BVY" FT HELIX 517..519 FT /evidence="ECO:0007829|PDB:1BVY" FT STRAND 526..534 FT /evidence="ECO:0007829|PDB:1BVY" FT TURN 543..545 FT /evidence="ECO:0007829|PDB:1BVY" FT HELIX 546..553 FT /evidence="ECO:0007829|PDB:1BVY" FT STRAND 565..571 FT /evidence="ECO:0007829|PDB:1BVY" FT HELIX 576..578 FT /evidence="ECO:0007829|PDB:1BVY" FT HELIX 581..591 FT /evidence="ECO:0007829|PDB:1BVY" FT TURN 592..594 FT /evidence="ECO:0007829|PDB:1BVY" FT STRAND 599..605 FT /evidence="ECO:0007829|PDB:1BVY" FT HELIX 610..628 FT /evidence="ECO:0007829|PDB:1BVY" FT STRAND 663..672 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 682..688 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 700..703 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 709..719 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 726..729 FT /evidence="ECO:0007829|PDB:4DQK" FT STRAND 741..746 FT /evidence="ECO:0007829|PDB:4DQK" FT HELIX 747..750 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 751..753 FT /evidence="ECO:0007829|PDB:4DQK" FT STRAND 756..759 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 762..770 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 775..783 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 787..793 FT /evidence="ECO:0007829|PDB:4DQL" FT TURN 794..798 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 801..807 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 815..820 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 828..831 FT /evidence="ECO:0007829|PDB:4DQL" FT TURN 836..838 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 842..848 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 851..853 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 857..862 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 864..871 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 877..883 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 899..902 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 905..908 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 909..923 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 931..938 FT /evidence="ECO:0007829|PDB:4DQL" FT TURN 940..942 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 947..955 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 960..967 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 976..982 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 984..992 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 996..1002 FT /evidence="ECO:0007829|PDB:4DQL" FT TURN 1003..1005 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 1006..1022 FT /evidence="ECO:0007829|PDB:4DQL" FT HELIX 1026..1038 FT /evidence="ECO:0007829|PDB:4DQL" FT STRAND 1042..1047 FT /evidence="ECO:0007829|PDB:4DQL" SQ SEQUENCE 1049 AA; 117781 MW; B0BE61F8A2EE33D5 CRC64; MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT RYLSSQRLIK EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA HNILLPSFSQ QAMKGYHAMM VDIAVQLVQK WERLNADEHI EVPEDMTRLT LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR ALDEAMNKLQ RANPDDPAYD ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN GKDPETGEPL DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK GDELMVLIPQ LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA CIGQQFALHE ATLVLGMMLK HFDFEDHTNY ELDIKETLTL KPEGFVVKAK SKKIPLGGIP SPSTEQSAKK VRKKAENAHN TPLLVLYGSN MGTAEGTARD LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH PPDNAKQFVD WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS AADMPLAKMH GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH LGVIPRNYEG IVNRVTARFG LDASQQIRLE AEEEKLAHLP LAKTVSVEEL LQYVELQDPV TRTQLRAMAA KTVCPPHKVE LEALLEKQAY KEQVLAKRLT MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE KQASITVSVV SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL ENAQSEGIIT LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC GDGSQMAPAV EATLMKSYAD VHQVSEADAR LWLQQLEEKG RYAKDVWAG //