AMO_ECOLI
ID AMO_ECOLI Reviewed; 757 AA.
AC P46883; O53008; P78153;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544};
DE AltName: Full=2-phenylethylamine oxidase;
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=Tyramine oxidase;
DE Flags: Precursor;
GN Name=tynA; Synonyms=maoA; OrderedLocusNames=b1386, JW1381;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H., Murooka Y.;
RT "Nucleotide sequence of the gene for monoamine oxidase (maoA) from
RT Escherichia coli.";
RL J. Ferment. Bioeng. 77:315-319(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.0
RP ANGSTROMS).
RC STRAIN=K12 / K10;
RX PubMed=8591028; DOI=10.1016/s0969-2126(01)00253-2;
RA Parsons M.R., Convery M.A., Wilmot C.M., Yadav K.D.S., Blakeley V.,
RA Corner A.S., Phillips S.E.V., McPherson M.J., Knowles P.F.;
RT "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia
RT coli at 2-A resolution.";
RL Structure 3:1171-1184(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-35, AND
RP CHARACTERIZATION.
RC STRAIN=K12 / W3350 / ATCC 27020;
RX PubMed=8647101; DOI=10.1111/j.1432-1033.1996.0584p.x;
RA Steinebach V., Benen J.A.E., Bader R., Postma P.W., De Vries S.,
RA Duine J.A.;
RT "Cloning of the maoA gene that encodes aromatic amine oxidase of
RT Escherichia coli W3350 and characterization of the overexpressed enzyme.";
RL Eur. J. Biochem. 237:584-591(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
RA Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
RA Garcia J.L., Diaz E.;
RT "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a
RT new aerobic hybrid pathway.";
RL J. Biol. Chem. 273:25974-25986(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-757.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9109378; DOI=10.1016/s0014-5793(97)00228-7;
RA Ferrandez A., Prieto M.A., Garcia J.L., Diaz E.;
RT "Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase
RT from Escherichia coli.";
RL FEBS Lett. 406:23-27(1997).
RN [9]
RP PROTEIN SEQUENCE OF 31-50.
RX PubMed=8631685; DOI=10.1128/jb.178.10.2941-2947.1996;
RA Yamashita M., Azakami H., Yokoro N., Roh J.-H., Suzuki H., Kumagai H.,
RA Murooka Y.;
RT "maoB, a gene that encodes a positive regulator of the monoamine oxidase
RT gene (maoA) in Escherichia coli.";
RL J. Bacteriol. 178:2941-2947(1996).
RN [10]
RP PROTEIN SEQUENCE OF 31-40.
RC STRAIN=K12;
RX PubMed=9043126; DOI=10.1099/00221287-143-2-513;
RA Hanlon S.P., Hill T.K., Flavell M.A., Stringfellow J.M., Cooper R.A.;
RT "2-phenylethylamine catabolism by Escherichia coli K-12: gene organization
RT and expression.";
RL Microbiology 143:513-518(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 31-757 IN COMPLEX WITH CALCIUM;
RP COPPER AND SUBSTRATE, ACTIVITY REGULATION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP AND SUBUNIT.
RX PubMed=9048544; DOI=10.1021/bi962205j;
RA Wilmot C.M., Murray J.M., Alton G., Parsons M.R., Convery M.A.,
RA Blakeley V., Corner A.S., Palcic M.M., Knowles P.F., McPherson M.J.,
RA Phillips S.E.V.;
RT "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia
RT coli: exploring the reductive half-reaction.";
RL Biochemistry 36:1608-1620(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 36-757 IN COMPLEX WITH CALCIUM
RP AND COPPER, TOPAQUINONE AT TYR-496, ACTIVE SITE, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=10387067; DOI=10.1021/bi9900469;
RA Murray J.M., Saysell C.G., Wilmot C.M., Tambyrajah W.S., Jaeger J.,
RA Knowles P.F., Phillips S.E.V., McPherson M.J.;
RT "The active site base controls cofactor reactivity in Escherichia coli
RT amine oxidase: X-ray crystallographic studies with mutational variants.";
RL Biochemistry 38:8217-8227(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 31-757 IN COMPLEX WITH CALCIUM;
RP COPPER AND SUBSTRATE, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10576737; DOI=10.1126/science.286.5445.1724;
RA Wilmot C.M., Hajdu J., McPherson M.J., Knowles P.F., Phillips S.E.;
RT "Visualization of dioxygen bound to copper during enzyme catalysis.";
RL Science 286:1724-1728(1999).
CC -!- FUNCTION: The enzyme prefers aromatic over aliphatic amines.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737,
CC ECO:0000269|PubMed:9048544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225237; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:10576737};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737,
CC ECO:0000269|PubMed:9048544};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit. Can also use zinc ion as cofactor
CC (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737,
CC ECO:0000269|PubMed:9048544};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737,
CC ECO:0000269|PubMed:9048544};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:10387067,
CC ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:10387067};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:10387067};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC -!- ACTIVITY REGULATION: Inhibited by 2-hydrazinopyridine.
CC {ECO:0000269|PubMed:9048544}.
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC phenylacetate from L-phenylalanine: step 2/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10387067,
CC ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000269|PubMed:10387067}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- CAUTION: When highly overexpressed there can be substoichiometric
CC amounts of TPQ in the enzyme; this may be due to imperfect conversion
CC of tyrosine to TPQ (see PubMed:8647101). {ECO:0000305}.
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DR EMBL; D23670; BAA04900.1; -; Genomic_DNA.
DR EMBL; L47571; AAC37012.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74468.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14996.1; -; Genomic_DNA.
DR EMBL; X97452; CAA66104.1; -; Genomic_DNA.
DR EMBL; X97453; CAA66107.1; -; Genomic_DNA.
DR PIR; E64889; E64889.
DR RefSeq; NP_415904.3; NC_000913.3.
DR RefSeq; WP_000535469.1; NZ_SSZK01000012.1.
DR PDB; 1D6U; X-ray; 2.40 A; A/B=31-757.
DR PDB; 1D6Y; X-ray; 2.40 A; A/B=31-757.
DR PDB; 1D6Z; X-ray; 2.10 A; A/B=31-757.
DR PDB; 1DYU; X-ray; 2.04 A; A/B=31-757.
DR PDB; 1JRQ; X-ray; 2.15 A; A/B=31-757.
DR PDB; 1LVN; X-ray; 2.40 A; A/B=31-757.
DR PDB; 1OAC; X-ray; 2.00 A; A/B=31-757.
DR PDB; 1QAF; X-ray; 2.20 A; A/B=36-756.
DR PDB; 1QAK; X-ray; 2.00 A; A/B=36-757.
DR PDB; 1QAL; X-ray; 2.20 A; A/B=36-756.
DR PDB; 1SPU; X-ray; 2.00 A; A/B=31-757.
DR PDB; 2W0Q; X-ray; 2.48 A; A/B=31-757.
DR PDB; 2WGQ; X-ray; 2.50 A; A/B=31-757.
DR PDB; 2WO0; X-ray; 2.60 A; A/B=31-757.
DR PDB; 2WOF; X-ray; 2.25 A; A/B=31-757.
DR PDB; 2WOH; X-ray; 2.70 A; A/B=31-757.
DR PDB; 6EZZ; X-ray; 1.80 A; A/B=31-757.
DR PDBsum; 1D6U; -.
DR PDBsum; 1D6Y; -.
DR PDBsum; 1D6Z; -.
DR PDBsum; 1DYU; -.
DR PDBsum; 1JRQ; -.
DR PDBsum; 1LVN; -.
DR PDBsum; 1OAC; -.
DR PDBsum; 1QAF; -.
DR PDBsum; 1QAK; -.
DR PDBsum; 1QAL; -.
DR PDBsum; 1SPU; -.
DR PDBsum; 2W0Q; -.
DR PDBsum; 2WGQ; -.
DR PDBsum; 2WO0; -.
DR PDBsum; 2WOF; -.
DR PDBsum; 2WOH; -.
DR PDBsum; 6EZZ; -.
DR AlphaFoldDB; P46883; -.
DR SMR; P46883; -.
DR BioGRID; 4260177; 11.
DR DIP; DIP-11057N; -.
DR IntAct; P46883; 6.
DR STRING; 511145.b1386; -.
DR DrugBank; DB01657; 2-amino-3-[4-hydroxy-6-oxo-3-(2-phenyl-cyclopropylimino)-cyclohexa-1,4-dienyl]-propionic acid.
DR DrugBank; DB01634; 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine.
DR DrugBank; DB03631; 3-(4-hydroxy-3-imino-6-oxo-cyclohexa-1,4-dienyl)-alanine.
DR DrugBank; DB02928; 3-Amino-6-Hydroxy-Tyrosine.
DR DrugBank; DB04334; 6-hydroxydopa quinone.
DR DrugBank; DB01576; Dextroamphetamine.
DR DrugBank; DB04325; Phenethylamine.
DR DrugBank; DB02178; Phenylacetaldehyde.
DR PaxDb; P46883; -.
DR PRIDE; P46883; -.
DR EnsemblBacteria; AAC74468; AAC74468; b1386.
DR EnsemblBacteria; BAA14996; BAA14996; BAA14996.
DR GeneID; 945939; -.
DR KEGG; ecj:JW1381; -.
DR KEGG; eco:b1386; -.
DR PATRIC; fig|1411691.4.peg.886; -.
DR EchoBASE; EB2934; -.
DR eggNOG; COG3733; Bacteria.
DR HOGENOM; CLU_011500_5_0_6; -.
DR InParanoid; P46883; -.
DR OMA; TNKLNPY; -.
DR PhylomeDB; P46883; -.
DR BioCyc; EcoCyc:AMINEOXID-MON; -.
DR BioCyc; MetaCyc:AMINEOXID-MON; -.
DR BRENDA; 1.4.3.21; 2026.
DR UniPathway; UPA00139; UER00723.
DR EvolutionaryTrace; P46883; -.
DR PRO; PR:P46883; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:EcoCyc.
DR GO; GO:0048038; F:quinone binding; IDA:EcoCyc.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019607; P:phenylethylamine catabolic process; IDA:EcoCyc.
DR Gene3D; 2.70.98.20; -; 1.
DR Gene3D; 3.30.457.10; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR InterPro; IPR036582; Mao_N_sf.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF07833; Cu_amine_oxidN1; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR SUPFAM; SSF55383; SSF55383; 1.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Copper; Direct protein sequencing; Manganese;
KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal; TPQ.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:8631685,
FT ECO:0000269|PubMed:8647101, ECO:0000269|PubMed:9043126"
FT CHAIN 31..757
FT /note="Primary amine oxidase"
FT /id="PRO_0000035673"
FT REGION 680..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1OAC"
FT ACT_SITE 496
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAK,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0,
FT ECO:0007744|PDB:2WOF"
FT BINDING 411..422
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10576737,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z"
FT BINDING 493..498
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10576737,
FT ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U,
FT ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z,
FT ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1SPU"
FT BINDING 554
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0,
FT ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH"
FT BINDING 556
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0,
FT ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH"
FT BINDING 563
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 564
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH"
FT BINDING 565
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10576737,
FT ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z,
FT ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1OAC,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:2WGQ"
FT BINDING 702
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH"
FT BINDING 708
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 719
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544,
FT ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y,
FT ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU,
FT ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN,
FT ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF,
FT ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL,
FT ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q,
FT ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0,
FT ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH"
FT MOD_RES 496
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:10387067,
FT ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ,
FT ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK,
FT ECO:0007744|PDB:1QAL"
FT VARIANT 42
FT /note="K -> E (in strain: W)"
FT VARIANT 59
FT /note="L -> I (in strain: W)"
FT CONFLICT 33
FT /note="G -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="K -> E (in Ref. 1; BAA04900)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..259
FT /note="GY -> VI (in Ref. 1; BAA04900)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="I -> II (in Ref. 1; BAA04900)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="P -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="A -> P (in Ref. 1; BAA04900)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="H -> D (in Ref. 1; BAA04900)"
FT /evidence="ECO:0000305"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1QAK"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1D6Y"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1OAC"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 369..379
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 382..399
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 404..408
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1QAF"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 437..444
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 450..470
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 478..493
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 496..505
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 510..518
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 554..564
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 568..582
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 590..600
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 603..606
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 614..624
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 630..637
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 662..665
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 667..672
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 694..697
FT /evidence="ECO:0007829|PDB:6EZZ"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:1OAC"
FT STRAND 707..719
FT /evidence="ECO:0007829|PDB:6EZZ"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:6EZZ"
FT STRAND 726..746
FT /evidence="ECO:0007829|PDB:6EZZ"
SQ SEQUENCE 757 AA; 84379 MW; 65600BCED35243DB CRC64;
MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DKTLKEFGAD VQWDDYAQLF
TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV SDTFINDVFQ SGLDQTFQVE
KRPHPLNALT ADEIKQAVEI VKASADFKPN TRFTEISLLP PDKEAVWAFA LENKPVDQPR
KADVIMLDGK HIIEAVVDLQ NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK
KRGITDAKKV ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL
EQKKIVKIEE GPVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG DMIHWRNWDF
HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG DPDIGWYFKA YLDSGDYGMG
TLTSPIARGK DAPSNAVLLN ETIADYTGVP MEIPRAIAVF ERYAGPEYKH QEMGQPNVST
ERRELVVRWI STVGNYDYIF DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR
YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI
GNEQDAAQKF DPGTIRLLSN PNKENRMGNP VSYQIIPYAG GTHPVAKGAQ FAPDEWIYHR
LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD NESLDNTDAV VWMTTGTTHV
ARAEEWPIMP TEWVHTLLKP WNFFDETPTL GALKKDK
