ID A0A1S3EFT7_CICAR Unreviewed; 747 AA.
AC A0A1S3EFT7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=LOC101511923 {ECO:0000313|RefSeq:XP_012573826.1};
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_012573826.1};
RN [1] {ECO:0000313|RefSeq:XP_012573826.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012573826.1};
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_012573826.1; XM_012718372.2.
DR AlphaFoldDB; A0A1S3EFT7; -.
DR GeneID; 101511923; -.
DR OrthoDB; 34972at2759; -.
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:SF18; 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.
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 55..144
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 180..283
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 309..717
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 471
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 471
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 747 AA; 83486 MW; C5CE8F6018FCF137 CRC64;
MATVEEKTTP PCCSLQNNNK SAAAASSTVD SRSDPPPKSP SAKGITVMAK AQTCHPLDPL
SAAEISVAIA TVRAAGATPE VRDSMRFIEV DMVEPEKHVV ALADAYFFPP FQPSLLPRTK
GGPVIPSKLP PRKARLVVYN KKSNETSIWI VELTEVHATT RGGHHRGKVI SSTIVPDVQP
PMDAVEYAEC EAVVKNYPPF QEAMKKRGIE DMDLVMVDPW CAGYDSEADA PSRRLAKPLF
FCRTESDCPM ENGYARPVEG IHVLVDMQNM VVLEFEDRKL VPLPPADPLR NYTSGETRGG
VDRSDVKPLQ IIQPDGPSFR VNGHFIQWQK WNFRIGFTPR EGLIIYSVAY IDGSRGRRPV
AHRLSFVEMV VPYGDPNDPH YRKNAFDAGE DGLGKNAHSL KKGCDCLGYI KYFDAHFTNF
YGSVETIENC VCLHEEDHGM LWKHQDWRTG LAEVRRSRRL TVSFICTVAN YEYGFYWHFY
QDGKIEAEVK LTGILSLGAL QQGETRKYGT TIAPGLYAPV HQHFFVARMD MAVDCKPGEA
FNQVVEVNVK IEEPGKNNVH NNAFYAEEKP LKSELEAMRD CDPLSARHWI VRNTRSVNRT
GYLTGYKLVP GANCLPLAGS EAKFLRRAAF LKHNLWVTPY ARGEMYPGGE FPNQNPRDGE
GLATWVKQNR PLEEADVVLW YVFGVTHIPR LEDWPVMPVE HIGFMLMPHG FFNCSPAVDV
PPSPSDLDDK ENGMPAKPSQ NGLIAKL
//
