ID M0FK55_9EURY Unreviewed; 705 AA.
AC M0FK55;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:ELZ58949.1};
GN ORFNames=C467_04505 {ECO:0000313|EMBL:ELZ58949.1};
OS Halorubrum hochstenium ATCC 700873.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227481 {ECO:0000313|EMBL:ELZ58949.1, ECO:0000313|Proteomes:UP000011689};
RN [1] {ECO:0000313|EMBL:ELZ58949.1, ECO:0000313|Proteomes:UP000011689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700873 {ECO:0000313|EMBL:ELZ58949.1,
RC ECO:0000313|Proteomes:UP000011689};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ58949.1}.
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DR EMBL; AOJO01000020; ELZ58949.1; -; Genomic_DNA.
DR RefSeq; WP_008582202.1; NZ_AOJO01000020.1.
DR AlphaFoldDB; M0FK55; -.
DR STRING; 1227481.C467_04505; -.
DR GeneID; 72712755; -.
DR PATRIC; fig|1227481.4.peg.879; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000011689; 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; 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 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; 2.
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; PS00490; MOLYBDOPTERIN_PROK_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011689}.
FT DOMAIN 12..62
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|SMART:SM00926"
FT REGION 683..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 74128 MW; 4F6EB4A1933CB097 CRC64;
MPDPSETSER RFESNPTVCP FCGVGCSVEY AGRGSATGVE GPVNGRGEIC PKGAAAFDVV
DHGDRLTEPL VEHGGTFVTA PWSEALDRVA SGIGEVVEEH GADAVQFFAS SNCTNEENYV
LQKLARVLGT NNVDNCARLC HASTVAAMSE RFGAGAMTNT LDDLGEADCI FVNGANPAEQ
HPVAFRSYIL PAVRDGATLV HVDPRENDTT EAADVHLPLR PGTDIQLLNA VAAVLVEEDL
VDEGFLAERT TGFDRLREHL AGVDVAASAE AAGVDPETVR EAARAYGEAD RAAVITGMGT
SQHRCGTDNV HALLNLALLT GNVGRPGTGV NPLRGQNNVQ GASDVGGLPG VLPGYEPVTD
PDARERVADE WGVEPPAEPG LTEVEATHRF GDEVRAAVVF GENPAVTEPN ATAVASAFDD
LDFCVVIDLF ETRTAEHADV VLPGSAWAEK SGTVTNTDRR VMRMRPNADL PGSARRDFEI
LTELGRRLTD RPEEFAYDGP ADAFDELTRV APIYEGMSYA GIGDGYQRWP FDAEAGTGTD
VLHAETFATG ERTAPLAVVD AVPPADDLDA GELTLTTGRV LQHFNSGALS RRSDRLMAMR
GEDVLQIHPA DAAERGIEDG DRVTVSNERG TVEAAADVTP AVREGVAFCT FHYAEPLANA
LTGDALDPAA KIPEFKHSAV AVEPAASAAG ESGAAGEGDA AAGDD
//
