ID HYCF_ECOLI Reviewed; 180 AA.
AC P16432; Q2MAA9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Formate hydrogenlyase subunit 6;
DE Short=FHL subunit 6;
DE AltName: Full=Hydrogenase-3 component F;
GN Name=hycF; Synonyms=hevF; OrderedLocusNames=b2720, JW2690;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2187144; DOI=10.1111/j.1365-2958.1990.tb00590.x;
RA Boehm R., Sauter M., Boeck A.;
RT "Nucleotide sequence and expression of an operon in Escherichia coli coding
RT for formate hydrogenlyase components.";
RL Mol. Microbiol. 4:231-243(1990).
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).
CC -!- FUNCTION: Probable electron transfer protein for hydrogenase 3.
CC -!- SUBUNIT: FHL comprises of a formate dehydrogenase, unidentified
CC electron carriers and a hydrogenase (isoenzyme 3). In this non-energy
CC conserving pathway, molecular hydrogen and carbodioxide are released
CC from formate.
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DR EMBL; X17506; CAA35551.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69230.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75762.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76797.1; -; Genomic_DNA.
DR PIR; S08624; S08624.
DR RefSeq; NP_417200.1; NC_000913.3.
DR RefSeq; WP_000493781.1; NZ_LN832404.1.
DR PDB; 7Z0S; EM; 2.60 A; F=1-180.
DR PDB; 7Z0T; EM; 3.40 A; F=1-180.
DR PDBsum; 7Z0S; -.
DR PDBsum; 7Z0T; -.
DR AlphaFoldDB; P16432; -.
DR EMDB; EMD-14429; -.
DR EMDB; EMD-14430; -.
DR SMR; P16432; -.
DR BioGRID; 4262940; 11.
DR BioGRID; 851386; 1.
DR ComplexPortal; CPX-317; Formate hydrogenlyase-H/Hydrogenase-3 complex.
DR IntAct; P16432; 10.
DR MINT; P16432; -.
DR STRING; 511145.b2720; -.
DR TCDB; 3.D.1.9.2; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; 511145-b2720; -.
DR EnsemblBacteria; AAC75762; AAC75762; b2720.
DR GeneID; 947048; -.
DR KEGG; ecj:JW2690; -.
DR KEGG; eco:b2720; -.
DR PATRIC; fig|1411691.4.peg.4021; -.
DR EchoBASE; EB0474; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_3_1_6; -.
DR InParanoid; P16432; -.
DR OMA; EHHRESF; -.
DR OrthoDB; 9808559at2; -.
DR PhylomeDB; P16432; -.
DR BioCyc; EcoCyc:HYCF-MONOMER; -.
DR BioCyc; MetaCyc:HYCF-MONOMER; -.
DR PRO; PR:P16432; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR GO; GO:0015944; P:formate oxidation; IDA:ComplexPortal.
DR GO; GO:0006007; P:glucose catabolic process; IDA:ComplexPortal.
DR CDD; cd10549; MtMvhB_like; 1.
DR Gene3D; 3.30.70.3270; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849:SF36; FORMATE HYDROGENLYASE SUBUNIT 6-RELATED; 1.
DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..180
FT /note="Formate hydrogenlyase subunit 6"
FT /id="PRO_0000159266"
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 66..95
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 40
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 20309 MW; 284B8C507B47DFDC CRC64;
MFTFIKKVIK TGTATSSYPL EPIAVDKNFR GKPEQNPQQC IGCAACVNAC PSNALTVETD
LATGELAWEF NLGHCIFCGR CEEVCPTAAI KLSQEYELAV WKKEDFLQQS RFALCNCRVC
NRPFAVQKEI DYAIALLKHN GDSRAENHRE SFETCPECKR QKCLVPSDRI ELTRHMKEAI
//
