ID A0A101FRI5_9FIRM Unreviewed; 674 AA.
AC A0A101FRI5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=FdhA {ECO:0000313|EMBL:KUK41899.1};
GN ORFNames=XD69_0063 {ECO:0000313|EMBL:KUK41899.1};
OS Clostridia bacterium 62_21.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635276 {ECO:0000313|EMBL:KUK41899.1, ECO:0000313|Proteomes:UP000067139};
RN [1] {ECO:0000313|EMBL:KUK41899.1, ECO:0000313|Proteomes:UP000067139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62_21 {ECO:0000313|EMBL:KUK41899.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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 -!- 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:KUK41899.1}.
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DR EMBL; LGFR01000003; KUK41899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FRI5; -.
DR PATRIC; fig|1635276.4.peg.511; -.
DR Proteomes; UP000067139; Unassembled WGS sequence.
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; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 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 InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
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 NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 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 4: Predicted;
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}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 674 AA; 74395 MW; 244241E19A550CAD CRC64;
MDYRAAICPY CGCGCGIHLV VNNGKIIGVE PWKEHPVNEG ANCIKGKNAY QFLYSEDRLK
TPLIREGGGF RKASWDEALD LIVRRLKVTP PGLFGFIASG KTTNEDSYVL QKFARVVVQT
NNIDYCARFC HASTMAGLLA TVGAGVMQTA QEDIERSDCI ILDGVNLKET FPILARRVLR
ARRNGAKVIV IDPRNTVTAR YLADVHLRLQ PGTDVLLLNA MMRIILDEGL ENKKFVAEKT
EGIDQLRANL SQIDLKEVEP ITGVPLDKIR EAAVTYAKAG NGCILYDEGI TQHTTGTDNV
KALADLALLT GHIGKPGGGV NSLRGQVNGE GTGDMGCLNI FYPGFKKVGE ETAEAFKQLW
GVDNLPTQPG LTYLDILNKC RTVYIVGANP AMAAPDSNGI RETLRKIDFL IVQDIYLTET
AELANVVLPS ATWVEREGTQ TWVDRRVQKI DKLIDPPGEA EPDWRVLCRL AEKMGYGNLF
PFKNASEIFE EIRRCVPQYK GITYERLARK AGGIQWPCPS EDHPGTPTMF LKGFPTASGR
AQFQPVTFRP PAEIPDSEHP YQLTTGRTIF HFHTGTMTRR TPKLDREIHG VFVEINPADA
EAAAVRHGDR VVVTTRRGSI EVSARVTPEV PRGLLFVPFH FAEGMANTLT NPALDPACKI
PEFKVCAAKL EVKR
//
