ID A0A125PIG2_9BASI Unreviewed; 803 AA.
AC A0A125PIG2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=RHOSPDRAFT_34150 {ECO:0000313|EMBL:KWU44359.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44359.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44359.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44359.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ954480; KWU44359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125PIG2; -.
DR STRING; 1305733.A0A125PIG2; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000062823; 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; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015328; DUF1965.
DR PANTHER; PTHR10638:SF20; 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; PF09248; DUF1965; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
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:UP000062823};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..803
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007178608"
FT DOMAIN 86..163
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 251..320
FT /note="DUF1965"
FT /evidence="ECO:0000259|Pfam:PF09248"
FT DOMAIN 332..734
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 405
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 486
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 486
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 803 AA; 90000 MW; E3EAD6B908722739 CRC64;
MRAGLALGTL IALGSAVCAA PAPPLERRKL PVFKNRFVTS RPAIHNYVTD VSGAQYNLTD
IPDVPTVNAP YPNVWAGLSI DEAAGVVNFL HNHTDLNLTA AADAGSWDNV ITNLDLAAPN
KTEVMAFKAG KCDEPPRMAQ VTIMFSACDE PFLEDYLVGP LPVSENTTAV PYSYRTTKGT
SRITNYDADA DKTQDFIVTT AQTCDDIITD LLGAPADSWD IWGFDPLWHE DGRVINWVGF
WGIPETVFDG ETLLPQGLYM KFDVTGRDPS QWSFLGWLHD YVFYPTTADF RHAWENGKIN
KTVRNAGMNE TWIGTDRTGP ELPYDNRAPP VQIAPGGQRF AVDVENQYAT WMDFSFFYSF
RRDSGLRLWD IKYKNETVMY ELGLNEALAH YAGNDPVQSG TAYLDTYYGF GPYAFELIPD
FDCPTHAFYA NTTFHANEVS TTHRRSICFF EDTASFPMQR HANGNYIAAT KNVAFKMKSA
STVGNYDYSF IYSFMLDGSI SVEVMASGYI QSAYYAQNGE YGYQIHDGLS GSMHDHVLNW
KADLDILGTK NTVGMHTIEP KTVKYVWDNS TRNTMHLVRS ELKNEDNATL HWPENSHSMF
LIYNKEEKNK YGEERAWRMM PHIGGAGMHA TIQNSTNLGP SMNFAKAPIY VTKQHDSEFT
SAHASNNYDT FDPIIDFEKY LDGENLEQED LVIWFNLGMH HVPHTGDLAN TVHTTAHAGM
LFSPSNYLLG NPALQSSQMI RMNYNSSASD IVEEVLTFGG QSASGMFNLT AIQPDYYSYE
GDSNTRKFPY DPLHPYNDTV AIV
//
