ID A0A2I0NP94_9EURY Unreviewed; 688 AA.
AC A0A2I0NP94;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:PKL55771.1};
GN ORFNames=CVV35_08150 {ECO:0000313|EMBL:PKL55771.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013822 {ECO:0000313|EMBL:PKL55771.1, ECO:0000313|Proteomes:UP000233331};
RN [1] {ECO:0000313|EMBL:PKL55771.1, ECO:0000313|Proteomes:UP000233331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-6 {ECO:0000313|EMBL:PKL55771.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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:PKL55771.1}.
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DR EMBL; PGYH01000074; PKL55771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0NP94; -.
DR Proteomes; UP000233331; 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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 8..64
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 688 AA; 76412 MW; 6E1A8A864AB71012 CRC64;
MTETNGKLRY VPTTCPYCGV GCGLNLVVND GKLVGVEPLK RTPVNEGKLC PKGATCWEFV
QSPDRLTKPL IKKNGTFEEA SWDEAYDLIA SKFKETYEKY GPKSLGFQVS CRTPNEECYI
MQKLARVAFK TNNIDNCARI CHGPSVAGLS LSFGSGAATN PFEDVLNADV IFLIGSNPIE
AHPLAGRRIV QAKKAGKKII VCDPRYTPTA RLADEWVRYN PSTNIALINS IMYWIIQENL
HDKEFIEKRT TGFEELKKTV ENYADVESIT GVPTERIKEI ARIYAGAKNA VLIYCLGITE
LTTGTDNVRS TANLSMLTGN VGRPGTGVNP LRGQNNVQGA CDMGAYPNVF SGYQKCEDDA
TRKRMEELWG VTGLEKEYGV TLTEQITQCG DPIKAMYIFA LNPVVSYPDS NHVMRSLEKL
DFLVVQDIFM TETAKYADVI LPGASFAEKD GTFTSGERRI NRVRKAVEPP GDAKEDWQIF
VDLAHKLGLQ GFDFNSPEDI WDDMRRVTPS MAGASYARME KPESVHWPCP TEDHPGTPIL
HREKFSSADG LGHFFGLEHR PPAEVADEEY PFTLMTGRLL FHYHTRTQTD RAKLLHHEVP
AGFVQINNED AARLKIQNGE KIKLTSRRGE VETLAKVTDQ VAPGVLMMTM HFGDAAANKL
TNTALDPLSK MPELKHSAVK VEKITGVQ
//