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Primary amine oxidase (EC 1.4.3.21) (2-phenylethylamine oxidase) (Copper amine oxidase) (Tyramine oxidase)

 AMO_ECOLI               Reviewed;         757 AA.
P46883; O53008; P78153;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Primary amine oxidase;
EC=1.4.3.21 {ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544};
AltName: Full=2-phenylethylamine oxidase;
AltName: Full=Copper amine oxidase;
AltName: Full=Tyramine oxidase;
Flags: Precursor;
Name=tynA; Synonyms=maoA; OrderedLocusNames=b1386, JW1381;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H.,
Murooka Y.;
"Nucleotide sequence of the gene for monoamine oxidase (maoA) from
Escherichia coli.";
J. Ferment. Bioeng. 77:315-319(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.0
ANGSTROMS).
STRAIN=K12 / K10;
PubMed=8591028; DOI=10.1016/S0969-2126(01)00253-2;
Parsons M.R., Convery M.A., Wilmot C.M., Yadav K.D.S., Blakeley V.,
Corner A.S., Phillips S.E.V., McPherson M.J., Knowles P.F.;
"Crystal structure of a quinoenzyme: copper amine oxidase of
Escherichia coli at 2-A resolution.";
Structure 3:1171-1184(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-35, AND
CHARACTERIZATION.
STRAIN=K12 / W3350 / ATCC 27020;
PubMed=8647101; DOI=10.1111/j.1432-1033.1996.0584p.x;
Steinebach V., Benen J.A.E., Bader R., Postma P.W., De Vries S.,
Duine J.A.;
"Cloning of the maoA gene that encodes aromatic amine oxidase of
Escherichia coli W3350 and characterization of the overexpressed
enzyme.";
Eur. J. Biochem. 237:584-591(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
STRAIN=W / ATCC 11105 / DSM 1900;
PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
Garcia J.L., Diaz E.;
"Catabolism of phenylacetic acid in Escherichia coli. Characterization
of a new aerobic hybrid pathway.";
J. Biol. Chem. 273:25974-25986(1998).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-757.
STRAIN=W / ATCC 11105 / DSM 1900;
PubMed=9109378; DOI=10.1016/S0014-5793(97)00228-7;
Ferrandez A., Prieto M.A., Garcia J.L., Diaz E.;
"Molecular characterization of PadA, a phenylacetaldehyde
dehydrogenase from Escherichia coli.";
FEBS Lett. 406:23-27(1997).
[9]
PROTEIN SEQUENCE OF 31-50.
PubMed=8631685; DOI=10.1128/jb.178.10.2941-2947.1996;
Yamashita M., Azakami H., Yokoro N., Roh J.-H., Suzuki H., Kumagai H.,
Murooka Y.;
"maoB, a gene that encodes a positive regulator of the monoamine
oxidase gene (maoA) in Escherichia coli.";
J. Bacteriol. 178:2941-2947(1996).
[10]
PROTEIN SEQUENCE OF 31-40.
STRAIN=K12;
PubMed=9043126; DOI=10.1099/00221287-143-2-513;
Hanlon S.P., Hill T.K., Flavell M.A., Stringfellow J.M., Cooper R.A.;
"2-phenylethylamine catabolism by Escherichia coli K-12: gene
organization and expression.";
Microbiology 143:513-518(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 31-757 IN COMPLEX WITH
CALCIUM; COPPER AND SUBSTRATE, ENZYME REGULATION, CATALYTIC ACTIVITY,
ACTIVE SITE, AND SUBUNIT.
PubMed=9048544; DOI=10.1021/bi962205j;
Wilmot C.M., Murray J.M., Alton G., Parsons M.R., Convery M.A.,
Blakeley V., Corner A.S., Palcic M.M., Knowles P.F., McPherson M.J.,
Phillips S.E.V.;
"Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia
coli: exploring the reductive half-reaction.";
Biochemistry 36:1608-1620(1997).
[12]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 36-757 IN COMPLEX WITH
CALCIUM AND COPPER, TOPAQUINONE AT TYR-496, ACTIVE SITE, CATALYTIC
ACTIVITY, AND SUBUNIT.
PubMed=10387067; DOI=10.1021/bi9900469;
Murray J.M., Saysell C.G., Wilmot C.M., Tambyrajah W.S., Jaeger J.,
Knowles P.F., Phillips S.E.V., McPherson M.J.;
"The active site base controls cofactor reactivity in Escherichia coli
amine oxidase: X-ray crystallographic studies with mutational
variants.";
Biochemistry 38:8217-8227(1999).
[13]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 31-757 IN COMPLEX WITH
CALCIUM; COPPER AND SUBSTRATE, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=10576737; DOI=10.1126/science.286.5445.1724;
Wilmot C.M., Hajdu J., McPherson M.J., Knowles P.F., Phillips S.E.;
"Visualization of dioxygen bound to copper during enzyme catalysis.";
Science 286:1724-1728(1999).
-!- FUNCTION: The enzyme prefers aromatic over aliphatic amines.
-!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) +
H(2)O(2). {ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544}.
-!- CATALYTIC ACTIVITY: 2-phenylethylamine + H(2)O + O(2) =
phenylacetaldehyde + NH(3) + H(2)O(2).
{ECO:0000269|PubMed:10576737}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P12807};
Note=Binds 1 copper ion per subunit. Can also use zinc ion as
cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544};
Note=Binds 2 calcium ions per subunit.
{ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544};
-!- COFACTOR:
Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
Evidence={ECO:0000269|PubMed:10387067};
Note=Contains 1 topaquinone per subunit.
{ECO:0000269|PubMed:10387067};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q43077};
Note=Binds 1 Mn(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q43077};
-!- ENZYME REGULATION: Inhibited by 2-hydrazinopyridine.
{ECO:0000269|PubMed:9048544}.
-!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
phenylacetate from L-phenylalanine: step 2/3.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544}.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000269|PubMed:10387067}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
-!- CAUTION: When highly overexpressed there can be substoichiometric
amounts of TPQ in the enzyme; this may be due to imperfect
conversion of tyrosine to TPQ (see PubMed:8647101). {ECO:0000305}.
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EMBL; D23670; BAA04900.1; -; Genomic_DNA.
EMBL; L47571; AAC37012.1; -; Genomic_DNA.
EMBL; U00096; AAC74468.1; -; Genomic_DNA.
EMBL; AP009048; BAA14996.1; -; Genomic_DNA.
EMBL; X97452; CAA66104.1; -; Genomic_DNA.
EMBL; X97453; CAA66107.1; -; Genomic_DNA.
PIR; E64889; E64889.
RefSeq; NP_415904.3; NC_000913.3.
RefSeq; WP_000535469.1; NZ_LN832404.1.
PDB; 1D6U; X-ray; 2.40 A; A/B=31-757.
PDB; 1D6Y; X-ray; 2.40 A; A/B=31-757.
PDB; 1D6Z; X-ray; 2.10 A; A/B=31-757.
PDB; 1DYU; X-ray; 2.04 A; A/B=31-757.
PDB; 1JRQ; X-ray; 2.15 A; A/B=31-757.
PDB; 1LVN; X-ray; 2.40 A; A/B=31-757.
PDB; 1OAC; X-ray; 2.00 A; A/B=31-757.
PDB; 1QAF; X-ray; 2.20 A; A/B=36-756.
PDB; 1QAK; X-ray; 2.00 A; A/B=36-757.
PDB; 1QAL; X-ray; 2.20 A; A/B=36-756.
PDB; 1SPU; X-ray; 2.00 A; A/B=31-757.
PDB; 2W0Q; X-ray; 2.48 A; A/B=31-757.
PDB; 2WGQ; X-ray; 2.50 A; A/B=31-757.
PDB; 2WO0; X-ray; 2.60 A; A/B=31-757.
PDB; 2WOF; X-ray; 2.25 A; A/B=31-757.
PDB; 2WOH; X-ray; 2.70 A; A/B=31-757.
PDBsum; 1D6U; -.
PDBsum; 1D6Y; -.
PDBsum; 1D6Z; -.
PDBsum; 1DYU; -.
PDBsum; 1JRQ; -.
PDBsum; 1LVN; -.
PDBsum; 1OAC; -.
PDBsum; 1QAF; -.
PDBsum; 1QAK; -.
PDBsum; 1QAL; -.
PDBsum; 1SPU; -.
PDBsum; 2W0Q; -.
PDBsum; 2WGQ; -.
PDBsum; 2WO0; -.
PDBsum; 2WOF; -.
PDBsum; 2WOH; -.
ProteinModelPortal; P46883; -.
SMR; P46883; -.
BioGrid; 4260177; 10.
DIP; DIP-11057N; -.
IntAct; P46883; 6.
STRING; 316385.ECDH10B_1511; -.
DrugBank; DB01634; 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine.
DrugBank; DB04325; 2-Phenylethylamine.
DrugBank; DB02928; 3-Amino-6-Hydroxy-Tyrosine.
DrugBank; DB04334; 6-hydroxydopa quinone.
DrugBank; DB02178; Phenylacetaldehyde.
PaxDb; P46883; -.
PRIDE; P46883; -.
EnsemblBacteria; AAC74468; AAC74468; b1386.
EnsemblBacteria; BAA14996; BAA14996; BAA14996.
GeneID; 945939; -.
KEGG; ecj:JW1381; -.
KEGG; eco:b1386; -.
PATRIC; fig|1411691.4.peg.886; -.
EchoBASE; EB2934; -.
EcoGene; EG13140; tynA.
eggNOG; ENOG4105F11; Bacteria.
eggNOG; COG3733; LUCA.
HOGENOM; HOG000250947; -.
InParanoid; P46883; -.
KO; K00276; -.
PhylomeDB; P46883; -.
BioCyc; EcoCyc:AMINEOXID-MONOMER; -.
BioCyc; MetaCyc:AMINEOXID-MONOMER; -.
BRENDA; 1.4.3.21; 2026.
UniPathway; UPA00139; UER00723.
EvolutionaryTrace; P46883; -.
PRO; PR:P46883; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0005509; F:calcium ion binding; IDA:EcoCyc.
GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0008131; F:primary amine oxidase activity; IDA:EcoCyc.
GO; GO:0048038; F:quinone binding; IDA:EcoCyc.
GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0055114; P:oxidation-reduction process; IDA:EcoCyc.
GO; GO:0019607; P:phenylethylamine catabolic process; IDA:EcoCyc.
Gene3D; 2.70.98.20; -; 1.
Gene3D; 3.30.457.10; -; 1.
InterPro; IPR000269; Cu_amine_oxidase.
InterPro; IPR012854; Cu_amine_oxidase-like_N.
InterPro; IPR015798; Cu_amine_oxidase_C.
InterPro; IPR036460; Cu_amine_oxidase_C_sf.
InterPro; IPR016182; Cu_amine_oxidase_N-reg.
InterPro; IPR015800; Cu_amine_oxidase_N2.
InterPro; IPR015802; Cu_amine_oxidase_N3.
InterPro; IPR036582; Mao_N_sf.
PANTHER; PTHR10638; PTHR10638; 1.
Pfam; PF01179; Cu_amine_oxid; 1.
Pfam; PF07833; Cu_amine_oxidN1; 1.
Pfam; PF02727; Cu_amine_oxidN2; 1.
Pfam; PF02728; Cu_amine_oxidN3; 1.
SUPFAM; SSF49998; SSF49998; 1.
SUPFAM; SSF54416; SSF54416; 2.
SUPFAM; SSF55383; SSF55383; 1.
PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Copper;
Direct protein sequencing; Manganese; Metal-binding; Oxidoreductase;
Periplasm; Reference proteome; Signal; TPQ.
SIGNAL 1 30 {ECO:0000269|PubMed:8631685,
ECO:0000269|PubMed:8647101,
ECO:0000269|PubMed:9043126}.
CHAIN 31 757 Primary amine oxidase.
/FTId=PRO_0000035673.
REGION 411 422 Substrate binding. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000269|PubMed:10576737}.
REGION 493 498 Substrate binding. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1SPU,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
ACT_SITE 413 413 Proton acceptor. {ECO:0000244|PDB:1OAC,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:9048544}.
ACT_SITE 496 496 Schiff-base intermediate with substrate;
via topaquinone. {ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WO0,
ECO:0000244|PDB:2WOF,
ECO:0000269|PubMed:10387067}.
METAL 554 554 Copper; via tele nitrogen.
{ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WO0,
ECO:0000244|PDB:2WOF,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 556 556 Copper; via tele nitrogen.
{ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WO0,
ECO:0000244|PDB:2WOF,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 563 563 Calcium 1. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 563 563 Manganese.
{ECO:0000250|UniProtKB:Q43077}.
METAL 564 564 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 565 565 Calcium 1. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 565 565 Manganese.
{ECO:0000250|UniProtKB:Q43077}.
METAL 603 603 Calcium 2. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 697 697 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 700 700 Calcium 2. {ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:2WGQ,
ECO:0000269|PubMed:10576737}.
METAL 702 702 Calcium 2. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 708 708 Calcium 1. {ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 708 708 Manganese.
{ECO:0000250|UniProtKB:Q43077}.
METAL 709 709 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
METAL 709 709 Calcium 2; via carbonyl oxygen.
METAL 719 719 Copper; via pros nitrogen.
{ECO:0000244|PDB:1D6U,
ECO:0000244|PDB:1D6Y,
ECO:0000244|PDB:1D6Z,
ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1LVN,
ECO:0000244|PDB:1OAC,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000244|PDB:1SPU,
ECO:0000244|PDB:2W0Q,
ECO:0000244|PDB:2WGQ,
ECO:0000244|PDB:2WO0,
ECO:0000244|PDB:2WOF,
ECO:0000244|PDB:2WOH,
ECO:0000269|PubMed:10387067,
ECO:0000269|PubMed:10576737,
ECO:0000269|PubMed:9048544}.
MOD_RES 496 496 2',4',5'-topaquinone.
{ECO:0000244|PDB:1DYU,
ECO:0000244|PDB:1JRQ,
ECO:0000244|PDB:1QAF,
ECO:0000244|PDB:1QAK,
ECO:0000244|PDB:1QAL,
ECO:0000269|PubMed:10387067}.
VARIANT 42 42 K -> E (in strain: W).
VARIANT 59 59 L -> I (in strain: W).
CONFLICT 33 33 G -> E (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 248 248 K -> E (in Ref. 1; BAA04900).
{ECO:0000305}.
CONFLICT 258 259 GY -> VI (in Ref. 1; BAA04900).
{ECO:0000305}.
CONFLICT 276 276 I -> II (in Ref. 1; BAA04900).
{ECO:0000305}.
CONFLICT 288 288 Missing (in Ref. 1). {ECO:0000305}.
CONFLICT 290 290 P -> I (in Ref. 1). {ECO:0000305}.
CONFLICT 456 456 A -> P (in Ref. 1; BAA04900).
{ECO:0000305}.
CONFLICT 659 659 H -> D (in Ref. 1; BAA04900).
{ECO:0000305}.
STRAND 37 39 {ECO:0000244|PDB:1QAK}.
HELIX 40 46 {ECO:0000244|PDB:1OAC}.
STRAND 50 54 {ECO:0000244|PDB:1OAC}.
TURN 55 58 {ECO:0000244|PDB:1OAC}.
STRAND 59 64 {ECO:0000244|PDB:1OAC}.
STRAND 67 71 {ECO:0000244|PDB:1OAC}.
STRAND 76 80 {ECO:0000244|PDB:1OAC}.
STRAND 83 86 {ECO:0000244|PDB:1OAC}.
STRAND 92 96 {ECO:0000244|PDB:1OAC}.
STRAND 98 100 {ECO:0000244|PDB:1OAC}.
HELIX 104 109 {ECO:0000244|PDB:1OAC}.
STRAND 110 112 {ECO:0000244|PDB:1D6Y}.
STRAND 116 118 {ECO:0000244|PDB:1OAC}.
HELIX 131 142 {ECO:0000244|PDB:1OAC}.
STRAND 152 159 {ECO:0000244|PDB:1OAC}.
HELIX 163 172 {ECO:0000244|PDB:1OAC}.
STRAND 181 188 {ECO:0000244|PDB:1OAC}.
STRAND 191 198 {ECO:0000244|PDB:1OAC}.
TURN 199 202 {ECO:0000244|PDB:1OAC}.
STRAND 203 210 {ECO:0000244|PDB:1OAC}.
HELIX 219 230 {ECO:0000244|PDB:1OAC}.
HELIX 233 241 {ECO:0000244|PDB:1OAC}.
HELIX 247 249 {ECO:0000244|PDB:1OAC}.
STRAND 250 255 {ECO:0000244|PDB:1OAC}.
TURN 261 264 {ECO:0000244|PDB:1OAC}.
STRAND 268 270 {ECO:0000244|PDB:1OAC}.
STRAND 272 279 {ECO:0000244|PDB:1OAC}.
STRAND 282 284 {ECO:0000244|PDB:1OAC}.
HELIX 286 288 {ECO:0000244|PDB:1OAC}.
STRAND 294 299 {ECO:0000244|PDB:1OAC}.
TURN 300 303 {ECO:0000244|PDB:1OAC}.
STRAND 304 310 {ECO:0000244|PDB:1OAC}.
STRAND 323 325 {ECO:0000244|PDB:1OAC}.
STRAND 337 339 {ECO:0000244|PDB:1OAC}.
STRAND 345 349 {ECO:0000244|PDB:1OAC}.
STRAND 352 355 {ECO:0000244|PDB:1OAC}.
STRAND 358 365 {ECO:0000244|PDB:1OAC}.
TURN 366 368 {ECO:0000244|PDB:1OAC}.
STRAND 369 379 {ECO:0000244|PDB:1OAC}.
STRAND 382 399 {ECO:0000244|PDB:1OAC}.
TURN 404 408 {ECO:0000244|PDB:1OAC}.
STRAND 410 412 {ECO:0000244|PDB:1QAF}.
HELIX 413 417 {ECO:0000244|PDB:1OAC}.
TURN 419 422 {ECO:0000244|PDB:1OAC}.
TURN 428 430 {ECO:0000244|PDB:1OAC}.
STRAND 437 444 {ECO:0000244|PDB:1OAC}.
STRAND 450 470 {ECO:0000244|PDB:1OAC}.
STRAND 478 493 {ECO:0000244|PDB:1OAC}.
STRAND 496 505 {ECO:0000244|PDB:1OAC}.
STRAND 510 518 {ECO:0000244|PDB:1OAC}.
STRAND 522 524 {ECO:0000244|PDB:1OAC}.
HELIX 535 538 {ECO:0000244|PDB:1OAC}.
TURN 539 541 {ECO:0000244|PDB:1OAC}.
STRAND 542 546 {ECO:0000244|PDB:1OAC}.
STRAND 549 552 {ECO:0000244|PDB:1OAC}.
STRAND 554 564 {ECO:0000244|PDB:1OAC}.
STRAND 568 582 {ECO:0000244|PDB:1OAC}.
STRAND 590 600 {ECO:0000244|PDB:1OAC}.
HELIX 603 606 {ECO:0000244|PDB:1OAC}.
STRAND 614 624 {ECO:0000244|PDB:1OAC}.
STRAND 630 643 {ECO:0000244|PDB:1OAC}.
HELIX 656 660 {ECO:0000244|PDB:1OAC}.
HELIX 662 665 {ECO:0000244|PDB:1OAC}.
STRAND 667 672 {ECO:0000244|PDB:1OAC}.
HELIX 694 697 {ECO:0000244|PDB:1OAC}.
TURN 698 700 {ECO:0000244|PDB:1OAC}.
STRAND 707 719 {ECO:0000244|PDB:1OAC}.
HELIX 723 725 {ECO:0000244|PDB:1OAC}.
STRAND 726 746 {ECO:0000244|PDB:1OAC}.
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


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