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Database: UniProt
Entry: A0A0A2U5X3_9FIRM
LinkDB: A0A0A2U5X3_9FIRM
Original site: A0A0A2U5X3_9FIRM 
ID   A0A0A2U5X3_9FIRM        Unreviewed;       652 AA.
AC   A0A0A2U5X3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
DE   Flags: Fragment;
GN   ORFNames=JT05_01255 {ECO:0000313|EMBL:KGP77070.1};
OS   Desulfosporosinus sp. Tol-M.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP77070.1, ECO:0000313|Proteomes:UP000030439};
RN   [1] {ECO:0000313|EMBL:KGP77070.1, ECO:0000313|Proteomes:UP000030439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Abu Laban N., Tan B., Dao A., Foght J.;
RT   "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT   probing of toluene- degrading methanogenic culture enriched from oil sands
RT   tailing of Alberta, Canada.";
RL   Submitted (OCT-2014) 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};
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:KGP77070.1}.
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DR   EMBL; JQID01000031; KGP77070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2U5X3; -.
DR   STRING; 1536651.JT05_01255; -.
DR   Proteomes; UP000030439; 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   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000030439}.
FT   DOMAIN          1..31
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGP77070.1"
SQ   SEQUENCE   652 AA;  71532 MW;  124C6018DF7C08CB CRC64;
     TSKRDKNYSP VNKGALCVKG RFGWDFIHSA DRLTTPLIKE NGEFRAASWD EALNFAANKL
     KGIKEQYGPD SIALFSSARV TNEENYLAQK LTRAAIGTNN VDHCARLCHA SSVAGIGAAF
     GSGAMTNSIN ELEKEARAIF IIGTNTTDNH PVIGYKIKKN VRETGAKLIV ADPRRIDLAK
     MADVHMRFRP GTDVALINGM MNVIISEGLM DKEFIEKRTE AYEQMAEVVM KYSPEVVAEI
     TGVPAEDIKK AARIYAESEA AAICYSMGIT QHSTGTDNVK SVCNLAMLTG NVGRPGTGVS
     ALRGQNNVQG ACDMGALPVC YPAYQPLGVD ANREKFEQAW GVKLSSNNGL TITAAINKAH
     QGELKALYIM GENPMISDPD LHHVDEALDK LECLIVQDIF LTETAQKADV VLPGVCFAEK
     DGTFTSTERR VQMVRKAVDP PGEARQDWKI LSEMSTRLGY SMDYATAEEI FEEMRTVTPS
     YAGMSYARLE GQGLHWPCPN EEHPGTPILH RGIFTRGLGL FHAVEFKEPF ELPDDQYPLI
     LSTGRSLFHY HTGTMTRRAQ ALDAHQPSNE VQVNSATAAR LNIYNGEMVK LITRRGSIEL
     KAKATDILAE NVVFTFFHFS EAAANILTNG EALDPVCGIP EFKVCAARLE KL
//
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