FDOI_ECOLI
ID FDOI_ECOLI Reviewed; 211 AA.
AC P0AEL0; P32174; Q2M8I9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Formate dehydrogenase, cytochrome b556(fdo) subunit;
DE AltName: Full=Aerobic formate dehydrogenase cytochrome b556 subunit;
DE AltName: Full=FDH-Z subunit gamma;
DE AltName: Full=Formate dehydrogenase-O subunit gamma;
GN Name=fdoI; OrderedLocusNames=b3892, JW3863;
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].
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 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 TOPOLOGY.
RX PubMed=9852007; DOI=10.1128/jb.180.24.6625-6634.1998;
RA Benoit S., Abaibou H., Mandrand-Berthelot M.-A.;
RT "Topological analysis of the aerobic membrane-bound formate dehydrogenase
RT of Escherichia coli.";
RL J. Bacteriol. 180:6625-6634(1998).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Allows to use formate as major electron donor during aerobic
CC respiration. Subunit gamma is probably the cytochrome b556(FDO)
CC component of the formate dehydrogenase.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups per subunit. Heme 1 is located at the
CC cytoplasmic interface, heme 2 is located at the periplasmic interface.
CC Electrons are transferred from the periplasmic to the cytoplasmic heme.
CC {ECO:0000250};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed by
CC subunits alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family.
CC {ECO:0000305}.
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DR EMBL; L19201; AAB03025.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13454.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77417.1; -; Genomic_DNA.
DR PIR; S40836; S40836.
DR RefSeq; NP_418328.1; NC_000913.3.
DR RefSeq; WP_000829013.1; NZ_STEB01000017.1.
DR AlphaFoldDB; P0AEL0; -.
DR SMR; P0AEL0; -.
DR BioGRID; 4262641; 46.
DR ComplexPortal; CPX-6029; Formate dehydrogenase Z complex.
DR IntAct; P0AEL0; 1.
DR STRING; 511145.b3892; -.
DR jPOST; P0AEL0; -.
DR PaxDb; P0AEL0; -.
DR PRIDE; P0AEL0; -.
DR EnsemblBacteria; AAD13454; AAD13454; b3892.
DR EnsemblBacteria; BAE77417; BAE77417; BAE77417.
DR GeneID; 66672199; -.
DR GeneID; 948383; -.
DR KEGG; ecj:JW3863; -.
DR KEGG; eco:b3892; -.
DR PATRIC; fig|1411691.4.peg.2817; -.
DR EchoBASE; EB1802; -.
DR eggNOG; COG2864; Bacteria.
DR HOGENOM; CLU_091368_1_1_6; -.
DR InParanoid; P0AEL0; -.
DR OMA; DIVWAKN; -.
DR PhylomeDB; P0AEL0; -.
DR BioCyc; EcoCyc:FDOI-MON; -.
DR BioCyc; MetaCyc:FDOI-MON; -.
DR PRO; PR:P0AEL0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR InterPro; IPR006471; Formate_DH_gsu.
DR Pfam; PF01292; Ni_hydr_CYTB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR TIGRFAMs; TIGR01583; formate-DH-gamm; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..211
FT /note="Formate dehydrogenase, cytochrome b556(fdo) subunit"
FT /id="PRO_0000087213"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..32
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 33..53
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 73..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..130
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 131..151
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 171..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 18
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 24606 MW; 166AC5A661C738D5 CRC64;
MKRRDTIVRY TAPERINHWI TAFCFILAAV SGLGFLFPSF NWLMQIMGTP QLARILHPFV
GVVMFASFII MFFRYWHHNL INRDDIFWAK NIRKIVVNEE VGDTGRYNFG QKCVFWAAII
FLVLLLVSGV IIWRPYFAPA FSIPVIRFAL MLHSFAAVAL IVVIMVHIYA ALWVKGTITA
MVEGWVTSAW AKKHHPRWYR EVRKTTEKKA E
