ID Q2FRK1_METHJ Unreviewed; 686 AA.
AC Q2FRK1;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Formate dehydrogenase, alpha subunit (F420) {ECO:0000313|EMBL:ABD41730.1};
DE EC=1.2.99.- {ECO:0000313|EMBL:ABD41730.1};
GN OrderedLocusNames=Mhun_2021 {ECO:0000313|EMBL:ABD41730.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD41730.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
RN [2] {ECO:0007829|PDB:7BKB, ECO:0007829|PDB:7BKC}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS).
RX PubMed=34516836; DOI=10.1126/science.abg5550;
RA Watanabe T., Pfeil-Gardiner O., Kahnt J., Koch J., Shima S., Murphy B.J.;
RT "Three-megadalton complex of methanogenic electron-bifurcating and
RT CO<sub>2</sub>-fixing enzymes.";
RL Science 373:1151-1156(2021).
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; CP000254; ABD41730.1; -; Genomic_DNA.
DR RefSeq; WP_011448992.1; NC_007796.1.
DR PDB; 7BKB; EM; 3.50 A; D/d=1-686.
DR PDB; 7BKC; EM; 3.00 A; D/d=1-686.
DR PDB; 7BKD; EM; 3.00 A; D=1-686.
DR PDB; 7BKE; EM; 2.80 A; D=1-686.
DR AlphaFoldDB; Q2FRK1; -.
DR SMR; Q2FRK1; -.
DR STRING; 323259.Mhun_2021; -.
DR EnsemblBacteria; ABD41730; ABD41730; Mhun_2021.
DR GeneID; 3924984; -.
DR KEGG; mhu:Mhun_2021; -.
DR eggNOG; arCOG01491; Archaea.
DR HOGENOM; CLU_000422_4_0_2; -.
DR InParanoid; Q2FRK1; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000001941; Chromosome.
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; 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 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.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7BKB, ECO:0007829|PDB:7BKC};
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 Oxidoreductase {ECO:0000313|EMBL:ABD41730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001941}.
FT DOMAIN 8..64
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 686 AA; 75818 MW; 33B5499B9713A842 CRC64;
MSENSEIMKY VATTCPYCGV GCTLNLVVSN GKVVGVEPNQ RSPINEGKLC PKGVTCWEHI
HSPDRLTTPL IKKDGKFIEA SWDEALDLVA KNLKVIYDKH GPKGLGFQTS CRTVNEDCYI
FQKFARVGFK TNNVDNCARI CHGPSVAGLS LSFGSGAATN GFEDALNADL ILIWGSNAVE
AHPLAGRRIA QAKKKGIQII AVDPRYTMTA RLADTYVRFN PSTHIALANS MMYWIIKEGL
EDKKFIQDRV NGFEDLKKTV ENYADAEAIH GVPLDVVKDI AFRYAKAKNA VIIYCLGITE
LTTGTDNVRS MGNLALLTGN VGREGVGVNP LRGQNNVQGA CDMGAYPNVY SGYQKCEVAE
NRAKMEKAWS VTNLPDWYGA TLTEQINQCG DEIKGMYILG LNPVVTYPSS NHVKAQLEKL
DFLVVQDIFF TETCQYADVI LPGACFAEKD GTFTSGERRI NRVRKAVNPP GQAKEDIHII
SELAAKMGFK GFELPTAKDV WDDMRAVTPS MFGATYEKLE RPEGICWPCP TEEHPGTPIL
HREKFATADG KGNLFGIDYR PPAEVADAEY PFTLMTGRLI FHYHSRTQTD RAADLHREVP
ESYAQINIED ARRLGIKNNE YIKLKSRRGE TTTLARVTDE VAPGVVYMTM HFADGVNNLT
NTVLDPMSKM PELKHCAISI EKVGGN
//
