ID A5UU80_ROSS1 Unreviewed; 1014 AA.
AC A5UU80;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ABQ90183.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:ABQ90183.1};
GN OrderedLocusNames=RoseRS_1793 {ECO:0000313|EMBL:ABQ90183.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ90183.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) 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}.
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DR EMBL; CP000686; ABQ90183.1; -; Genomic_DNA.
DR RefSeq; WP_011956530.1; NC_009523.1.
DR AlphaFoldDB; A5UU80; -.
DR STRING; 357808.RoseRS_1793; -.
DR KEGG; rrs:RoseRS_1793; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_9_0_0; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000006554; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABQ90183.1}.
FT DOMAIN 85..143
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 115641 MW; A173199D019E9DE2 CRC64;
MADSLVKNIL RTLAQRQRAE AQQEVVARQP ATQPGAVERS VPQPAPAHAV QGATAELSGY
PPVERWQHWT EYDPKAWPQK ISRSYTLVPT ICFNCESACG LLAYVDTSTL KIQKFEGNPL
HPGSRGRNCA KGPATLNQVY DPDRILYPLK RVGRRGEGKW KRVSWDEALD DIAARIRCAI
VEKRLTEIMY HVGRPGHDGI MEWVLPAWGV DAHNSHTNVC SSSARCGQAL WMGYDRPSPD
HAHARVILLI SSHLETGHYF NPHAQRIMEG KMAGAKLIVF DTRLSNTASL ADEWIAPWPG
SETAILLAIA RHLIVTRKYD RTFVRRWVNW EEYLRHEHPD LPLRFETFEA KLEELYARYT
FEFAAQESGV SVEQIARVAD YIAQCDGRLA THTWRSATSA NLGGWMVARC LWFLNVLTGS
IGKEGGTSAN VWDKWVPRHP NMAPHVKVWN ELTWPQEYPL SFYELSYLLP HFLKEQRGKI
DVYFTRVYNP LWTNPDGMSW MEVLTDESKI GLHVHLSPGW SETGLFADYI LPMGHGAERH
DMMSQETHGG CWIAFRQPVI REALRRLGRP VDDTRKANPG EVWEETEFWI ELSWRIDPDG
SLGIRKTFES PYRPGEKITV DELYGWMFEN HVPGLPEAAA KEGLTPLEYM RRYGAFEIRK
GVQPTYDQPL AESEVEGVTV DPETRVVYTK KPAAPSSNIT PVPYFQPDPE RGRPIGVQLE
DGSLVSGFPT PSRKLEFYST TMRHWGWPEY AIPTYVHSHV HPSKIDRERN EAILLSTFRL
PTLIHTRSGN AKWLYEISHK NPVWIHPSDA QRLGVQTGDL IKVVTSIGYF VDRVWVTEGI
RPGVIACSHH LGRWRLREDE GGKLSTALVE LAPAGESRWQ MRQVHGIKPY ASADPDTEHI
WWEDAGVHQN LTFAVQPDPV SGMHCWHQKV RLERAGPDDR YGDIFVDTRR AHEVYREWLA
MTRPASQVSP NGLRRPHWWL RPFRPDLEAY YLPGRDPGNG HIAVHAVSAS DHKK
//
