ID A0A0J7AS58_COCIT Unreviewed; 665 AA.
AC A0A0J7AS58;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, 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 ORFNames=CIRG_00194 {ECO:0000313|EMBL:KMP00052.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP00052.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS028093; KMP00052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7AS58; -.
DR STRING; 404692.A0A0J7AS58; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
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:SF33; 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.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
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 TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 105..191
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 236..635
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 631..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 391
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 391
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 665 AA; 75054 MW; CDA399C97650D4B1 CRC64;
MSLHPFDPLT PGEIRLVVKI LEASFPGVPL RHKVIEVQEP IKKDVVPYLE AERLGQPLPA
KPARILTALF HRMDTKVFMK ALINAEKKSL LQCRELPKGV QGPTDVDEMI EMEKVCNDHP
AVKAEIAKMN LPPNVVVCND PWIYGTDSET EDRRLFQHYM YMCDVDHPQT NHYSLPCAFS
PVFDGMTKEL VRMDYLPTGT DHSFTSTKPW KPVKTVQYAH DLLDEPLRTD LKPYIVQQPE
GPSFKVDGNH VYWQKWRFRV GFNYRDGLVI YNVSYDRRNV FYRLSLCEMT VPYGDPRAPY
HRKQAFDVGD VGFGNTANQL SLGCDCLGHI KYFDGFRTDS KGNPVLLKNV ICLHEQDAGL
QHKHTNYRTN AATVVRNRQL VVQMICTVSN YEYIFAWIFD QAGGIELEVR ATGILSTMPI
DNEDGTKVPW GTNVGPGVMA AYHQHVFSMR VDPAIDGHNN TVVYSDSVAL PDEPNMNPYG
VGYAQETTVL KNSCSADLSV ENARVFKIRN DNVINPTSGN PVAYKLGVMP SQLMIMAERS
FNRRRAAFAT KPIWVTKYQD GELYSAGEFT NQSKKSSGVE LWSARNDNTE NTDVVLWHSF
ALTHNPRPED FPVMPVEKIS VTLKPDGFFE KNPALDVPPS DQSFNKSSLH QDEPACSGCP
ANSKL
//
