ID   A0A1K1P2H3_SELRU        Unreviewed;      1002 AA.
AC   A0A1K1P2H3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SFW41783.1};
GN   ORFNames=SAMN02910323_1740 {ECO:0000313|EMBL:SFW41783.1};
OS   Selenomonas ruminantium.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=971 {ECO:0000313|EMBL:SFW41783.1, ECO:0000313|Proteomes:UP000182958};
RN   [1] {ECO:0000313|Proteomes:UP000182958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3 {ECO:0000313|Proteomes:UP000182958};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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; FPJA01000007; SFW41783.1; -; Genomic_DNA.
DR   RefSeq; WP_072306293.1; NZ_FPJA01000007.1.
DR   AlphaFoldDB; A0A1K1P2H3; -.
DR   Proteomes; UP000182958; Unassembled WGS sequence.
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:InterPro.
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   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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000182958};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          43..99
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1002 AA;  112472 MW;  A06219A294CECD4E CRC64;
     MNLTRRDFLK TTGLTGVGLA LASLGLDMPK VKAAAKEFKL KGAREFTSIC HFCACGCGVI
     GYVKDDKLIN LEGASDNPVN RGGLCSKGLG YGQIPNSDQR ATKPLYRAPG SDHWEEISWD
     EAIDKAARAL KKARDENWKQ TEVIDGQTVD VHRTDAIGFI GGSQINNEEC YQNIKMARAL
     GVTYIDNQTR VCHATTPPAM NAAFGRGAMT NHWGDLKHSK LIWIEGSNIA ECHPMGLKNV
     MKAKNNGAKI VHVDVRYTRT SKIADYFFQL RPGTDIAFLG YIISYIIENK KYNEDYIRRN
     TNAYCILRDD YKFDEGIFSG YNAEKHKYNM ETWGYALGAD KKPQKASDLF APNTVMSRMK
     EHFSRYTLDK VSGITGMSKD DIELAAKIFC EYSPTVMMYA LGMTQHTVGV ENIRCFTILQ
     LLRGNIGVPG GGIDAMRGQP NVQASTDFGI MFQYLPGYLS FPTEKTNTLE KWTRASGTFR
     AKWLKNMLKA WFGDYATPAN DYAFNLIGVR NSSHNDSIYG LFEDAYRGTV KCLYLCGQNP
     HVTNANAGMV HDGLCRMDTV IAQDIFVNET AEFWNRPGDN PADIQTEVIF LPACSYLERR
     GTITNSMRMI QWRMEGPKPL GDSKPDYEIN NLLWRKIREL YQDSTDPKDE IIQRMTWNYS
     DDQTVEDILK EINGYDLTTG KLVSGIGQLK DDGTTSSGMW IYAGVYGNGE HKAQRRGQED
     EGGLGIYPNF GWTWPDNIHL LYNRASCDEN GQPVDPEHKI VWWDAAKNRW EGYDVPDVGN
     RNAAPGTPDG NKPFRMTGEG YGRLFAAEYS DLNPDGMTRD HSYTPVDGPL PEFYEPVESP
     TKNALHKDEK AQFNPCVVYP RLPEKQRIGT KDEFPYVLCS SGIAEHWCSG TVTRNIPWLN
     ELVKEPFVEM SHKLADQLGV KLGDKVKVSS ARGNVTVKAM VTDRARPLTI NGEETHMVWM
     PYSWGFKGLS KGPSTNYITI DALDPNVQEQ EFKACLVNIT KA
//