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Database: UniProt
Entry: G7WLW9_METH6
LinkDB: G7WLW9_METH6
Original site: G7WLW9_METH6 
ID   G7WLW9_METH6            Unreviewed;       695 AA.
AC   G7WLW9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Formate dehydrogenase, alpha subunit (F420) {ECO:0000313|EMBL:AET63712.1};
GN   OrderedLocusNames=Mhar_0325 {ECO:0000313|EMBL:AET63712.1};
OS   Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET63712.1, ECO:0000313|Proteomes:UP000005877};
RN   [1] {ECO:0000313|EMBL:AET63712.1, ECO:0000313|Proteomes:UP000005877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6Ac {ECO:0000313|EMBL:AET63712.1,
RC   ECO:0000313|Proteomes:UP000005877};
RX   PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA   Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT   "The genome characteristics and predicted function of methyl-group
RT   oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT   spp.";
RL   PLoS ONE 7:E36756-E36756(2012).
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; CP003117; AET63712.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7WLW9; -.
DR   STRING; 1110509.Mhar_0325; -.
DR   KEGG; mhi:Mhar_0325; -.
DR   PATRIC; fig|1110509.7.peg.366; -.
DR   HOGENOM; CLU_000422_4_0_2; -.
DR   Proteomes; UP000005877; 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; 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   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; 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   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:UP000005877}.
FT   DOMAIN          5..61
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   695 AA;  77153 MW;  4A4E3FA80D552A94 CRC64;
     MIPDMKFVAT TCPYCGVGCG LLLAVRDERV VGVEPWQAHP INEGKLCQKG RYAHQFIHSE
     DRLKTPLIKR GGSFVPASWD EALQLIARRL SSYRPEEVFF LASAKATNEE NYLFQKFARV
     VMKTNNVDHC ARLCHSSTVS ALAKAFGSGA MTNSILDLEE ARCIFVIGSN TFEQHPLIGR
     RLVLARRRGA KVISADPRLT PTAKEADLHL PIRPGTDVAL INGLVRRIIE GGWEDRGFIE
     ERTRGFETLR ETVMKEESTL PGTSRITGVP EGDIEAAAEM IATLKPAALL YSMGVTQHTS
     GVENVLALAN LMMLTGNIGR PGSGVNPLRG QNNVQGACDM GALPNVFSGY QSVEEDGCRR
     RMKRVWGVEE LGEARAGITS TEMMEILADR PGRMKALYLM GENPMISEAD QNRVRRALDN
     VEFMVSQEIF MTETTELADV VLPAASFAEK DGTFTNTDRR VQRLRKAIDP PGEAMPDWEI
     LSRLARAMGY GKMFDYRRAE DIFEEVARAT PSYAGISYRR LEEPHALQWP CPGPHHPGTP
     ILHVERFATP DGLGHFTPVE WRPPAEVPSE DYPLILTTGR SLWHWHAGSM TRRSKSLGGE
     VETGWVEMNE EDAEEMGIGD GEVVRVSSRR GRIELPARVT SEIKRGVIFV PFHFAECPAN
     RLTNAALDPV SKIPEFKACA ARVDKLRGWQ HPRGG
//
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