ID A0A7D5E574_9EURY Unreviewed; 758 AA.
AC A0A7D5E574;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:QLC34977.1};
GN Name=fdhF {ECO:0000313|EMBL:QLC34977.1};
GN ORFNames=EFA46_012020 {ECO:0000313|EMBL:QLC34977.1};
OS Halarchaeum sp. CBA1220.
OG Plasmid pcba1220-01 {ECO:0000313|Proteomes:UP000267112}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae.
OX NCBI_TaxID=1853682 {ECO:0000313|EMBL:QLC34977.1, ECO:0000313|Proteomes:UP000267112};
RN [1] {ECO:0000313|EMBL:QLC34977.1, ECO:0000313|Proteomes:UP000267112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1220 {ECO:0000313|EMBL:QLC34977.1,
RC ECO:0000313|Proteomes:UP000267112};
RC PLASMID=pcba1220-01 {ECO:0000313|Proteomes:UP000267112};
RA Roh S.W., Lee C., Song H.S.;
RT "Genomic analysis of Halarchaeum grantii CBA1220.";
RL Submitted (JUN-2020) 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP054708; QLC34977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7D5E574; -.
DR KEGG; halr:EFA46_012020; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000267112; Plasmid pcba1220-01.
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; cd00508; MopB_CT_Fdh-Nap-like; 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; 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 PIRSF; PIRSF000144; CbbBc; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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}; Plasmid {ECO:0000313|EMBL:QLC34977.1}.
FT DOMAIN 57..115
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 717..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83928 MW; 0C7244333A3807D1 CRC64;
MSSDERKEGV AGFMQRAKEQ ANRNVEHFAE GMAAGSMPEG KLFDIAQQIS DKRLGELTVD
DTTCGYCAVG CRFDVYTDGE EVLATRATDP EKSPVNDIST CVKGKFSYNF ANSEERLTDP
LVRDENGEWR EASWEEALTR VVEGFQSIID EHGNEAMSVI ASSKATNEEN YLMGKFARQV
LGTNTVDNCN RLCHSSTVAG LAKTYGYGAA SISVKDFDEA DLIFLTGSNT TEAHPVLGTR
VKQHVKEGGD LIVFDPRETQ IAEYADQYTE IRPGYDTVWV NGVTRYLIEN DLYDEEFVAE
RTTGFEEVKE AVDEFTLDYV EEVTGAPPEE IQAAAEAIAE ADRTVFGWTL GITEHSHGTD
NVAALANLAA ITGNLGKPGT GVSPFRGQNN VQGGGGDMGP LPDNFPGYQK VADDEVRAKF
EEAWDCDIPA ERGYYTTEMF NAFEDGPLEG MYCIGENPSL SEPGKKHADE VLEEMEFLVV
QDLFLNETAK YADVVLPAVS FLEKEGTFAN TDRRVQKVNQ VLEKKGNAKA DWEILQELAN
RMGREWNYTN TNEINEEMRS LTPIYGGISH ERIEEEGGIQ WPCWDEDHPG TERLYTEEFN
TEDGKANLVP VGYAEPMAPQ TEEFPLTLTT GRVLYQYHTG TMTHPEEGIM KYNDRDFVEV
NPSTAASYGI EDGDPVRIES DKGEIVVTAQ VTERVGEETV FAPIHFAETA VNTLTDSERL
DPEAKTPEFK ATAVRISPVE GRDSVSRPNN VEPARGDD
//
