ID A6IP50_RAT Unreviewed; 1333 AA. AC A6IP50; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 29-MAY-2024, entry version 6. DE RecName: Full=aldehyde oxidase {ECO:0000256|ARBA:ARBA00013041}; DE EC=1.2.3.1 {ECO:0000256|ARBA:ARBA00013041}; GN Name=Aox1 {ECO:0000313|EMBL:EDL99010.1, ECO:0000313|RGD:620528}; GN ORFNames=rCG_22494 {ECO:0000313|EMBL:EDL99010.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:EDL99010.1}; RN [1] {ECO:0000313|EMBL:EDL99010.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL99010.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [2] {ECO:0000313|EMBL:EDL99010.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL99010.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F., RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH473965; EDL99010.1; -; Genomic_DNA. DR RGD; 620528; Aox1. DR Proteomes; UP000234681; Chromosome 9. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:TreeGrafter. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. 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}. FT DOMAIN 4..91 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 235..420 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000259|PROSITE:PS51387" FT ACT_SITE 1265 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1" FT BINDING 43 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 48 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 51 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 73 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 113 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 116 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 148 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 150 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3" FT BINDING 263..270 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 366 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 410 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 428 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 771 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 802 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 916 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 918 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2" FT BINDING 1083 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 1333 AA; 146898 MW; CFBB85D327B11F3F CRC64; MDPPQLLFYV NGQKVVENNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP STKSIRHHPV NACLTPICSL YGTAVTTVEG IGNTRTRLHP VQERIAKCHG TQCGFCTPGM VMSMYALLRN HPEPSLDQLT DALGGNLCRC TGYRPIIDAC KTFCRASGCC ESKENGVCCL DQGINGSAEF QEGDETSPEL FSEKEFQPLD PTQELIFPPE LMRIAEKQPP KTRVFYSNRM TWISPVTLEE LVEAKFKYPG APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELSIINQTG DGLTLGAGLS LDQVKDILTD VVQKLPEETT QTYRALLKHL RTLAGSQIRN MASLGGHIVS RHLDSDLNPL LAVGNCTLNL LSKDGKRQIP LSEQFLRKCP DSDLKPQEVL VSVNIPCSRK WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIKELSI LYGGVGPTTI GAKNSCQKLI GRPWNEEMLD TACRLVLDEV TLAGSAPGGK VEFKRTLIIS FLFKFYLEVL QGLKREDPGH YPSLTNNYES ALEDLHSKHH WRTLTHQNVD SMQLPQDPIG RPIMHLSGIK HATGEAIYCD DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQDTT TFGTETLLAT DKVHCVGQLV CAVIADSETR AKQAAKHVKV VYRDLEPLIL TIEEAIQHKS FFESERKLEC GNVDEAFKIA DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKHIQDIV AATLKLSVNK VMCHVRRVGG AFGGKVGKTS IMAAITAFAA SKHGRAVRCT LERGEDMLIT GGRHPYLGKY KVGFMRDGRI VALDVEHYCN GGSSLDESLW VIEMGLLKMD NAYKFPNLRC RGWACRTNLP SNTALRGFGF PQAGLVTEAC VTEVAIRCGL SPEQVRTINM YKQIDNTHYK QEFSAKTLFE CWRECMAKCS YSERKTAVGK FNAENSWKKR GMAVIPLKFP VGVGSVAMGQ AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELKM PMSSVHLRGT STETVPNTNA SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSVS LSAVGYFRGY ESNINWEKGE GHPFEYFVYG AACSEVEIDC LTGDHKNIRT DIVMDVGHSI NPALDIGQVE GAFIQGMGLY TIEELSYSPQ GILYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS KGLGESGVFL GCSVFFAIHD AVRAARQERG ISGPWKLTSP LTPEKIRMAC EDKFTKMIPR DEPGSYVPWN IPV //