FDOI_ECOL6
ID FDOI_ECOL6 Reviewed; 211 AA.
AC P0AEL1; P32174;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=c4842;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83271.1; -; Genomic_DNA.
DR RefSeq; WP_000829013.1; NC_004431.1.
DR AlphaFoldDB; P0AEL1; -.
DR SMR; P0AEL1; -.
DR STRING; 199310.c4842; -.
DR EnsemblBacteria; AAN83271; AAN83271; c4842.
DR GeneID; 66672199; -.
DR KEGG; ecc:c4842; -.
DR eggNOG; COG2864; Bacteria.
DR HOGENOM; CLU_091368_1_1_6; -.
DR OMA; DIVWAKN; -.
DR BioCyc; ECOL199310:C4842-MON; -.
DR Proteomes; UP000001410; 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..211
FT /note="Formate dehydrogenase, cytochrome b556(fdo) subunit"
FT /id="PRO_0000087214"
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
