ID CYB2_YEAST Reviewed; 591 AA. AC P00175; D6VZC0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 27-MAR-2024, entry version 226. DE RecName: Full=L-lactate dehydrogenase (cytochrome); DE EC=1.1.2.3 {ECO:0000269|PubMed:3004948}; DE AltName: Full=Cytochrome b2 {ECO:0000303|PubMed:3004948, ECO:0000303|PubMed:4593578}; DE AltName: Full=Flavocytochrome b2 {ECO:0000303|PubMed:11914072, ECO:0000303|PubMed:2329585}; DE Short=FCB2 {ECO:0000303|PubMed:11914072}; DE AltName: Full=L-lactate ferricytochrome c oxidoreductase; DE Short=L-LCR; DE Flags: Precursor; GN Name=CYB2; OrderedLocusNames=YML054C; ORFNames=YM9958.08C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP DISRUPTION PHENOTYPE. RX PubMed=3004948; DOI=10.1002/j.1460-2075.1985.tb04076.x; RA Guiard B.; RT "Structure, expression and regulation of a nuclear gene encoding a RT mitochondrial protein: the yeast L(+)-lactate cytochrome c oxidoreductase RT (cytochrome b2)."; RL EMBO J. 4:3265-3272(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP PROTEIN SEQUENCE OF 81-394. RX PubMed=6365548; DOI=10.1111/j.1432-1033.1984.tb07976.x; RA Ghrir R., Becam A.-M., Lederer F.; RT "Primary structure of flavocytochrome b2 from baker's yeast. Purification RT by reverse-phase high-pressure liquid chromatography and sequencing of RT fragment alpha cyanogen bromide peptides."; RL Eur. J. Biochem. 139:59-74(1984). RN [5] RP PROTEIN SEQUENCE OF 395-591. RX PubMed=3902473; DOI=10.1111/j.1432-1033.1985.tb09213.x; RA Lederer F., Cortial S., Becam A.-M., Haumont P.-Y., Perez L.; RT "Complete amino acid sequence of flavocytochrome b2 from baker's yeast."; RL Eur. J. Biochem. 152:419-428(1985). RN [6] RP PROTEIN SEQUENCE OF 81-94. RX PubMed=165435; DOI=10.1038/255422a0; RA Guiard B., Lederer F., Jacq C.; RT "More similarity between bakers'yeast L-(+)-lactate dehydrogenase and liver RT microsomal sytochrome B5."; RL Nature 255:422-423(1975). RN [7] RP PROTEIN SEQUENCE OF 83-88 AND 564-570, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 201238 / W303-1B; RX PubMed=11502169; DOI=10.1021/bi010277r; RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., RA Schmitter J.-M.; RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular RT complex."; RL Biochemistry 40:9758-9769(2001). RN [8] RP PROTEIN SEQUENCE OF 88-183. RX PubMed=776230; DOI=10.1016/s0300-9084(76)80437-3; RA Guiard B., Lederer F.; RT "Complete amino acid sequence of the heme-binding core in bakers' yeast RT cytochrome b2 (L-(+)-lactate dehydrogenase)."; RL Biochimie 58:305-316(1976). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=4593578; DOI=10.1111/j.1432-1033.1974.tb03271.x; RA Jacq C., Lederer F.; RT "Cytochrome b2 from bakers' yeast (L-lactate dehydrogenase). A double- RT headed enzyme."; RL Eur. J. Biochem. 41:311-320(1974). RN [10] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RX PubMed=22984289; DOI=10.1074/mcp.m112.021105; RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.; RT "Intermembrane space proteome of yeast mitochondria."; RL Mol. Cell. Proteomics 11:1840-1852(2012). RN [12] {ECO:0007744|PDB:1FCB} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 81-591 IN COMPLEX WITH FMN; HEME B RP AND PYRUVATE, COFACTOR, AND DOMAIN. RX PubMed=2329585; DOI=10.1016/0022-2836(90)90240-m; RA Xia Z.-X., Mathews F.S.; RT "Molecular structure of flavocytochrome b2 at 2.4-A resolution."; RL J. Mol. Biol. 212:837-863(1990). RN [13] {ECO:0007744|PDB:1KBI, ECO:0007744|PDB:1KBJ} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 81-591 IN COMPLEXES WITH FMN; HEME RP B AND PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND DOMAIN. RX PubMed=11914072; DOI=10.1021/bi0119870; RA Cunane L.M., Barton J.D., Chen Z.-W., Welsh F.E., Chapman S.K., Reid G.A., RA Mathews F.S.; RT "Crystallographic study of the recombinant flavin-binding domain of Baker's RT yeast flavocytochrome b(2): comparison with the intact wild-type enzyme."; RL Biochemistry 41:4264-4272(2002). RN [14] {ECO:0007744|PDB:2OZ0} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 81-591 OF MUTANT GLN-453 IN RP COMPLEX WITH FMN; HEME B AND PYRUVATE, COFACTOR, ACTIVE SITE, REACTION RP MECHANISM, AND MUTAGENESIS OF HIS-453. RX PubMed=17563122; DOI=10.1021/bi7005543; RA Tsai C.L., Gokulan K., Sobrado P., Sacchettini J.C., Fitzpatrick P.F.; RT "Mechanistic and structural studies of H373Q flavocytochrome b2: effects of RT mutating the active site base."; RL Biochemistry 46:7844-7851(2007). CC -!- FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to CC pyruvate with subsequent transfer of electrons to cytochrome c CC (PubMed:11914072). Is involved in the utilization of (S)-lactate as a CC sole source of carbon for growth (PubMed:3004948). Can also use CC ferricyanide as an electron acceptor in vitro (PubMed:4593578, CC PubMed:3004948). {ECO:0000269|PubMed:11914072, CC ECO:0000269|PubMed:3004948, ECO:0000269|PubMed:4593578}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome CC c] + 2 H(+) + pyruvate; Xref=Rhea:RHEA:19909, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16651, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.3; CC Evidence={ECO:0000269|PubMed:11914072, ECO:0000305|PubMed:3004948, CC ECO:0000305|PubMed:4593578}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19910; CC Evidence={ECO:0000269|PubMed:3004948}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:17563122, CC ECO:0000269|PubMed:2329585}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently CC per subunit. {ECO:0000269|PubMed:11914072}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.49 mM for (S)-lactate {ECO:0000269|PubMed:11914072}; CC KM=10 uM for cytochrome c {ECO:0000269|PubMed:11914072}; CC Note=kcat is 207 sec(-1) with cytochrome c as electron acceptor. kcat CC is 400 sec(-1) with ferricyanide as electron acceptor. CC {ECO:0000269|PubMed:11914072}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:4593578}. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space CC {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:22984289}. CC -!- INDUCTION: By L-lactate. Induced during respiratory adaptation. CC -!- DOMAIN: Consists of two discrete domains, an N-terminal cytochrome b CC domain from residues 81 to 179 and a C-terminal flavin-binding domain CC from residues 180 to 566. In addition there is an extended C-terminal CC tail (PubMed:2329585, PubMed:11914072). The cytochrome b domain is CC required for efficient cytochrome c reduction (PubMed:11914072). CC {ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585}. CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene leads to a deficiency CC in L-lactate dehydrogenase activity and consequently to the inability CC to use L-lactate as a sole source of carbon. CC {ECO:0000269|PubMed:3004948}. CC -!- MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome b5 CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the FMN-dependent CC alpha-hydroxy acid dehydrogenase family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/YLDHS/"; 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; X03215; CAA26959.1; -; Genomic_DNA. DR EMBL; Z46729; CAA86721.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09844.1; -; Genomic_DNA. DR PIR; A24583; CBBY2. DR RefSeq; NP_013658.1; NM_001182412.1. DR PDB; 1FCB; X-ray; 2.40 A; A/B=81-591. DR PDB; 1KBI; X-ray; 2.30 A; A/B=81-591. DR PDB; 1KBJ; X-ray; 2.50 A; A/B=180-591. DR PDB; 1LCO; X-ray; 2.90 A; A/B=81-591. DR PDB; 1LDC; X-ray; 2.90 A; A/B=81-591. DR PDB; 1LTD; X-ray; 2.60 A; A/B=86-591. DR PDB; 1QCW; X-ray; 2.75 A; A/B=182-591. DR PDB; 1SZE; X-ray; 3.00 A; A/B=81-591. DR PDB; 1SZF; X-ray; 2.70 A; A/B=81-591. DR PDB; 1SZG; X-ray; 2.70 A; A/B=81-591. DR PDB; 2OZ0; X-ray; 2.80 A; A/B=81-591. DR PDB; 3KS0; X-ray; 2.70 A; A/B=86-180. DR PDBsum; 1FCB; -. DR PDBsum; 1KBI; -. DR PDBsum; 1KBJ; -. DR PDBsum; 1LCO; -. DR PDBsum; 1LDC; -. DR PDBsum; 1LTD; -. DR PDBsum; 1QCW; -. DR PDBsum; 1SZE; -. DR PDBsum; 1SZF; -. DR PDBsum; 1SZG; -. DR PDBsum; 2OZ0; -. DR PDBsum; 3KS0; -. DR AlphaFoldDB; P00175; -. DR SMR; P00175; -. DR BioGRID; 35113; 83. DR DIP; DIP-5810N; -. DR IntAct; P00175; 15. DR MINT; P00175; -. DR STRING; 4932.YML054C; -. DR PaxDb; 4932-YML054C; -. DR PeptideAtlas; P00175; -. DR ABCD; P00175; 1 sequenced antibody. DR EnsemblFungi; YML054C_mRNA; YML054C; YML054C. DR GeneID; 854950; -. DR KEGG; sce:YML054C; -. DR AGR; SGD:S000004518; -. DR SGD; S000004518; CYB2. DR VEuPathDB; FungiDB:YML054C; -. DR eggNOG; KOG0537; Eukaryota. DR eggNOG; KOG0538; Eukaryota. DR GeneTree; ENSGT00390000018717; -. DR HOGENOM; CLU_020639_1_1_1; -. DR InParanoid; P00175; -. DR OMA; RIWFRPK; -. DR OrthoDB; 1887365at2759; -. DR BioCyc; MetaCyc:YML054C-MONOMER; -. DR BioCyc; YEAST:YML054C-MONOMER; -. DR BRENDA; 1.1.2.3; 984. DR SABIO-RK; P00175; -. DR BioGRID-ORCS; 854950; 7 hits in 10 CRISPR screens. DR EvolutionaryTrace; P00175; -. DR PRO; PR:P00175; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P00175; Protein. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IDA:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006089; P:lactate metabolic process; IMP:SGD. DR CDD; cd02922; FCB2_FMN; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf. DR InterPro; IPR018506; Cyt_B5_heme-BS. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR037396; FMN_HAD. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd. DR PANTHER; PTHR10578:SF149; L-LACTATE DEHYDROGENASE (CYTOCHROME); 1. DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF01070; FMN_dh; 1. DR PRINTS; PR00363; CYTOCHROMEB5. DR SMART; SM01117; Cyt-b5; 1. DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Electron transport; Flavoprotein; KW FMN; Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; KW Reference proteome; Respiratory chain; Transit peptide; Transport. FT TRANSIT 1..80 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:165435, FT ECO:0000269|PubMed:6365548" FT CHAIN 81..591 FT /note="L-lactate dehydrogenase (cytochrome)" FT /id="PRO_0000006480" FT DOMAIN 88..165 FT /note="Cytochrome b5 heme-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT DOMAIN 197..563 FT /note="FMN hydroxy acid dehydrogenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683" FT ACT_SITE 453 FT /note="Proton acceptor" FT /evidence="ECO:0000305|PubMed:17563122" FT BINDING 123 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 146 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 177 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 219 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0007744|PDB:1KBI" FT BINDING 223 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 223 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 275..278 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 308 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 332 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 334 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 360 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 376 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0007744|PDB:1KBI" FT BINDING 429 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 453 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 456 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 489..493 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT BINDING 512..513 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:11914072, FT ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, FT ECO:0007744|PDB:1KBI" FT MUTAGEN 453 FT /note="H->Q: 12000-fold decrease in catalytic activity and FT 50000-fold decrease in catalytic efficiency, with FT ferricyanide as electron acceptor." FT /evidence="ECO:0000269|PubMed:17563122" FT CONFLICT 165 FT /note="Q -> E (in Ref. 4; AA sequence and 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 466 FT /note="E -> Q (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 513 FT /note="R -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 570 FT /note="V -> P (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 95..98 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:1KBI" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:1KBI" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 139..142 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 150..154 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:1FCB" FT HELIX 183..194 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 205..215 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 218..225 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:1LDC" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 266..274 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:1KBI" FT TURN 285..288 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 289..297 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 298..301 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 315..320 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:1FCB" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 339..352 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 370..377 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 398..401 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:1LTD" FT HELIX 412..421 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 434..442 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 446..450 FT /evidence="ECO:0007829|PDB:1KBI" FT TURN 453..456 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 464..476 FT /evidence="ECO:0007829|PDB:1KBI" FT TURN 477..479 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 481..483 FT /evidence="ECO:0007829|PDB:1FCB" FT STRAND 484..491 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 495..504 FT /evidence="ECO:0007829|PDB:1KBI" FT STRAND 507..511 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 513..545 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 555..557 FT /evidence="ECO:0007829|PDB:1KBI" FT TURN 561..564 FT /evidence="ECO:0007829|PDB:1KBI" FT HELIX 574..579 FT /evidence="ECO:0007829|PDB:1KBI" SQ SEQUENCE 591 AA; 65539 MW; DBADA0751B3C5B83 CRC64; MLKYKPLLKI SKNCEAAILR ASKTRLNTIR AYGSTVPKSK SFEQDSRKRT QSWTALRVGA ILAATSSVAY LNWHNGQIDN EPKLDMNKQK ISPAEVAKHN KPDDCWVVIN GYVYDLTRFL PNHPGGQDVI KFNAGKDVTA IFEPLHAPNV IDKYIAPEKK LGPLQGSMPP ELVCPPYAPG ETKEDIARKE QLKSLLPPLD NIINLYDFEY LASQTLTKQA WAYYSSGAND EVTHRENHNA YHRIFFKPKI LVDVRKVDIS TDMLGSHVDV PFYVSATALC KLGNPLEGEK DVARGCGQGV TKVPQMISTL ASCSPEEIIE AAPSDKQIQW YQLYVNSDRK ITDDLVKNVE KLGVKALFVT VDAPSLGQRE KDMKLKFSNT KAGPKAMKKT NVEESQGASR ALSKFIDPSL TWKDIEELKK KTKLPIVIKG VQRTEDVIKA AEIGVSGVVL SNHGGRQLDF SRAPIEVLAE TMPILEQRNL KDKLEVFVDG GVRRGTDVLK ALCLGAKGVG LGRPFLYANS CYGRNGVEKA IEILRDEIEM SMRLLGVTSI AELKPDLLDL STLKARTVGV PNDVLYNEVY EGPTLTEFED A //