ID A0A0B4E0D4_9RHOB Unreviewed; 765 AA.
AC A0A0B4E0D4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:KID10896.1};
GN ORFNames=GC1_04320 {ECO:0000313|EMBL:KID10896.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID10896.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID10896.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID10896.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
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:KID10896.1}.
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DR EMBL; AFCF02000001; KID10896.1; -; Genomic_DNA.
DR RefSeq; WP_019295575.1; NZ_AFCF02000001.1.
DR AlphaFoldDB; A0A0B4E0D4; -.
DR STRING; 1002340.GC1_04320; -.
DR eggNOG; COG1529; Bacteria.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000031201; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron 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 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 20..140
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 765 AA; 82399 MW; CE9EE8D91C4C1861 CRC64;
MDKFGKSQPV KRVEDVRFLT GQGNYVEDAA PADALRAWVL RSPVAHGVIT ALHTEDALEA
EGVHAVITLA DLEAAGINVS MDGTTVKNRD GTDGASPERP MLARNKVRYV GEPVAVVVAE
TLDQARDAGE LIELEIGDLP VKLDLHPGGE ALHGSVPDNK AFDWGMGDEA ATAEAFRTAA
HTVALQVEDN RIMVSTMEPR GCFAEWQQGR LHFTFGGQGV WGMKSQLASK LGLNEDDIKV
TTPDVGGGFG MKAFAYPEYF AVAHAATVLS RPVFWMSDRS EAMLSDNGGR DLTSLAELAF
DEDLKITAYR VSTRCNLGAY NAHFGQPIQT QLFSRVLAGV YDIQTAWLQV EGIYTNTTQV
DAYRGAGRPE AIYVLERVMD RAARELGVDP LELRRRNFIK PAAFPYGTVT GETYDVGDFD
KVLTRAAKEA DLKGFAARRA ENGKRGKYRG VGVCYYIESI LGDPSEGAEV EFLEDGRVNI
YVGTQSNGQG HETVYAQFLA DQSGIPAEMI QVIQGDSDRI AQGGGTGGSR SVTTQANATL
AAVETMIAAF ISFLAEEMGV EEDAVEFDGD TFRAPGSNLT PTMLEAAEMA RAQGRTDLQR
HAARARLPGR SFPNGAHIAE IVIDPETGQA DVERYTVVDD FGNLINPMLA EGQVHGGVAQ
GLGQAMLERV VYDEDGQLLT ASFMDYALPR ASGVPMIGFT SEPVPSTQNP MGMKGCGEAG
TVGALAAVAN AVQDAVWDRG VRQVDMPFTP LRIWEVLRDV SEAAE
//
