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Database: UniProt
Entry: A0A2I0NP94_9EURY
LinkDB: A0A2I0NP94_9EURY
Original site: A0A2I0NP94_9EURY 
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
//
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