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
//