ID D6KGI1_9ACTN Unreviewed; 890 AA.
AC D6KGI1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Formate dehydrogenase-O, major subunit {ECO:0000313|EMBL:EFF88407.2};
GN ORFNames=SSTG_06056 {ECO:0000313|EMBL:EFF88407.2};
OS Streptomyces sp. e14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF88407.2, ECO:0000313|Proteomes:UP000004704};
RN [1] {ECO:0000313|EMBL:EFF88407.2, ECO:0000313|Proteomes:UP000004704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain e14.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG753630; EFF88407.2; -; Genomic_DNA.
DR AlphaFoldDB; D6KGI1; -.
DR STRING; 645465.SSTG_06056; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000004704; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR048158; Formate_DH_Act.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR NCBIfam; NF041513; formate_DH_Act; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT DOMAIN 15..419
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 449..490
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 735..854
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 145..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 98236 MW; D4A9729DA600B32A CRC64;
MGTSFGRGGA TTFQQDLQNS DCIVIQGSNM AECHPVGFQW VMEAKARGAK VIHVDPRFTR
TSAVADVHVP LRAGSDIAFL GGIVNYVLSH DKYFRDYVVA YSNGPVVLGE DFRDTEDLDG
VFSGLDPENR KYDNGTWQYE GMEVQAASGE RDQEYEKRTG GGSSVSEAGR GEAHGSGGAD
IGAGEPERDE TMTHPRCVFQ VLKRHYARYT PEMVERICGV PQDLFRQVCE LVTENSGRER
TTAFAYAVGW TQHTVGVQYI RAASVLQTLL GNIGRPGGGI LALRGHASIQ GSTDIPTLFN
LLPGYIPMPH AHQQEDLDSF VSAEAAGKGY WGEMRSYLVS LLKAYWGDAA RPDNDFCFDY
LPRLTGSHST YETVQAQLEG TCKGYFLMGE NPAVGSANAK LQRLGMANLD WLVVRDFSLI
ESATWWKDGP EIETGELRTE DIGTEVFFLP AAAHTEKDGS FTNTQRLLQW HHQAVEPPGE
ARSDLWFTFH LGRIIRAKLA GSTDPMDRPV LDLTWDYATK GETAEPVAQT VLAEINGYDA
EGRPLSSYEQ LNDDGSTACG CWIYCGVYAD DVNQAARRKP GKEQNWVANE WGWAWPANRR
ILYNRASADP DGKPWSERKA LVWWDAEQAE WTGHDIADFA KDKSPHHRPP PGAKAAEALS
GTDAFVMQAD GKAWLYVPAG LTDGPLPAHY EPQDSPFPNL LYGQQRNPVR QLLPSGPDNR
YQPSGGEPGT EVFPFVATTY RLTEHHTAGG MSRWQPYLAE LQPEFFCEVS PELAAERALE
HTGWATIVSA RGVIEARVLV TDRMTPLRVH GRTLHQVGLP YHWGPNGYST GDAANELVHL
SLDPNTHIQE TKAFAVDIRP GRRPRGPAAP ALVRAYRARA GIDEHTGTEM
//
