ID O65749_CICAR Unreviewed; 670 AA.
AC O65749;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1999, sequence version 2.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=LOC101491799 {ECO:0000313|RefSeq:NP_001265996.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|EMBL:CAA08855.1};
RN [1] {ECO:0000313|EMBL:CAA08855.1, ECO:0000313|RefSeq:NP_001265996.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9824285; DOI=10.1016/S0014-5793(98)01219-8;
RA Rea G., Laurenzi M., Tranquilli E., D'Ovidio R., Federico R., Angelini R.;
RT "Developmentally and wound-regulated expression of the gene encoding a cell
RT wall copper amine oxidase in chickpea seedlings.";
RL FEBS Lett. 437:177-182(1998).
RN [2] {ECO:0000313|RefSeq:NP_001265996.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000672};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000256|RuleBase:RU000672};
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC ECO:0000256|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
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DR EMBL; AJ009825; CAA08855.1; -; mRNA.
DR RefSeq; NP_001265996.1; NM_001279067.2.
DR STRING; 3827.O65749; -.
DR PaxDb; 3827-XP_004508350-1; -.
DR GeneID; 101491799; -.
DR KEGG; cam:101491799; -.
DR eggNOG; KOG1186; Eukaryota.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000087171; Chromosome Ca7.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 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; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638:SF68; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE 2: Evidence at transcript level;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001265996.1};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..670
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001265996.1"
FT /id="PRO_5017842462"
FT DOMAIN 29..114
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 122..214
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 244..655
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 408
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 408
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 670 AA; 75739 MW; 09ADB4D7AFD95396 CRC64;
MASTTIKLSF FFAITLIFLQ AVTPLNLQHP LDPLTKEEFS IVQTVVLHKY PTSKNSVAFH
YIGLDDPDKD DVLKYETQPT LITIPRKSFV VAIINSQNHE IVIDLRLKTI VSDNIHKGYG
FPILSADEQG VAIKLPLKYP PFIASVNKRG LNLSEIVCST FSMGWFGEEK NSRTVRVDCF
MKENTVNIYV RPISGITIVV DLQLMKIVEY NDRGIEAVPT AEKTDYRFSH QNPPFGPKLN
SLVSHQPQGS GAHINGYSVS WANWRFHIGF DARAGIVISL ASIYDLEKHK SRRVLYKGYI
SELFVPYQDP TEEFYFKTFF DSGEFGFGLS TVSLIPNRDC PSHAQFIDTY IHSADGSPIL
LKNAICVFEQ YGNIMWRHTE TGIPNEFPEE SRTEVNLIVR TVVTVGNYDN VLDWEFKTSG
SIKPAIALSG ILEIKGANIK HKDEIKEDQY GTLVSANSIG IYHDHFYMYY LDFDVDGVNN
SFEKTSLKTV RITDGSSKRK SYWTTETQTA KTESDAKITI GLSPAELVVV NPNKKTAVGN
DVGYRLIPAI PAHPLLTEDD YPQIRGAFTN YNVWVTPYNR TEKWAGGLYV DHSRGDDTLA
VWTQKNRDIE NKDIVLWHVV GIHHVPAQED FPIMPLLSTS FELRPTNFFE RNPVLNTLSP
RDVNWPGCSN
//
