HYFA_ECOLI
ID HYFA_ECOLI Reviewed; 205 AA.
AC P23481; P76565;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Hydrogenase-4 component A;
DE EC=1.-.-.-;
GN Name=hyfA {ECO:0000303|PubMed:9387241}; Synonyms=yffE;
GN OrderedLocusNames=b2481, JW2466;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2016588; DOI=10.1099/00221287-137-2-361;
RA Andrews S.C., Harrison P.M., Guest J.R.;
RT "A molecular analysis of the 53.3 minute region of the Escherichia coli
RT linkage map.";
RL J. Gen. Microbiol. 137:361-367(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP POSSIBLE FUNCTION.
RX PubMed=9387241; DOI=10.1099/00221287-143-11-3633;
RA Andrews S.C., Berks B.C., McClay J., Ambler A., Quail M.A., Golby P.,
RA Guest J.R.;
RT "A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-
RT translocating formate hydrogenlyase system.";
RL Microbiology 143:3633-3647(1997).
RN [6]
RP INDUCTION, AND OPERON.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12426353; DOI=10.1128/jb.184.23.6642-6653.2002;
RA Skibinski D.A., Golby P., Chang Y.S., Sargent F., Hoffman R., Harper R.,
RA Guest J.R., Attwood M.M., Berks B.C., Andrews S.C.;
RT "Regulation of the hydrogenase-4 operon of Escherichia coli by the
RT sigma(54)-dependent transcriptional activators FhlA and HyfR.";
RL J. Bacteriol. 184:6642-6653(2002).
RN [7]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=14702328; DOI=10.1128/jb.186.2.580-587.2004;
RA Self W.T., Hasona A., Shanmugam K.T.;
RT "Expression and regulation of a silent operon, hyf, coding for hydrogenase
RT 4 isoenzyme in Escherichia coli.";
RL J. Bacteriol. 186:580-587(2004).
CC -!- FUNCTION: Probable electron transfer protein for hydrogenase 4.
CC {ECO:0000305|PubMed:9387241}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC -!- INDUCTION: Most efficiently induced by formate during post-exponential
CC growth at low external pH (pH 6.5) in the absence of respiratory
CC electron acceptors O(2+), NO(3-) or trimethylamine-N-oxide, i.e. under
CC anaerobic control (PubMed:12426353, PubMed:14702328). Transcription is
CC activated by FhlA and HyfR, inhibited by HycA, part of the sigma-54
CC (rpoN) regulon (PubMed:12426353). Subject to catabolite repression
CC (PubMed:14702328). First member of a 10 gene operon (hyfABCDEFGHIJ); it
CC is not clear if the 2 following genes (hydR-focB) are also in the
CC operon (PubMed:12426353). {ECO:0000269|PubMed:12426353,
CC ECO:0000269|PubMed:14702328}.
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DR EMBL; M63654; AAB88563.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75534.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16359.1; -; Genomic_DNA.
DR PIR; H65023; H65023.
DR RefSeq; NP_416976.4; NC_000913.3.
DR RefSeq; WP_001336048.1; NZ_LN832404.1.
DR AlphaFoldDB; P23481; -.
DR BioGRID; 4259199; 13.
DR DIP; DIP-9983N; -.
DR IntAct; P23481; 3.
DR STRING; 511145.b2481; -.
DR TCDB; 3.D.1.9.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P23481; -.
DR PRIDE; P23481; -.
DR EnsemblBacteria; AAC75534; AAC75534; b2481.
DR EnsemblBacteria; BAA16359; BAA16359; BAA16359.
DR GeneID; 946959; -.
DR KEGG; ecj:JW2466; -.
DR KEGG; eco:b2481; -.
DR PATRIC; fig|1411691.4.peg.4258; -.
DR EchoBASE; EB1139; -.
DR eggNOG; COG1142; Bacteria.
DR HOGENOM; CLU_043374_3_0_6; -.
DR InParanoid; P23481; -.
DR OMA; APVQCRH; -.
DR PhylomeDB; P23481; -.
DR BioCyc; EcoCyc:MON0-152; -.
DR PRO; PR:P23481; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF12798; Fer4_3; 2.
DR Pfam; PF12800; Fer4_4; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..205
FT /note="Hydrogenase-4 component A"
FT /id="PRO_0000159267"
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 41..72
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 73..102
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 140..172
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 205 AA; 22154 MW; C06ED8FB0617B46B CRC64;
MNRFVVAEPL WCTGCNTCLA ACSDVHKTQG LQQHPRLALA KTSTITAPVV CHHCEEAPCL
QVCPVNAISQ RDDAIQLNES LCIGCKLCAV VCPFGAISAS GSRPVNAHAQ YVFQAEGSLK
DGEENAPTQH ALLRWEPGVQ TVAVKCDLCD FLPEGPACVR ACPNQALRLI TGDSLQRQMK
EKQRLAASWF ANGGEDPLSL TQEQR
