ID A0A069JL13_9ACTN Unreviewed; 1090 AA.
AC A0A069JL13;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KDQ65453.1};
GN ORFNames=DT87_31745 {ECO:0000313|EMBL:KDQ65453.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ65453.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ65453.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ65453.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:KDQ65453.1}.
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DR EMBL; JJOB01000003; KDQ65453.1; -; Genomic_DNA.
DR RefSeq; WP_037882949.1; NZ_JJOB01000003.1.
DR AlphaFoldDB; A0A069JL13; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000027475; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR048158; Formate_DH_Act.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR NCBIfam; NF041513; formate_DH_Act; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
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.
PE 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 18..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 120351 MW; 3F0E5DC7A72F5F39 CRC64;
MGVHDLLGRW PAYRQLTGDD PLGRGRAAMS PATEELRPRT ATADRVVKSV CPYCAVGCGQ
QVYVKDDRVV QIEGDPDSPV SRGRLCPKGS ATLQLTTGSA RRHQVLYRRP YGTDWEPLDL
ETAMDMVADR VVETRRRTWE WAHEGVRTAR TMGIASLGGA TLDNEENYLI KKLFTGLGIV
QVENQARVCH SSTVAGLGTS FGRGGATTFM QDLQHADCIV IQGSNFAEAH PVGFQWVMEA
KARGARVIHV DPRFTRTSAL SDQYVPIRAG SDIAFLGGVI NHVLTEEKDF REYVLAYTNA
ATLVGDAFRD TEDLDGIFSG LDEERGHYDT ETWQYRDTEV QAPSGDVDEL YERRTESAED
HGRIHDAAES ETHGSGGART GARPPRDETL RDPRCVYQIL KRHYARYTPE MVEKICGIGR
EAFLEVCDAL TSNSGPDRTS AFAYAVGWTQ HSTGSQCIRA ASVLQLLLGN IGRPGGGIQA
LRGHASIQGS SDIPTLFNLL PGYLPMPHAH AHENLDAFIR ASRTAKGFWG DMRAYFVSLL
KAYYGDAATA ENDFCFDHLP RLTGSHGTYE TVMAQLDGSC QGYFLMGENP AVGSANARLQ
RLGMARLEWL VVRDFSLIES ATWWQDGPET ETGEMRTEDI GTEVFFFPAA SHTEKSGSFT
NTNRWLQWHH AAVEPQGDAR SDLWFMYHLG RRVKERLASS TDPMDDAVRD LTWDYPVEGP
LEEPVATSVL AEINGHGPDG APLSAYTELK DDGSTRCGCW IYCGVYADGV NQAARRKPHT
EQDWVASEWA WAWPANRRIL YNRASAAPDG NPWSERKAYV WWDEAERRWT GHDVPDFVPD
RAPDHVPEPG ATGPDALRGD DPFIMQADGK GWLYAPAGLE DGPLPTHYEP QDSPFGNALH
PSRPRSPVRR LHPREGNRYH PSGDEPGAGV YPYIVTTHRL TEHFTAGGMS RWSPYLSELQ
PEFFCEVSPQ LAAERGLEHG GWATIVTARN AVEARVMVTG RITPLTVHGR TVHQIGLPFH
WGPNGVSTGD AANELVAIAL DPNALIQEDK ALTADIRPGR RPRGPALPEL VAEYRGRAGI
TETTGTQEAT
//
