FDOG_ECOLI
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 03-AUG-2022, entry version 193.
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; Proteobacteria; 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; P32176; -.
DR PRIDE; P32176; -.
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; KWDGAKW; -.
DR PhylomeDB; P32176; -.
DR BioCyc; EcoCyc:FDOG-MON; -.
DR BioCyc; MetaCyc:FDOG-MON; -.
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: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; IC: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:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0015944; P:formate oxidation; IDA:EcoCyc.
DR GO; GO:0006788; P:heme oxidation; IC:ComplexPortal.
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 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; SSF50692; 1.
DR TIGRFAMs; TIGR01553; formate-DH-alph; 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
