ID A0A396U5V5_9GAMM Unreviewed; 1506 AA.
AC A0A396U5V5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Xanthine dehydrogenase {ECO:0000313|EMBL:RHW77857.1};
GN ORFNames=D1094_02720 {ECO:0000313|EMBL:RHW77857.1};
OS Colwellia sp. RSH04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=2305464 {ECO:0000313|EMBL:RHW77857.1, ECO:0000313|Proteomes:UP000266369};
RN [1] {ECO:0000313|Proteomes:UP000266369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSH04 {ECO:0000313|Proteomes:UP000266369};
RA Meng X.;
RL Submitted (SEP-2018) 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 -!- 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:RHW77857.1}.
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DR EMBL; QXIO01000001; RHW77857.1; -; Genomic_DNA.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000266369; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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 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; 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; 3.
DR SMART; SM01008; Ald_Xan_dh_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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266369};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT DOMAIN 3..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 278..476
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1506 AA; 166169 MW; B5A2CA5BC7C12636 CRC64;
MSNTVSFYLN GQSVSIENPS PNLLLIDYLR SPQVSLAGAK KGCGEGGCGA CTVILSRWDE
ESKQPEHRSI NSCLRAVCSL QGLSVTTVEG TGASRRPPPA FPKQSLAGAR AGAPLEGAVS
KHLRNAQKKG LEIRVNSLLE GNHGAESKPL QSVDIDNLPE IDTSINPVAY RLAVNNGSQC
GYCSTGFVMN MSAFLANTPE PTKKQIEQAF DGNICRCTGY RPILTAMKTF AIDWSEADEA
NRMKLLVDDQ VKAQHVGDTV SIPYPKEAKG NKIDGVEING NEQQWRTPKH IGELLEFYQE
NSYKDIYLLH ANTSYGVYTD DFVSHKYLVD ISQLKELYTI ENEGKFLRVG AGKTYTEVLK
HLDNIIDKES LSQTTAIGAL QFMAHRTAGT IIRNAASLGG NTMLVLKHIC KGTGEPFPSD
LFTVLSALGT ELIYIDLQTG EKHSAIANEL ALQVEKDQSL ANHILLVEYK IPVKSDDYAF
EVVQPHKVAL RDINAHSIVN STSILALSDK LTVEKVNLTY GAIAPYPWRA KVTEKLMKGS
CLSLENFPKY AESLSIEVEE ELIRWKERMS GLKDEGFTDS YKIELATAFL YKSMVTALLE
ASPESVPENQ RSAGKITWGH WPVSDGSQNY TNQSYKAPIS QPYVKLMALY QTSGQVRYTH
EMEVPPTTVN ASFVQSQRAL ANFAYCDPKT KESPISIEAL SVKLKEIFPQ FIRLVTEKDT
PRAGVKDVGI GGDQPVFAKE RVSYVGQSIA LAIAVEEKQA NIIAQYISDN CIAYTDVDWA
PEWQSPVLTL EDAIKRGSIF PDFPASAPFY NHIWQVVRNH SHFGWTTENK DPLDTNIVQR
EVELGGNQCK VIESTQTCGG QIHFYMETQS CVALPGEAEN MTFHPSSQSP MEMHQTAAAV
LGVEHNSVDV GIRQLGGGYG GKTEQAKFVI GATAVAAKAM EKPVRLIMPR ANDTSMIGKR
HPYYGQYQIA IDDGTTNTDD KGIIRGVDYN FFGDGGAFYD CSFIVSNCLQ TRVDNAYMID
NFKSQLDVCR TNTAPNTAFR SFGDIQGKLI SENAIDDAAF SIGMDPIDVR EKNLYKRGDV
TPYGQALSYC YMREVWDYLK VKSDVIGRRA EVAEFNKNNK WRKRGLYMLP VKYGSGYNLV
QLEQASAMVS VYSGDGTIVI NQGGVDMGQG MVTKLEQIAA YILNVPMDMI RIQLPKTDVI
PNPTSTGGST GTAYNGLAVK QTCEKMRSRL LEFGYDMLKE KGNDWCNEQN IDFWNYGEQG
WSAQVEKFGK PVLIWQNLIA LANQKRISLV ETFNAKIPGG ETAVPNLVFK TLEQQKAIPG
IEVAETAIPG GFDSFCGFTY SAACSEVEVD ILTGEVKIIR SDLMYDMGWS INPALDIGQV
EGAFIQGVGY VMTEKLVFEP KGEDQGRLNT VNTWRYKPPG ITNVPLEMNV HLFPRDKAEN
VPENPNDLLS AKEVGEPPLV LASSVFFAIK AAIRESRVER GLSGLFQLDA PATVQEVRKA
LAVDLK
//
