FDOI_ECO57
ID FDOI_ECO57 Reviewed; 211 AA.
AC P0AEL2; P32174;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Z5434, ECs4818;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59085.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38241.1; -; Genomic_DNA.
DR PIR; A86078; A86078.
DR PIR; B91231; B91231.
DR RefSeq; NP_312845.1; NC_002695.1.
DR RefSeq; WP_000829013.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEL2; -.
DR SMR; P0AEL2; -.
DR STRING; 155864.EDL933_5216; -.
DR PRIDE; P0AEL2; -.
DR EnsemblBacteria; AAG59085; AAG59085; Z5434.
DR EnsemblBacteria; BAB38241; BAB38241; ECs_4818.
DR GeneID; 66672199; -.
DR GeneID; 915078; -.
DR KEGG; ece:Z5434; -.
DR KEGG; ecs:ECs_4818; -.
DR PATRIC; fig|386585.9.peg.5034; -.
DR eggNOG; COG2864; Bacteria.
DR HOGENOM; CLU_091368_1_1_6; -.
DR OMA; DIVWAKN; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
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 3: Inferred from homology;
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_0000087215"
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
