ID A0A1E7DPM0_9BACI Unreviewed; 972 AA.
AC A0A1E7DPM0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:OES45037.1};
GN ORFNames=BA724_05945 {ECO:0000313|EMBL:OES45037.1};
OS Domibacillus iocasae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714016 {ECO:0000313|EMBL:OES45037.1, ECO:0000313|Proteomes:UP000095658};
RN [1] {ECO:0000313|EMBL:OES45037.1, ECO:0000313|Proteomes:UP000095658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29979 {ECO:0000313|EMBL:OES45037.1,
RC ECO:0000313|Proteomes:UP000095658};
RA Verma A., Pal Y., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus iocasae genome sequencing.";
RL Submitted (JUN-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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OES45037.1}.
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DR EMBL; MAMP01000021; OES45037.1; -; Genomic_DNA.
DR RefSeq; WP_069938659.1; NZ_MAMP01000021.1.
DR AlphaFoldDB; A0A1E7DPM0; -.
DR STRING; 1714016.BA724_05945; -.
DR Proteomes; UP000095658; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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 InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000095658};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..66
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 66..106
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 126..156
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 169..198
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 245..301
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 972 AA; 107862 MW; 8E523DFABAB1F619 CRC64;
MSIPGDVSVM QALKEQAIDI PSVCYHPALG AIETCDTCIV EVNGEFVRSC STMIQDGDVI
DAVSPDVKQA QEIAMNRILY NHELYCTVCD YNNGRCEVHN TVKQMKIEHQ SEPFTPKPHE
IDNSNPFYRY DPDQCILCGR CVEACQDVQV TETLSIDWSL KRPRVIWDKH STINESSCVS
CGHCSTVCPC NAMMEKGMEG EAGFLTGIKK PTLRPMIELT KNVETGYSSI LAISDVEAAM
RESRIKKTKT VCTYCGVGCS FDVWTKDRKI LKVEPQMEAP ANGISTCIKG KFGWDFVNSE
ERLTKPLIRE GDSFREAEWE EALALIEGKF REAKDTYGPD SMAFISSSKC TNEESYLMQK
LARGVIGTNN VDNCSRYCQT PATVGLFRTV GYGGDSGSIT DIEQAELVIV VGSNTSESHP
VLATRVKRSH KLKGQKLIVS DLRKHEMADR ADLFIQPRAG TDLVWLSAVT KYIVEQGWAD
ESFLSNRVNG LDDYVKSLEK YTMEYAEQVT GLPKEMMIQV AEAVHEADTT SVLWAMGVTQ
HSGGSDTSTA ISNLLLITGN YGKPGAGSYP LRGHNNVQGA SDFGSMPDRF PGYEKVADDA
VRAKYEKGWG VKIPADPGLN NHEMVSGIHA GDVKVMYLKG EDMGLVDSNL NYVHEAFEKL
DFFVVQDIFL SKTAQYADVV LPAAPSFEKE GTFTNTERRI QRLYQVFEPL GDSKPDWQII
MEVANRLGAG WTYNHPSEIM AEAASLMPLY AGVTYDRLSG YNSLQWPVAS DGTDSPLLFL
DEFPFPDGKA RLFPVEWTKP LEYEEEYDLH VNNGRLLEHF HEGNMTYKSK GITSKTPSVF
LEVSPELAAE RGLEDGTVVR LTSPHGSVKV PCLVTDRVKG KEVYLPMNDS DEGAINYLTS
SHADKDTDTP AYKEISAKME ILKTKGDSPL PRINSRNGDP QPQIGVQVEK KWARPDYIFP
GDLVKKGVGQ RG
//