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Database: UniProt
Entry: Q72BS5_DESVH
LinkDB: Q72BS5_DESVH
Original site: Q72BS5_DESVH 
ID   Q72BS5_DESVH            Unreviewed;       906 AA.
AC   Q72BS5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   SubName: Full=Aldehyde oxidoreductase {ECO:0000313|EMBL:AAS96037.1};
DE            EC=1.2.-.- {ECO:0000313|EMBL:AAS96037.1};
GN   Name=mop {ECO:0000313|EMBL:AAS96037.1};
GN   OrderedLocusNames=DVU_1559 {ECO:0000313|EMBL:AAS96037.1};
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882 {ECO:0000313|EMBL:AAS96037.1, ECO:0000313|Proteomes:UP000002194};
RN   [1] {ECO:0000313|EMBL:AAS96037.1, ECO:0000313|Proteomes:UP000002194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC   {ECO:0000313|Proteomes:UP000002194};
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA   Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA   Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA   Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA   Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA   Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   EMBL; AE017285; AAS96037.1; -; Genomic_DNA.
DR   RefSeq; WP_010938851.1; NC_002937.3.
DR   RefSeq; YP_010778.1; NC_002937.3.
DR   AlphaFoldDB; Q72BS5; -.
DR   SMR; Q72BS5; -.
DR   STRING; 882.DVU_1559; -.
DR   PaxDb; 882-DVU_1559; -.
DR   EnsemblBacteria; AAS96037; AAS96037; DVU_1559.
DR   KEGG; dvu:DVU_1559; -.
DR   PATRIC; fig|882.5.peg.1436; -.
DR   eggNOG; COG1529; Bacteria.
DR   eggNOG; COG2080; Bacteria.
DR   HOGENOM; CLU_001681_2_3_7; -.
DR   OrthoDB; 9775084at2; -.
DR   PhylomeDB; Q72BS5; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 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   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   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 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   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AAS96037.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002194}.
FT   DOMAIN          2..79
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   906 AA;  97449 MW;  0AD6DE8BDF75A6BC CRC64;
     MIKRMVTING APRMAITRPD TTLATYLRES LGLTSVKVGC GQGHCGSCNV IVDGKLVRSC
     SYKMSRLTEG ATITTLEGIG TPDNLHPLQV AWMAHGAAQC GFCSPGFIVS AKALIDTNPK
     PSRDDVRDWF QKHRNACRCT GYKPLVDAVM DAAAVVRGEM KVDDLLYRIP ADGRIWGTKY
     PRPSALAKVT GTLDFGADLG IKMPEETLRC ALVQAEASHA KILGIDTSEA EKMPGVFKVV
     THKDIKGKNR ITGLITFPSN KGDGWDRPIL CDEKVFQYGD AIAIVCADTE EHAKAAAAAV
     KVDLEVLPAY MSAPAAMADD AMEIHPGTPN VYFEQHLVKG PETKPIFDKA DVVVEDDFYV
     GRQPHMPIEP DVGFAFFNED GKLCIHSKSI GLHLHLYMIA PGLGIEPDNI IMVQNPTGGT
     FGYKFSPTME ALVGAAAMAT GRPVFLNYSW YQQQTYTGKR SPFFINLRYA ATREGKLLAM
     ESDWSVDHGP YSEFGDLLTL RGAQFIGAGY DIPSIRGLGR TVCTNHAWGS AFRGYGSPQS
     EFASEVLMDE LAEKLGIDPL ELRYRNVYRE GATTPTGQVP EVLSLPELLD TARPRYLAAK
     EKAARESTAE VKKGVGISVG VYGCGLDGPD TAEIAVELNE DGTVTIFATW HDHGQGADMG
     TLGTAHEALR PLGIAPENIR LVLNDTAVCP NAGPAGGSRS QVVVGRAIKA GCELLLGGMR
     KADGTFRTYA EMRDEKIATR YSGKWSAPCT DCNAEGQGSP FAVYMYGVFL AEVSVELATG
     KTTVDKMTLV ADIGKIVNRL TVDGQLYGGI AQGIGLALSE DFEDIKKHST MPGAGFPYIK
     QIPDEIDLVY VEVPRPEGPF GAGGVGELPL TCPHAAIINA IHNACGVRVT RLPALPEKVL
     AGLQGK
//
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