CYB2_YEAST
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 03-AUG-2022, entry version 218.
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/";
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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; 79.
DR DIP; DIP-5810N; -.
DR IntAct; P00175; 15.
DR MINT; P00175; -.
DR STRING; 4932.YML054C; -.
DR PaxDb; P00175; -.
DR PRIDE; P00175; -.
DR ABCD; P00175; 1 sequenced antibody.
DR EnsemblFungi; YML054C_mRNA; YML054C; YML054C.
DR GeneID; 854950; -.
DR KEGG; sce:YML054C; -.
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; FTRLMQT; -.
DR BioCyc; MetaCyc:YML054C-MON; -.
DR BioCyc; YEAST:YML054C-MON; -.
DR BRENDA; 1.1.2.3; 984.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-390918; Peroxisomal lipid metabolism.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR SABIO-RK; P00175; -.
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; 3.10.120.10; -; 1.
DR Gene3D; 3.20.20.70; -; 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 Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 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
