ID   FDOG_ECOLI              Reviewed;        1016 AA.
AC   P32176; P78131; Q2M8J1;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 5.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Formate dehydrogenase-O major subunit;
DE            EC=1.17.1.9;
DE   AltName: Full=Aerobic formate dehydrogenase major subunit;
DE   AltName: Full=FDH-Z subunit alpha;
DE   AltName: Full=Formate dehydrogenase-O subunit alpha;
DE   Flags: Precursor;
GN   Name=fdoG; OrderedLocusNames=b3894, JW3865;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP   252-261; 344-348 AND 822.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-190, AND CHARACTERIZATION.
RC   STRAIN=K12;
RX   PubMed=8522521; DOI=10.1128/jb.177.24.7141-7149.1995;
RA   Abaibou H., Pommier J., Giordano G., Mandrand-Berthelot M.-A.;
RT   "Expression and characterization of the Escherichia coli fdo locus and a
RT   possible physiological role for aerobic formate dehydrogenase.";
RL   J. Bacteriol. 177:7141-7149(1995).
RN   [5]
RP   EXPORT VIA THE TAT-SYSTEM.
RX   PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA   Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA   Palmer T., Georgiou G.;
RT   "Export pathway selectivity of Escherichia coli twin arginine translocation
RT   signal peptides.";
RL   J. Biol. Chem. 282:8309-8316(2007).
CC   -!- FUNCTION: Allows to use formate as major electron donor during aerobic
CC       respiration. Subunit alpha possibly forms the active site.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.9;
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed by
CC       subunits alpha, beta and gamma.
CC   -!- INTERACTION:
CC       P32176; P13024: fdhE; NbExp=4; IntAct=EBI-368676, EBI-550129;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- PTM: Exported by the Tat system. The position of the signal peptide
CC       cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; L19201; AAB03027.2; -; Genomic_DNA.
DR   EMBL; U00096; AAD13456.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77415.1; -; Genomic_DNA.
DR   EMBL; X87583; CAA60887.1; -; Genomic_DNA.
DR   PIR; A65195; S40838.
DR   RefSeq; NP_418330.1; NC_000913.3.
DR   RefSeq; WP_010723259.1; NZ_LN832404.1.
DR   BioGRID; 4263323; 36.
DR   BioGRID; 852691; 1.
DR   ComplexPortal; CPX-6029; Formate dehydrogenase Z complex.
DR   DIP; DIP-9576N; -.
DR   IntAct; P32176; 12.
DR   MINT; P32176; -.
DR   STRING; 511145.b3894; -.
DR   jPOST; P32176; -.
DR   PaxDb; 511145-b3894; -.
DR   GeneID; 948394; -.
DR   KEGG; ecj:JW3865; -.
DR   KEGG; eco:b3894; -.
DR   PATRIC; fig|511145.12.peg.4008; -.
DR   EchoBASE; EB1804; -.
DR   eggNOG; COG0243; Bacteria.
DR   eggNOG; COG3383; Bacteria.
DR   HOGENOM; CLU_000422_1_0_6; -.
DR   InParanoid; P32176; -.
DR   OMA; QYFEMMN; -.
DR   PhylomeDB; P32176; -.
DR   BioCyc; EcoCyc:FDOG-MONOMER; -.
DR   BioCyc; MetaCyc:FDOG-MONOMER; -.
DR   PHI-base; PHI:10994; -.
DR   PRO; PR:P32176; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009326; C:formate dehydrogenase complex; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; HDA:EcoCyc.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IDA:EcoCyc.
DR   GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0019645; P:anaerobic electron transport chain; NAS:ComplexPortal.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0045333; P:cellular respiration; IEP:EcoCyc.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0015944; P:formate oxidation; IDA:EcoCyc.
DR   GO; GO:0006788; P:heme oxidation; NAS:ComplexPortal.
DR   CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR   CDD; cd02752; MopB_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; IPR006443; Formate-DH-alph_fdnG.
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   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR01553; formate-DH-alph; 1.
DR   PANTHER; PTHR43598:SF6; FORMATE DEHYDROGENASE-O MAJOR SUBUNIT; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
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.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase;
KW   Periplasm; Reference proteome; Selenocysteine; Signal.
FT   SIGNAL          1..33
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           34..1016
FT                   /note="Formate dehydrogenase-O major subunit"
FT                   /id="PRO_0000063223"
FT   DOMAIN          43..106
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         50
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         92
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   NON_STD         196
FT                   /note="Selenocysteine"
FT   CONFLICT        252..261
FT                   /note="GAKLIVIDPR -> RREADCDRSC (in Ref. 1; AAB03027)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344..348
FT                   /note="ENGFA -> GKRLR (in Ref. 1; AAB03027)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1016 AA;  112549 MW;  DED0952028055769 CRC64;
     MQVSRRQFFK ICAGGMAGTT AAALGFAPSV ALAETRQYKL LRTRETRNTC TYCSVGCGLL
     MYSLGDGAKN AKASIFHIEG DPDHPVNRGA LCPKGAGLVD FIHSESRLKF PEYRAPGSDK
     WQQISWEEAF DRIAKLMKED RDANYIAQNA EGVTVNRWLS TGMLCASASS NETGYLTQKF
     SRALGMLAVD NQARVUHGPT VASLAPTFGR GAMTNHWVDI KNANLVVVMG GNAAEAHPVG
     FRWAMEAKIH NGAKLIVIDP RFTRTAAVAD YYAPIRSGTD IAFLSGVLLY LLNNEKFNRE
     YTEAYTNASL IVREDYGFED GLFTGYDAEK RKYDKSSWTY ELDENGFAKR DTTLQHPRCV
     WNLLKQHVSR YTPDVVENIC GTPKDAFLKV CEYIAETSAH DKTASFLYAL GWTQHSVGAQ
     NIRTMAMIQL LLGNMGMAGG GVNALRGHSN IQGLTDLGLL SQSLPGYMTL PSEKQTDLQT
     YLTANTPKPL LEGQVNYWGN YPKFFVSMMK AFFGDKATAE NSWGFDWLPK WDKGYDVLQY
     FEMMKEGKVN GYICQGFNPV ASFPNKNKVI GCLSKLKFLV TIDPLNTETS NFWQNHGELN
     EVDSSKIQTE VFRLPSTCFA EENGSIVNSG RWLQWHWKGA DAPGIALTDG EILSGIFLRL
     RKMYAEQGGA NPDQVLNMTW NYAIPHEPSS EEVAMESNGK ALADITDPAT GAVIVKKGQQ
     LSSFAQLRDD GTTSCGCWIF AGSWTPEGNQ MARRDNADPS GLGNTLGWAW AWPLNRRILY
     NRASADPQGN PWDPKRQLLK WDGTKWTGWD IPDYSAAPPG SGVGPFIMQQ EGMGRLFALD
     KMAEGPFPEH YEPFETPLGT NPLHPNVISN PAARIFKDDA EALGKADKFP YVGTTYRLTE
     HFHYWTKHAL LNAILQPEQF VEIGESLANK LGIAQGDTVK VSSNRGYIKA KAVVTKRIRT
     LKANGKDIDT IGIPIHWGYE GVAKKGFIAN TLTPFVGDAN TQTPEFKSFL VNVEKV
//