ID A0A1Y6IWD3_9VIBR Unreviewed; 832 AA.
AC A0A1Y6IWD3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Xanthine dehydrogenase molybdenum-binding subunit {ECO:0000313|EMBL:SMS00792.1};
DE EC=1.17.1.4 {ECO:0000313|EMBL:SMS00792.1};
GN Name=xdhA {ECO:0000313|EMBL:SMS00792.1};
GN ORFNames=VIM7927_02063 {ECO:0000313|EMBL:SMS00792.1};
OS Vibrio mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=474394 {ECO:0000313|EMBL:SMS00792.1, ECO:0000313|Proteomes:UP000196125};
RN [1] {ECO:0000313|EMBL:SMS00792.1, ECO:0000313|Proteomes:UP000196125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7927 {ECO:0000313|EMBL:SMS00792.1,
RC ECO:0000313|Proteomes:UP000196125};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FXXI01000003; SMS00792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6IWD3; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000196125; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
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;
KW Oxidoreductase {ECO:0000313|EMBL:SMS00792.1}.
FT DOMAIN 37..144
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 160..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 91257 MW; 24CDC53A6D3A59D8 CRC64;
MRKLISHPYT AQHLQSQKTL ETVGQPFPHE SAGKQVAGEA LFVDDYPEPR GCLHGALITS
DIAKGTMTHL DLSDVRQSPG VVRVITCHDI PGLNDIGTIH KGDPLLCQGE IRYFRQPIAF
VIAETHQLAC QAAQKALIEY EETSDPVISY QQASQRDHLL PPHQMGTSLQ GQTPEDASLR
GQSPEGTLRI QGDLAVGGQE HFYLESQISL AELTEDGGIF VRTSTQNPTE VQNLIAEVLG
IPFNHVTVDM RRMGGGFGGK ETQAAPWACL ASLGTILTKK AVKFRLPRAI DMSTTGKRHP
FFNRYALTAT DDGEILSADI EVNGLCGHSA DLSDAIVDRA MFHADNAYFL GDACITGNRL
KTDTVSHTAF RGFGGPQGMI VIEKAMQDLG VTLRQDPLDL RLKNLYRPGK SVTPYGMEVE
QTQELREVLT RLEASSDYRQ RRQQIHEWNQ NSPILKKGLA LTPVKFGISF TATHLNQAGA
LIHIYTDGTV QVSHGGTEMG QGLHTKIQQI VAQTFGIPMD WILVTSTRTD KVPNTSPTAA
SSGADLNGMA AHNAAMTIKE RLLDFATAHY CSQSHSSECL SSQSSSQSNF GRLSSQPSAT
QPEIKDGKLY YDSGEVDWAT LIQQAYLNRV SLSSTGYYST PKIGYDRTKA NGRPFFYFAI
GASCSEVMID TLTGEMTVER VDILHDVGNS LNPAIDIGQI EGAYIQGLGW LTTEELIWNE
HGHLLSNSPM NYKIPSICDY PKQMNITLYD VPNPEHSIYR SKAVGEPPFM HAISTWCAIY
DAIAAISDHQ MIPELDTPAT GERILTACQQ QYDWLEQGGQ APNQPAETIG NR
//
