UniProt: A0A150X4P8

Database: UniProt
Entry: A0A150X4P8_9BACT

LinkDB:  A0A150X4P8_9BACT 
Original site:  A0A150X4P8_9BACT

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Ontology (4)   
   GO (4)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (19)   
   Pfam (7)   
   PROSITE (3)   
All databases (35)   

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ID   A0A150X4P8_9BACT        Unreviewed;      1512 AA.
AC   A0A150X4P8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:KYG73582.1};
GN   ORFNames=AWW68_12895 {ECO:0000313|EMBL:KYG73582.1};
OS   Roseivirga spongicola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC   Roseivirga.
OX   NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG73582.1, ECO:0000313|Proteomes:UP000075606};
RN   [1] {ECO:0000313|EMBL:KYG73582.1, ECO:0000313|Proteomes:UP000075606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG73582.1,
RC   ECO:0000313|Proteomes:UP000075606};
RA   Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT   "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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:KYG73582.1}.
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DR   EMBL; LRPC01000028; KYG73582.1; -; Genomic_DNA.
DR   RefSeq; WP_068222051.1; NZ_LRPC01000028.1.
DR   STRING; 333140.AWW68_12895; -.
DR   OrthoDB; 9759099at2; -.
DR   Proteomes; UP000075606; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; 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   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 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; 4.
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.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075606}.
FT   DOMAIN          3..91
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          283..489
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1512 AA;  168253 MW;  F60C71B2F9B8B042 CRC64;
     MSNQVSFFLN GQQVVLEDPS PKLLLIDFLR SPEIGLTGAK KGCGQGGCGA CTVIMSSWNK
     EKKEVEHKSI NSCLRPVCSL GGLSITTVEG TGGTKRPENK HLTFTLPASR GVAPGAIQPT
     DHWNESKSNL LEHQEKKKSL VRSSLEKIRD AKGLEHVLVG DENLHEIHEG MNPVAHRLAI
     NNGSQCGYCT VGFVMNMSAF LAQNPSPTKQ QIEEAFDGNI CRCTGYRAIL TGMKTFASDW
     TEEDEKERMK CLTEDKCDQV LVHDQVKIPF PEAAKAPLPD TKILESQCDW VTPRTLDELK
     RIMRKNPGET TRIVFGNTSF GIYADEYPQV KLMVDIKLIE ELKGIKQTKD GISFGATTTY
     SELFDFLENL NPEPTSRLGA SLYMVHRTAG MIVRNAASVA GNTMLVLKHL MQGEPFPSDL
     FTALDGNDAT ITYLKVSTGR TTEDHVDELV RKLRRTPSLA DDIIILRYFI PQGKGEEVVL
     SQKVSIREVN SHSIVNSTIR LELGKDLKVD EASIVFGGIA PITWHARNSE RWLKGKKLSL
     DLLPRLLGIV RREVIKELAY WEEKGRSNGL PSEGFTDEYR VKLAMSYIYK AIVRAIVEKK
     PKEIPENISS AAKIDWGNWG VSKGTQHYTI QDFKAPVSQP YIKLMAFHQA MGEVHYTHEI
     ELPPIGQNGA FIQSQRTLAL YHFINPETKA QIDRDQLADY LEDKFEGFYA LINHEDIPPG
     GVNLQGMGAD QPIFAVDQIL YPGQAIAMVI AESEQLAIEI AEFASSNCLA YKPINWQKGW
     EKPIMSIDEA IEKESIFPDC PKSSPFVTHI WKITRPGTEL YWTNENKKPL DKKPVKRKTK
     VDGNNCLVIE NTQVSGEQIH FYMETQSCVA IPEDDNQILI HPSSQSPMEM HQTAAISLAA
     EHNKVNIDVR QLGGGYGGKT EQAKFVIGPV AVAAKALNIP IRMALKREHD TAMIGKRHGY
     YGQYQIAVDQ GDIREEDKGI IRGLLVKLWG DGGAFYDCSF VVSNCIQLRL DNAYLIKNFE
     SQLDVCRTNK APNTAMRAFG DIQGKLILEN AVDDAAFSVG MDPYDLRLKN MYQRGDVTPF
     GQALSYCYMR DVWKYIEEKS DYRARVKKVE EFNKNNKWKK RGIYAIPVKY GSGYNLVMLE
     QAAAIVSIYS GDGSISINQG GVDMGQGMMT KVEQIASYIL NVPMELIQIH KPSTKVIPNP
     SSTGGSTGTA YNGEAVKQAC EKMRQRLMEF GQKLLKENGE DWCKAQGIDY WNYGKEGWSA
     NVIRPNVDKH PRLIWQNLVG LAYQYRIDLI AAFTAPIPGG TTPVPAMTFK PIDQQKEIPG
     IELAPVQSTA GVVDSFVGWT FSAACSEVEV DVLTGEVKIL KSDIVFDMGW SLNPAIDIGQ
     VEGAFVQGVG YVTTEKLVFQ PDGEEVGRLN TLNTWRYKPP AVTSIPLEMN TYLYPRNNSS
     EVPENPNELM SSKEVGEPPL VLASSVFFAI KAAVRASRLE RGHSGLFKLD APATVQEVNL
     ALDVTDRDLK SI
//

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