ID B8J4K7_DESDA Unreviewed; 1012 AA.
AC B8J4K7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ACL48465.1};
DE EC=1.17.1.9 {ECO:0000313|EMBL:ACL48465.1};
DE Flags: Precursor;
GN OrderedLocusNames=Ddes_0555 {ECO:0000313|EMBL:ACL48465.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL48465.1};
RN [1] {ECO:0000313|EMBL:ACL48465.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL48465.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-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 -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011771}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001358; ACL48465.1; -; Genomic_DNA.
DR STRING; 525146.Ddes_0555; -.
DR KEGG; dds:Ddes_0555; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_2_7; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02752; MopB_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 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; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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; 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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 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:ACL48465.1}; Selenium {ECO:0000313|EMBL:ACL48465.1};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933,
KW ECO:0000313|EMBL:ACL48465.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 43..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ACL48465.1"
SQ SEQUENCE 1012 AA; 112548 MW; DBA0253481FC9810 CRC64;
MKSTRRSFLK GVGAGVLCLT LGHLGFDLGE AQAYAGKLKI EGAKEVSSIC PFCSVQCQII
AYVKGGKLVS TEGDPDFPIT EGALCAKGAA LYSMYTSDHR LMKPMYRAPF SDKWEEKDWD
WTLEQIARRV KDARDKDMIL KNDKGQTVNR LETIFWMGTS HASNEECAVI HQALRGLGVV
HMDHQARVUH SPTVAALAES FGRGAMTNHW IDIKNADAVL IIGSNAAEHH PVAFKWIMKA
KDNGAVLMHV DPKFSRTSAR CDFHVPLRSG TDIPFLGGML NYILENGLYH KEYVNNYTNA
AFVVGDGYAF EDGLFSGYDA AARKYDKSKW ALAKGPDGGP VVDPTHQNPR CVINLMKDHY
SRYTLKNVSD VTGVSQDNLL KVYKNFCATG RPDKAGTILY ALGWTQHTVG VQNIRLSSLV
QLLLGNIGIA GGGINALRGE PNVQGSTDHA LLYNNIPGYH GTPQAPWQTL GEYNKANTPV
TVVPNSANWW GNRPKYVTSL LKGWFGDAAT PENDFCYSLL PKLEPGVDYS YMFVMDRIYN
KKIKGGFIMG VNPMNSFPNT NKMRAALDNL DWLVCSEIHN SETTDNWQRP GVDPKTKKTE
VFLLPSAHRI EKAGTISNSG RWLQWFDKAV EPAGEARNFA DVVVPLFNTI RRMYKTEGGV
LPEAVLQMHW TDKYDPEDWA RRINGFFWAD TKVGDKTYKR GQLVPAFGAL KDDGTTSSLN
WIYTGSWTEE DGNKSRRRDP SQTPMQAKIG LFPNWSWCWP LNRRILYNRA SVDMNGKPFN
PNRAVIEWDG SKWVGDVPDG PWPPMADPKG KLPFIMVKDG LAQFYGPGPA DGPFPEHYEP
AETPLATHPF SKQLSSPVYK YHKTDMDQIA PPADPRYPIV LTTYSLTEHW CGGGETRNVP
NLLETEPQLY VEMSHELAKE KGIKNGDGVV LESARGNCEA IAMVTVRIRP FTVMGKTVHL
VGMPFAFGWT TPKTGDSTNR LTVGAYDPNT TIPESKACCV NLRKADKLTE IG
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