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Database: UniProt
Entry: A0A1E7DPM0_9BACI
LinkDB: A0A1E7DPM0_9BACI
Original site: A0A1E7DPM0_9BACI 
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
//
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