FDOH_ECOLI
ID FDOH_ECOLI Reviewed; 300 AA.
AC P0AAJ5; P32175; Q2M8J0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Formate dehydrogenase-O iron-sulfur subunit;
DE AltName: Full=Aerobic formate dehydrogenase iron-sulfur subunit;
DE AltName: Full=FDH-Z subunit beta;
DE AltName: Full=Formate dehydrogenase-O subunit beta;
GN Name=fdoH; OrderedLocusNames=b3893, JW3864;
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).
CC -!- FUNCTION: Allows to use formate as major electron donor during aerobic
CC respiration. The beta chain is an electron transfer unit containing 4
CC cysteine clusters involved in the formation of iron-sulfur centers.
CC Electrons are transferred from the gamma chain to the molybdenum
CC cofactor of the alpha subunit (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AAJ3};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P0AAJ3};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed by
CC subunits alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L19201; AAB03026.1; -; Genomic_DNA.
DR EMBL; U00096; AAD13455.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77416.1; -; Genomic_DNA.
DR PIR; S40837; S40837.
DR RefSeq; NP_418329.1; NC_000913.3.
DR RefSeq; WP_000331377.1; NZ_SSZK01000026.1.
DR AlphaFoldDB; P0AAJ5; -.
DR SMR; P0AAJ5; -.
DR BioGRID; 4263325; 24.
DR ComplexPortal; CPX-6029; Formate dehydrogenase Z complex.
DR IntAct; P0AAJ5; 4.
DR STRING; 511145.b3893; -.
DR jPOST; P0AAJ5; -.
DR PaxDb; P0AAJ5; -.
DR PRIDE; P0AAJ5; -.
DR EnsemblBacteria; AAD13455; AAD13455; b3893.
DR EnsemblBacteria; BAE77416; BAE77416; BAE77416.
DR GeneID; 67417236; -.
DR GeneID; 948395; -.
DR KEGG; ecj:JW3864; -.
DR KEGG; eco:b3893; -.
DR PATRIC; fig|1411691.4.peg.2816; -.
DR EchoBASE; EB1803; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_0_3_6; -.
DR InParanoid; P0AAJ5; -.
DR OMA; KACQSAC; -.
DR PhylomeDB; P0AAJ5; -.
DR BioCyc; EcoCyc:FDOH-MON; -.
DR BioCyc; MetaCyc:FDOH-MON; -.
DR PRO; PR:P0AAJ5; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IDA:EcoCyc.
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:0045333; P:cellular respiration; IEP:EcoCyc.
DR GO; GO:0015944; P:formate oxidation; IDA:EcoCyc.
DR GO; GO:0006788; P:heme oxidation; IC:ComplexPortal.
DR CDD; cd10558; FDH-N; 1.
DR Gene3D; 1.20.5.480; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006470; Formate_DH_bsu_Proteobacteria.
DR InterPro; IPR038384; Formate_DH_C_sf.
DR InterPro; IPR014603; Formate_DH_Fe-S_su.
DR InterPro; IPR015246; Formate_DH_TM.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF09163; Form-deh_trans; 1.
DR PIRSF; PIRSF036298; FDH_4Fe4S; 1.
DR TIGRFAMs; TIGR01582; FDH-beta; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..300
FT /note="Formate dehydrogenase-O iron-sulfur subunit"
FT /id="PRO_0000159249"
FT TOPO_DOM 1..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9852007"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 280..300
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9852007"
FT DOMAIN 30..60
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 91..123
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 124..153
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 158..189
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
SQ SEQUENCE 300 AA; 33100 MW; 950B40FE1A6016E7 CRC64;
MAYQSQDIIR RSATNGLTPA PQARDFQEEV AKLIDVTTCI GCKACQVACS EWNDIRDTVG
NNIGVYDNPN DLSAKSWTVM RFSEVEQNDK LEWLIRKDGC MHCSDPGCLK ACPAEGAIIQ
YANGIVDFQS EQCIGCGYCI AGCPFDIPRL NPEDNRVYKC TLCVDRVVVG QEPACVKTCP
TGAIHFGTKE SMKTLASERV AELKTRGYDN AGLYDPAGVG GTHVMYVLHH ADKPNLYHGL
PENPEISETV KFWKGIWKPL AAVGFAATFA ASIFHYVGVG PNRADEEENN LHEEKDEERK
