ID A0A0D8CPW6_9GAMM Unreviewed; 793 AA.
AC A0A0D8CPW6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KJE38603.1};
GN ORFNames=SG35_24860 {ECO:0000313|EMBL:KJE38603.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE38603.1};
RN [1] {ECO:0000313|EMBL:KJE38603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE38603.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJE38603.1}.
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DR EMBL; JYNI01000059; KJE38603.1; -; Genomic_DNA.
DR RefSeq; WP_053043340.1; NZ_CP059735.1.
DR AlphaFoldDB; A0A0D8CPW6; -.
DR STRING; 485447.SG35_24860; -.
DR PATRIC; fig|485447.4.peg.5466; -.
DR OrthoDB; 9758509at2; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 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; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su.
DR NCBIfam; TIGR02965; xanthine_xdhB; 1.
DR PANTHER; PTHR11908:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 38..145
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 86314 MW; ADAE27FD52D14B2D CRC64;
MRSLKKVEQQ SARESIQDPG MGGVGRSKKH ESADKHVSGE AVYIDDRPEL RGQLHAAVGQ
SQFARARIKS MDLSAVKAAE GVKAVITVKD VPGHVDIGPV FPGDPVLALD EVEYLGQPLF
AVAATSHDLA RKAALLAKVE YEELEPVLTV KDALAKQHFV RPPFTMQRGD SAAAIDSAKH
VLSGEISVGG QEHFYLEGQV STAEPTEDGG MTIFSSSQHP SEVQKLVAEV LDVPLNKITV
DTRRMGGGFG GKETQAAPWA CIAALLANKC QLPVKMKLSR SDDMCLTGKR HPFENNYQVG
FDDSGRIQGI DITVNGNCGY SPDLSDAIVD RAMFHSDNAY YLDNATVTGN RCKTNTVSHT
AYRGFGGPQG MMTIEMVMDD IARHLGKDPL EIRKINLYGH GERNITHYHQ TVEHNNLDKL
IDSLEQSSDY QARRKQISEF NKENTILKKG IALTPVKFGI SFTVQHLNQA GALVHIYTDG
TIHLNHGGTE MGQGLFTKVA QIVAEEFQVD VDTIGVSATR TDKVPNTSPT AASSGTDLNG
KAAQNAAITL KKRLVDFAAE HFNVETEQVI FADNQVHIGA EVGKKTMAFA ELIQLAYMNR
VSLSSTGYYK TPKIHFDRET AKGRPFFYYA NGAAVSEVLI DTLTGEYKLL RADILHDVGK
SLNPSIDIGQ IEGAFIQGMG WLTTEELMWN DKGRLLSNNP ATYKIPAISD APVDFNVALL
PDDPNKEHTV YNSKAVGEPP FMLGISVWSA IKDAVASVAD YQVSPKLNTP ATPEKVLWAV
QDMQKAALDK SGA
//
