ID A0A1S2XIA4_CICAR Unreviewed; 761 AA.
AC A0A1S2XIA4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=LOC101507021 {ECO:0000313|RefSeq:XP_004489782.1};
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|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004489782.1};
RN [1] {ECO:0000313|RefSeq:XP_004489782.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004489782.1};
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 RefSeq; XP_004489782.1; XM_004489725.3.
DR AlphaFoldDB; A0A1S2XIA4; -.
DR STRING; 3827.A0A1S2XIA4; -.
DR PaxDb; 3827-XP_004489782-1; -.
DR GeneID; 101507021; -.
DR KEGG; cam:101507021; -.
DR eggNOG; KOG1186; Eukaryota.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000087171; Chromosome Ca2.
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; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638:SF90; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 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.
PE 3: Inferred from homology;
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 TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 194..297
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 323..731
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 485
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 485
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 761 AA; 85057 MW; 17FDA69BD4B8F920 CRC64;
MASAQEKATP PNNSPSSSAP PPPPPPSSTW PDPTQDPTRN TTSLDSFPPK TTPTTKGIPV
MMRAQTCHPL DPLTAAEISV AVATVRAAGA TPEVRDSMRF VEVVLVEPVK QVVALADAYF
FPPFQPSLLP RTKGGGPLIP TKLPTRKARL VVYNKKSNET SIWIVELREV HAATRGGPHR
GKVISSQVVP NVQPPMDAME YAECEAVVKD FPPFREAMKR RGIEDMDLVM VDAWCVGYHS
EADSPNRRLA KPLIFCRSES DCPMENGYAR PVEGIYVLVD MQNMVVLEFE DRKLIPLPPT
DPLRNYTSGE TRGGVDRSDV KPLQIIQPEG PSFRVNGHFI QWQKWNFRIG FTPREGLVIY
SVAYIDGSRG RRPVAHRLSF VEMVVPYGDP NDPHYRKNAF DAGEDGLGKN AHSLKKGCDC
LGYIKYFDAH FTNFTGGVET IENCVCLHEE DHGILWKHQD WRTGLAEVRR SRRLTVSFIC
TVANYEYGFF WHFYQDGKIE AEVKLTGILS LGAMQPGEAR KYGTTIAPGL YAPVHQHFFV
ARMDMSVDCK PGEAFNQVVE VDVKVEDPGK NNVHNNAFYA EEKLLKSELE AMRDCNPLSA
RHWIVRNTRT VNRTGQLTGY RLVPGSNCLP LAGSEAKFLR RAAFLKHNLW VTPYVHNEMH
PGGEFPNQNP RVGEGLATWV KQNRSLEEAD IVLWYVFGVT HIPRLEDWPV MPVEHIGFML
MPHGFFNCSP AVDVPPSAGD LDDKENVMSA KPIQNGLIAK L
//
