ID TETX_BACT4 Reviewed; 388 AA. AC Q93L51; DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Flavin-dependent monooxygenase {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000303|PubMed:15452119}; DE AltName: Full=TetX monooxygenase {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000303|PubMed:16128584}; DE Short=TetX {ECO:0000255|HAMAP-Rule:MF_00845}; DE EC=1.14.13.231 {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000269|PubMed:15452119}; DE AltName: Full=TetX2 {ECO:0000303|PubMed:21590745}; GN Name=tetX2 {ECO:0000303|PubMed:11472924}; OS Bacteroides thetaiotaomicron. OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=818; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BT5482A; TRANSPOSON=CTnDOT; RX PubMed=11472924; DOI=10.1128/aem.67.8.3488-3495.2001; RA Whittle G., Hund B.D., Shoemaker N.B., Salyers A.A.; RT "Characterization of the 13-kilobase ermF region of the Bacteroides RT conjugative transposon CTnDOT."; RL Appl. Environ. Microbiol. 67:3488-3495(2001). RN [2] RP FUNCTION IN INACTIVATING OXYTETRACYCLINE, CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ANTIBIOTIC RESISTANCE. RC STRAIN=BT5482A; TRANSPOSON=CTnDOT; RX PubMed=15452119; DOI=10.1074/jbc.m409573200; RA Yang W., Moore I.F., Koteva K.P., Bareich D.C., Hughes D.W., Wright G.D.; RT "TetX is a flavin-dependent monooxygenase conferring resistance to RT tetracycline antibiotics."; RL J. Biol. Chem. 279:52346-52352(2004). RN [3] RP FUNCTION IN INACTIVATING TIGECYCLINE, BIOPHYSICOCHEMICAL PROPERTIES, AND RP ANTIBIOTIC RESISTANCE. RC STRAIN=BT5482A; TRANSPOSON=CTnDOT; RX PubMed=16128584; DOI=10.1021/bi0506066; RA Moore I.F., Hughes D.W., Wright G.D.; RT "Tigecycline is modified by the flavin-dependent monooxygenase TetX."; RL Biochemistry 44:11829-11835(2005). RN [4] RP FUNCTION IN INACTIVATING TETRACYCLINE AND ANALOGS, AND ANTIBIOTIC RP RESISTANCE. RX PubMed=26097034; DOI=10.1016/j.chembiol.2015.05.017; RA Forsberg K.J., Patel S., Wencewicz T.A., Dantas G.; RT "The Tetracycline Destructases: A Novel Family of Tetracycline-Inactivating RT Enzymes."; RL Chem. Biol. 22:888-897(2015). RN [5] RP FUNCTION IN INACTIVATING CHLORTETRACYCLINE, AND ACTIVITY REGULATION. RX PubMed=28481346; DOI=10.1038/nchembio.2376; RA Park J., Gasparrini A.J., Reck M.R., Symister C.T., Elliott J.L., RA Vogel J.P., Wencewicz T.A., Dantas G., Tolia N.H.; RT "Plasticity, dynamics, and inhibition of emerging tetracycline resistance RT enzymes."; RL Nat. Chem. Biol. 13:730-736(2017). RN [6] {ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R} RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD WITH RP AND WITHOUT ANTIBIOTICS, COFACTOR, SUBUNIT, AND DOMAIN. RC STRAIN=BT5482A; TRANSPOSON=CTnDOT; RX PubMed=21402075; DOI=10.1016/j.febslet.2011.03.012; RA Volkers G., Palm G.J., Weiss M.S., Wright G.D., Hinrichs W.; RT "Structural basis for a new tetracycline resistance mechanism relying on RT the TetX monooxygenase."; RL FEBS Lett. 585:1061-1066(2011). RN [7] {ECO:0007744|PDB:3P9U} RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD, RP COFACTOR, SUBUNIT, AND DOMAIN. RX PubMed=21590745; DOI=10.1002/prot.23052; RA Walkiewicz K., Davlieva M., Wu G., Shamoo Y.; RT "Crystal structure of Bacteroides thetaiotaomicron TetX2: a tetracycline RT degrading monooxygenase at 2.8 A resolution."; RL Proteins 79:2335-2340(2011). RN [8] {ECO:0007744|PDB:3V3N} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD AND RP MINOCYCLINE, FUNCTION, REACTION MECHANISM, COFACTOR, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF LYS-64; PHE-235; THR-280; RP SER-326 AND ASN-371, AND EXPRESSION IN E.COLI. RX PubMed=23236139; DOI=10.1073/pnas.1209335110; RA Walkiewicz K., Benitez Cardenas A.S., Sun C., Bacorn C., Saxer G., RA Shamoo Y.; RT "Small changes in enzyme function can lead to surprisingly large fitness RT effects during adaptive evolution of antibiotic resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 109:21408-21413(2012). RN [9] {ECO:0007744|PDB:3V3O} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD AND RP TIGECYCLINE, AND COFACTOR. RA Walkiewicz K., Shamoo Y.; RT "Crystal structure of TetX2 T280A: an adaptive mutant in complex with RT tigecycline."; RL Submitted (DEC-2011) to the PDB data bank. RN [10] {ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV} RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD AND RP WITH ANTIBIOTICS, COFACTOR, AND SUBUNIT. RX PubMed=23999299; DOI=10.1107/s0907444913013802; RA Volkers G., Damas J.M., Palm G.J., Panjikar S., Soares C.M., Hinrichs W.; RT "Putative dioxygen-binding sites and recognition of tigecycline and RT minocycline in the tetracycline-degrading monooxygenase TetX."; RL Acta Crystallogr. D 69:1758-1767(2013). CC -!- FUNCTION: An FAD-requiring monooxygenase active on tetracycline CC antibiotic derivatives, which leads to their inactivation CC (PubMed:15452119, PubMed:16128584). Hydroxylates carbon 11a of CC oxytetracycline and tigecycline (PubMed:15452119, PubMed:26097034). CC Acts on many tetracycline analogs (chlorotetracycline, demeclocycline, CC doxycycline, minocycline, oxytetracyclinee), probably by CC monooxygenization (PubMed:15452119, PubMed:16128584). Tigecycline, a CC new generation tetracycline antibiotic, is rendered less effective CC against E.coli by this monooxygenation, is much weaker at inhibiting CC translation in vitro and binds Mg(2+) considerably less well CC (PubMed:16128584, PubMed:26097034). Expression in E.coli BW25113 CC reduces its growth rate about 5%. The reaction probably proceeds by FAD CC reduction by NADPH and, second, hydroxylation of antibiotic in a ping- CC pong mechanism (PubMed:23236139). Degrades chlortetracycline, probably CC by monooxygenation (PubMed:15452119, PubMed:28481346). Slowly oxidizes CC anhydrotetracycline, the final substrate in tetracycline biosynthesis CC (PubMed:26097034). {ECO:0000255|HAMAP-Rule:MF_00845, CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:16128584, CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:26097034, CC ECO:0000269|PubMed:28481346}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a tetracycline + H(+) + NADPH + O2 = an 11a- CC hydroxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61444, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:144644, CC ChEBI:CHEBI:144645; Evidence={ECO:0000255|HAMAP-Rule:MF_00845, CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:16128584, CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:26097034, CC ECO:0000269|PubMed:28481346}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADPH + O2 + tetracycline = 11a-hydroxytetracycline + CC H2O + NADP(+); Xref=Rhea:RHEA:50004, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77932, ChEBI:CHEBI:132727; CC EC=1.14.13.231; Evidence={ECO:0000305|PubMed:15452119, CC ECO:0000305|PubMed:26097034}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADPH + O2 + tigecycline = 11a-hydroxytigecycline + H2O CC + NADP(+); Xref=Rhea:RHEA:61448, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142708, ChEBI:CHEBI:142709; CC Evidence={ECO:0000269|PubMed:16128584}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADPH + O2 + oxytetracycline = 11a-hydroxy- CC oxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61452, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133011, CC ChEBI:CHEBI:144646; Evidence={ECO:0000269|PubMed:15452119}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00845, ECO:0000269|PubMed:15452119, CC ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745, CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:23999299, CC ECO:0000269|Ref.9}; CC Note=Binds 1 FAD per subunit, which helps bind the antibiotic CC substrate. {ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745, CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:23999299, CC ECO:0000269|Ref.9}; CC -!- ACTIVITY REGULATION: Anhydrotetracycline, a poor substrate, prevents CC tetracycline degradation in vitro. {ECO:0000269|PubMed:28481346}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=19.9 uM for demeclocycline {ECO:0000269|PubMed:15452119}; CC KM=28.4 uM for minocycline {ECO:0000269|PubMed:15452119}; CC KM=35 uM for minocycline {ECO:0000269|PubMed:23236139}; CC KM=44 uM for tigecycline {ECO:0000269|PubMed:16128584}; CC KM=54 uM for tetracycline {ECO:0000269|PubMed:15452119}; CC KM=76.3 uM for oxytetracycline {ECO:0000269|PubMed:15452119}; CC KM=83.7 uM for doxycycline {ECO:0000269|PubMed:15452119}; CC KM=110 uM for chlortetracycline {ECO:0000269|PubMed:15452119}; CC KM=133 uM for NADPH {ECO:0000269|PubMed:15452119}; CC KM=75 uM for NADPH {ECO:0000269|PubMed:23236139}; CC Note=kcat varies from 1.3 sec(-1) for oxytetracycline to 0.12 sec(-1) CC for minocycline. {ECO:0000269|PubMed:15452119}; CC pH dependence: CC Optimum pH is 8.5. {ECO:0000269|PubMed:15452119}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00845, CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:21402075, CC ECO:0000269|PubMed:21590745, ECO:0000269|PubMed:23236139, CC ECO:0000269|PubMed:23999299}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00845}. CC -!- DOMAIN: Consists of an N-terminal FAD-binding domain with a Rossman CC fold and a C-terminal substrate-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00845, ECO:0000269|PubMed:21402075, CC ECO:0000269|PubMed:21590745, ECO:0000269|PubMed:23236139, CC ECO:0000269|PubMed:23999299}. CC -!- MISCELLANEOUS: Encoded in a conjugative transposon. Immediately CC upstream of this gene is an N-terminally truncated tetX1 gene that is CC inactive. {ECO:0000269|PubMed:11472924}. CC -!- MISCELLANEOUS: Tetracycline antibiotics bind to the ribosomal acceptor CC site (A-site), preventing binding of the aminoacyl-tRNA to the A-site. CC The hydrophilic side of tetracycline makes many hydrogen-bonding CC interactions with oxygen atoms of the ribosome's phosphate backbone. CC {ECO:0000305|PubMed:16128584}. CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00845}. 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; AJ311171; CAC47932.1; -; Genomic_DNA. DR RefSeq; WP_008651082.1; NZ_RWHY01000040.1. DR PDB; 2XDO; X-ray; 2.09 A; A/B/C/D=11-388. DR PDB; 2XYO; X-ray; 3.00 A; A/B/C/D=11-388. DR PDB; 2Y6Q; X-ray; 2.37 A; A/B/C/D=11-388. DR PDB; 2Y6R; X-ray; 3.10 A; A/B/C/D=11-388. DR PDB; 3P9U; X-ray; 2.81 A; A/B/C/D=11-388. DR PDB; 3V3N; X-ray; 2.70 A; A/B/C/D=11-388. DR PDB; 3V3O; X-ray; 2.90 A; A/B/C/D=11-388. DR PDB; 4A6N; X-ray; 2.30 A; A/B/C/D=11-388. DR PDB; 4A99; X-ray; 2.18 A; A/B/C/D=11-388. DR PDB; 4GUV; X-ray; 2.73 A; A/B/C/D=11-388. DR PDBsum; 2XDO; -. DR PDBsum; 2XYO; -. DR PDBsum; 2Y6Q; -. DR PDBsum; 2Y6R; -. DR PDBsum; 3P9U; -. DR PDBsum; 3V3N; -. DR PDBsum; 3V3O; -. DR PDBsum; 4A6N; -. DR PDBsum; 4A99; -. DR PDBsum; 4GUV; -. DR AlphaFoldDB; Q93L51; -. DR SMR; Q93L51; -. DR DrugBank; DB13092; Meclocycline. DR GeneID; 82860462; -. DR BRENDA; 1.14.13.231; 709. DR EvolutionaryTrace; Q93L51; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR HAMAP; MF_00845; TetX_monooxygenase; 1. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR043683; TetX_monooxygenase. DR PANTHER; PTHR46972; MONOOXYGENASE ASQM-RELATED; 1. DR PANTHER; PTHR46972:SF1; RHODANESE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Cytoplasm; FAD; Flavoprotein; KW Monooxygenase; NADP; Nucleotide-binding; Oxidoreductase; KW Transposable element. FT CHAIN 1..388 FT /note="Flavin-dependent monooxygenase" FT /id="PRO_0000448378" FT BINDING 26..27 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:21402075, FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO, FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U, FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O, FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, FT ECO:0007744|PDB:4GUV" FT BINDING 45..48 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:21402075, FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO, FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U, FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O, FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, FT ECO:0007744|PDB:4GUV" FT BINDING 54 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845, FT ECO:0000305|PubMed:21402075" FT BINDING 61 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845, FT ECO:0007744|PDB:3V3O" FT BINDING 117 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845, FT ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745, FT ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO, FT ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R, FT ECO:0007744|PDB:3P9U, ECO:0007744|PDB:3V3N, FT ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N, FT ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV" FT BINDING 139 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:21402075, FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO, FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U, FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O, FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, FT ECO:0007744|PDB:4GUV" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21402075, FT ECO:0000269|PubMed:23999299, ECO:0007744|PDB:2Y6Q, FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3V3N, FT ECO:0007744|PDB:4A99" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21402075, FT ECO:0000269|PubMed:23999299, ECO:0007744|PDB:2Y6Q, FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3V3O, FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99" FT BINDING 311 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845, FT ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745, FT ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO, FT ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R, FT ECO:0007744|PDB:3P9U, ECO:0007744|PDB:3V3N, FT ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N, FT ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV" FT BINDING 321..324 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:21402075, FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO, FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U, FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O, FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, FT ECO:0007744|PDB:4GUV" FT MUTAGEN 64 FT /note="K->R: E.coli is more resistant to minocycline (MCN), FT no change in affinity for MCN, decreased affinity for FT NADPH, decreased growth rate in E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT MUTAGEN 235 FT /note="F->Y: E.coli is more resistant to MCN, decreased FT affinity for MCN, slightly decreased affinity for NADPH, FT increased growth rate in E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT MUTAGEN 280 FT /note="T->A: E.coli is more resistant to MCN, 2-fold FT increased affinity for MCN, 4-fold increase for NADPH, FT increased growth rate in E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT MUTAGEN 280 FT /note="T->S: E.coli is more resistant to MCN, slightly FT increased affinity for MCN, decreased affinity for NADPH, FT decreased growth rate in E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT MUTAGEN 326 FT /note="S->I: E.coli is more resistant to MCN, no change in FT affinity for MCN or NADPH, increased growth rate in FT E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT MUTAGEN 371 FT /note="N->I: E.coli is more resistant to MCN, 2-fold FT increased affinity for MCN, slightly increased affinity for FT NADPH, increased growth rate in E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT MUTAGEN 371 FT /note="N->T: E.coli is more resistant to MCN, increased FT affinity for MCN, decreased affinity for NADPH, increased FT growth rate in E.coli." FT /evidence="ECO:0000269|PubMed:23236139" FT TURN 13..16 FT /evidence="ECO:0007829|PDB:4A99" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 26..36 FT /evidence="ECO:0007829|PDB:2XDO" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:3V3N" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 67..73 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 77..83 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 94..101 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:3V3N" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:3V3N" FT HELIX 117..126 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 146..153 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:2XDO" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 184..197 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 198..201 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 203..209 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 221..229 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 232..240 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:3P9U" FT HELIX 256..266 FT /evidence="ECO:0007829|PDB:2XDO" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 272..280 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 285..291 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 311..314 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:4A99" FT HELIX 324..339 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:2XDO" FT HELIX 346..376 FT /evidence="ECO:0007829|PDB:2XDO" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:4A99" SQ SEQUENCE 388 AA; 43708 MW; C0F8976A7A82F394 CRC64; MTMRIDTDKQ MNLLSDKNVA IIGGGPVGLT MAKLLQQNGI DVSVYERDND REARIFGGTL DLHKGSGQEA MKKAGLLQTY YDLALPMGVN IADEKGNILS TKNVKPENRF DNPEINRNDL RAILLNSLEN DTVIWDRKLV MLEPGKKKWT LTFENKPSET ADLVILANGG MSKVRKFVTD TEVEETGTFN IQADIHQPEI NCPGFFQLCN GNRLMASHQG NLLFANPNNN GALHFGISFK TPDEWKNQTQ VDFQNRNSVV DFLLKEFSDW DERYKELIHT TLSFVGLATR IFPLEKPWKS KRPLPITMIG DAAHLMPPFA GQGVNSGLVD ALILSDNLAD GKFNSIEEAV KNYEQQMFIY GKEAQEESTQ NEIEMFKPDF TFQQLLNV //