AMOH_ARTGO
ID AMOH_ARTGO Reviewed; 684 AA.
AC Q59118;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Histamine oxidase;
DE EC=1.4.3.22 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Copper amine oxidase;
OS Arthrobacter globiformis.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP TOPAQUINONE AT TYR-402.
RC STRAIN=ATCC 8010 / DSM 20124 / BCRC 10598 / JCM 1332 / KCTC 9101 / NBRC
RC 12137 / NCIMB 8907 / NRRL B-2979 / 168;
RX PubMed=7876243; DOI=10.1074/jbc.270.9.4712;
RA Choi Y.-H., Matsuzaki R., Fukui T., Shimizu E., Yorifuji T., Sato H.,
RA Ozaki Y., Tanizawa K.;
RT "Copper/topa quinone-containing histamine oxidase from Arthrobacter
RT globiformis. Molecular cloning and sequencing, overproduction of precursor
RT enzyme, and generation of topa quinone cofactor.";
RL J. Biol. Chem. 270:4712-4720(1995).
CC -!- FUNCTION: Oxidizes histamine. Other amines including phenethylamine,
CC tyramine, tryptamine, putrescine, and benzylamine also serve as
CC substrate.
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; Evidence={ECO:0000250|UniProtKB:P19801};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + histamine + O2 = H2O2 + imidazole-4-acetaldehyde +
CC NH4(+); Xref=Rhea:RHEA:25625, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27398, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58432; EC=1.4.3.22;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P46883};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By histamine.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; D38508; BAA07517.1; -; Genomic_DNA.
DR PIR; A56102; A56102.
DR AlphaFoldDB; Q59118; -.
DR SMR; Q59118; -.
DR BindingDB; Q59118; -.
DR ChEMBL; CHEMBL3988597; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052598; F:histamine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR GO; GO:0097185; P:cellular response to azide; IDA:UniProtKB.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
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; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE 1: Evidence at protein level;
KW Copper; Cytoplasm; Direct protein sequencing; Disulfide bond; Manganese;
KW Metal-binding; Oxidoreductase; TPQ.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..684
FT /note="Histamine oxidase"
FT /id="PRO_0000064109"
FT REGION 647..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 402
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 316..327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 399..404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 451
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 453
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 460
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 590
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 601
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 601
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 612
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 402
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:7876243"
FT DISULFID 337..363
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 684 AA; 75111 MW; 4D6047F132A30CC7 CRC64;
MTLQTTPSTP LVQDPPVPAT LVHAAAQHPL EQLSAEEIHE ARRILAEAGL VGESTRFAYL
GLIEPPKTTR QGDVTGAARL VRAMLWDAAQ SRSLDVRLSL ATGLVVDRRE LNPEADGQLP
VLLEEFGIIE DILSEDPQWN AALTARGLTP AQVRVAPLSA GVFEYGNEEG KRLLRGLGFR
QDHPADHPWA HPIDGLVAFV DVENRRVNHL IDDGPVPVPE VNGNYTDPAI RGELRTDLLP
IEIMQPEGPS FTLEGNHLSW AGWDLRVGFD AREGLVLHQL HHSHKGRRRP VIHRASISEM
VVPYGDPSPY RSWQNYFDSG EYLVGRDANS LRLGCDCLGD ITYMSPVVAD DFGNPRTIEN
GICIHEEDAG ILWKHTDEWA GSDEVRRNRR LVVSFFTTVG NYDYGFYWYL YLDGTIEFEA
KATGIVFTAA LPDKDYAYAS EIAPGLGAPY HQHLFSARLD MMIDGDANRV EELDLVRLPK
GPGNPHGNAF TQKRTLLARE SEAVRDADGA KGRVWHISNP DSLNHLGHPV GYTLYPEGNP
TLAMADDSSI ASRAAFARHH LWVTRHAEEE LYAAGDFVNQ HPGGAVLPAY VAQDRDIDGQ
DLVVWHSFGL THFPRPEDWP IMPVDTTGFT LKPHGFFDEN PTLNVPSSAA GHCGTGSERE
HAAPGGTAVG HSGPDTGGQG HCGH
