UniProt: A0A2K6UKR4

Database: UniProt
Entry: A0A2K6UKR4_SAIBB

LinkDB:  A0A2K6UKR4_SAIBB 
Original site:  A0A2K6UKR4_SAIBB

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (34)   
   InterPro (21)   
   Pfam (7)   
   PROSITE (4)   
   SMART (2)   
All databases (51)   

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ID   A0A2K6UKR4_SAIBB        Unreviewed;      1338 AA.
AC   A0A2K6UKR4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=aldehyde oxidase {ECO:0000256|ARBA:ARBA00013041};
DE            EC=1.2.3.1 {ECO:0000256|ARBA:ARBA00013041};
GN   Name=AOX1 {ECO:0000313|Ensembl:ENSSBOP00000032505.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000032505.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000032505.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate;
CC         Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240; Evidence={ECO:0000256|ARBA:ARBA00001403};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC         Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC         ChEBI:CHEBI:29067; EC=1.2.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000039};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000127-2};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000127-3};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   RefSeq; XP_003925726.1; XM_003925677.1.
DR   STRING; 39432.ENSSBOP00000032505; -.
DR   Ensembl; ENSSBOT00000049406.1; ENSSBOP00000032505.1; ENSSBOG00000032424.1.
DR   GeneID; 101033246; -.
DR   KEGG; sbq:101033246; -.
DR   CTD; 316; -.
DR   GeneTree; ENSGT00950000183114; -.
DR   OMA; QCRWKVG; -.
DR   OrthoDB; 5485853at2759; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:Ensembl.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR014313; Aldehyde_oxidase.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR   NCBIfam; TIGR02969; mam_aldehyde_ox; 1.
DR   PANTHER; PTHR11908:SF86; ALDEHYDE OXIDASE; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW   3}; Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000127-3};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW   3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220}.
FT   DOMAIN          5..92
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          236..421
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        1270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT   BINDING         44
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         52
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         74
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         114
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         117
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         149
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         151
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         264..271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         367
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         411
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         429
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         776
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         807
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         921
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         923
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         1088
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
SQ   SEQUENCE   1338 AA;  148172 MW;  616863D70FC1EAEB CRC64;
     MDRTPELLFY VNGRKVTEKN VDPETMLLPY LRRKLRLTGT KYGCGGGGCG ACTVMISRYN
     PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH PVQERIAKCH GTQCGFCTPG
     MVMSIYTLLR NHPEPTLDQL TDALGGNLCR CTGYRPIIDA CKTFCKTSGC CQSKENGICC
     LDQGINGLPE FEEGSETSPK LFTEEEFLPL DPTQELIFPP ELMIMAEKQP QRTRMFGSER
     MAWFSPVTLK ELLELKFKYP QAPVVMGNTS VGPEVKFKGV FHPVVISPDR IEELSVVIHA
     SNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYRALLKH LRTLAGSQIR NMASLGGHII
     SRHPDSDLNP LLAVGNCTLN LLSKEGKRQI PLDEQFLSKC PNADLKPQEI LISVNIPYSR
     KWEFVSAFRQ AQRQENALPI VNSGMRVFFG EEDGIIRELS ISYGGIGPTT ICAKDSCQKV
     IGRHWNEEML DTACRLVLNE VSLPGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKTNSV
     HYPSLADKYA SALEDLHSRH HCSTLKYQKI GPKQHPEDPV GHPIMHLSGV KHATGEAIYC
     DDMPPVDQEL FLTFVTSSRA HAKILSIDLS EALSMPGVVD IMTAEHLSDV NSFCFFTETE
     TFLATDKVFC VGHLVCAVLA DSEVQAKRAA KRVKIVYQDL EPLILTIEEA IQHNSFFKPE
     RKLEYGNVDE AFKVVDHILE GEIHMGGQEH FYMETQSMLV VPKGEDQEID VYVSTQFPKY
     IQDIVASTLK LPANKVMCHV RRVGGAFGGK AFKTGTIAAV TAFAANKHGR AVRCVLERGE
     DMLITGGRHP YLGKYKAGFM NDGRILALDM EHYSNAGTSL EESLFVIEMG LLKMDNAYKF
     PNLRCQGWAC RTNLPSNTAF RGFGFPQAGL ITESCIVEVA AKCGLSPEKV RMINMYKEID
     QTPYKQEINA KNLAQCWREC MAMSSYSERK VVVEKFNMEN YWKKKGLSMV PLKFPVGLGS
     RAAGQAAALV HIYLDGSVLV THGGIEMGQG VHTKMIQVAS RELRMPMSNV HLRGTSTETV
     PNANVSGGSV VADLNGLAVK NACQTLLKRL EPIISKNPKG TWKDWAQTAF NESISLSAVG
     YFRGYESDMN WEKGEGHPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPALD
     IGQIEGAFIQ GMGLYTIEEL NYSPQGVLHT RGPDQYKIPA ICDMPTQLHI SLLPPSQNSN
     TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RRERGLRGPL RLNSPLTPEK IRMACEDKFT
     KMIPRDEPGS YVPWNVPI
//

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