ID A0A177HZU4_9ACTN Unreviewed; 1090 AA.
AC A0A177HZU4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Formate dehydrogenase-O major subunit {ECO:0000313|EMBL:OAH16335.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:OAH16335.1};
GN Name=fdoG {ECO:0000313|EMBL:OAH16335.1};
GN ORFNames=STSP_02980 {ECO:0000313|EMBL:OAH16335.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH16335.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH16335.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) 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:OAH16335.1}.
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DR EMBL; LOHS01000020; OAH16335.1; -; Genomic_DNA.
DR RefSeq; WP_067270907.1; NZ_LOHS01000020.1.
DR AlphaFoldDB; A0A177HZU4; -.
DR STRING; 1716141.STSP_02980; -.
DR PATRIC; fig|1716141.3.peg.315; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000077381; 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,
KW ECO:0000313|EMBL:OAH16335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 13..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 120431 MW; 2ED8A00126BDB485 CRC64;
MAIPGPIRSW PVLRQLTGTD PSGRGSSVTS HRTQTLRPRT ATADRVAKSV CPYCAVGCGQ
QVYVKGDKVV QIEGDPDSPV SRGRLCPKGS ASLQLTTGPS RRHQVLYRRP YGTDWEPLDL
ETAMDMVADR VVETRRRTWE WEHDGLRTAR TLGIASLGGA TLDNEENYLI KKLLTGLGVV
QVENQARVCH SSTVAGLGAS FGRGGATTFM QDQQHSDCIV IQGSNYAEAH PVGFQWVMEA
KARGARIIHV DPRFTRTSAL ADLYVPIRAG TDIAFLGGII NHVLTEEKDF REYVLAYTNA
ATLVSEDFRD TEDLDGVFSG LDPDRHHYDP RSWQYENTEV QQPIGAVDEQ YEWHQPAGDS
HDRVHAAGGA ETHGSGGPRA AARPERDETL QHPRCVYQIL KRHYARYTPE MVEKICGVPR
ATFLRVCDEL TANSGPDRTS SFAYAVGWTQ HTTGAQYIRA ASILQLLLGN IGRPGGGIQA
LRGHASIQGS SDIPTLFNLL PGYLPMPHAH AHEDLDSFIR ASRTDKGFWG NMRAYFVSLL
KAYYGDAATP ENDFCFDHLP RLTGSHSTYE TVATMLDGVC KGYFLMGENP AVGSANTRLQ
RLAMSHLDWL VVRDFSLIES ATWWKDGPEI ETGELRTEDI GTEVFFFPAA AHTEKSGSFT
NTNRWVQWHE AAVEPEGDAR SDLWFMYHLG RRIKERLAGS TDPMDQPIKD LTWDYPVDGV
LREPVAAAVL GEINGHGPDG APLSSYTELK DDGSTNCGCW IYCGIFADGV NQAARRKPHT
EQDWVAAEWA WAWPANRRIL YNRASAAPDG RPWSERKAYV WWDEAAGKWT GHDNPDFLPD
RPPGYVPPDD ATGPDALRGD DPFIMQADGK GWLYAPAGLE DGPLPTHYEP QDSPFGNALY
PETPRSPVRE LLRREGNRYH PSGDEPGADV YPYVVTTHRL TEHFTAGGMS RWTPHLAELQ
PEFFCEVSPA LAAERGLENG GWATIVSARG AVEARVLVTE RIRPLTVHGR TVHQIGLPFH
WGPNGTVPGD AANELVAIAL DPNAHIQEDK ALTADIRAGR RPRGPDLPLL VAEYRRRAGI
TDTTGTEART
//
