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Database: UniProt
Entry: P23481
LinkDB: P23481
Original site: P23481 
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   10-APR-2019, entry version 137.
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
RT   coli 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.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of 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.,
RA   Mau B., 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
RT   MG1655 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
RT   proton-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.,
RA   Harper R., 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
RT   hydrogenase 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;
CC         Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- INDUCTION: Most efficiently induced by formate during post-
CC       exponential growth at low external pH (pH 6.5) in the absence of
CC       respiratory electron acceptors O(2+), NO(3-) or trimethylamine-N-
CC       oxide, i.e. under anaerobic control (PubMed:12426353,
CC       PubMed:14702328). Transcription is activated by FhlA and HyfR,
CC       inhibited by HycA, part of the sigma-54 (rpoN) regulon
CC       (PubMed:12426353). Subject to catabolite repression
CC       (PubMed:14702328). First member of a 10 gene operon
CC       (hyfABCDEFGHIJ); it is not clear if the 2 following genes (hydR-
CC       focB) are also in the operon (PubMed:12426353).
CC       {ECO:0000269|PubMed:12426353, ECO:0000269|PubMed:14702328}.
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   ProteinModelPortal; P23481; -.
DR   SMR; 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   jPOST; P23481; -.
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   EcoGene; EG11150; hyfA.
DR   eggNOG; ENOG4108MFN; Bacteria.
DR   eggNOG; COG1142; LUCA.
DR   HOGENOM; HOG000163385; -.
DR   InParanoid; P23481; -.
DR   KO; K12136; -.
DR   PhylomeDB; P23481; -.
DR   BioCyc; EcoCyc:MONOMER0-152; -.
DR   BioCyc; ECOL316407:JW2466-MONOMER; -.
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:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0004159; F:dihydrouracil dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0002058; F:uracil binding; IBA:GO_Central.
DR   GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR   GO; GO:0006212; P:uracil catabolic process; IBA:GO_Central.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF12798; Fer4_3; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Reference proteome; Repeat; Transport.
FT   CHAIN         1    205       Hydrogenase-4 component A.
FT                                /FTId=PRO_0000159267.
FT   DOMAIN        2     31       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       41     72       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       73    102       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      140    172       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        12     12       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        15     15       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        18     18       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        22     22       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        51     51       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        54     54       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        59     59       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        63     63       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL        82     82       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL        85     85       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL        88     88       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL        92     92       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       146    146       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       149    149       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       158    158       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       162    162       Iron-sulfur 1 (4Fe-4S). {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
//
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