(data stored in ACNUC7421 zone)

SWISSPROT: MHPC_ECO57

ID   MHPC_ECO57              Reviewed;         288 AA.
AC   Q8X5K0; Q7AH52;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 3.
DT   05-JUL-2017, entry version 101.
DE   RecName: Full=2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase;
DE            EC=3.7.1.14;
DE   AltName: Full=2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase;
DE   AltName: Full=2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase;
DE   AltName: Full=2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase;
GN   Name=mhpC; OrderedLocusNames=Z0447, ECs0404;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-
CC       oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol
CC       ring fission product of the bacterial meta-cleavage pathway for
CC       degradation of phenylpropionic acid. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-
CC       dioate + H(2)O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate.
CC   -!- CATALYTIC ACTIVITY: (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-
CC       1,9-dioate + H(2)O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate.
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MhpC family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG54700.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAB33827.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG54700.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33827.1; ALT_INIT; Genomic_DNA.
DR   PIR; D90679; D90679.
DR   PIR; H85529; H85529.
DR   RefSeq; NP_308431.3; NC_002695.1.
DR   RefSeq; WP_000121896.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; Q8X5K0; -.
DR   SMR; Q8X5K0; -.
DR   STRING; 155864.Z0447; -.
DR   ESTHER; ecoli-mhpc; Carbon-carbon_bond_hydrolase.
DR   EnsemblBacteria; AAG54700; AAG54700; Z0447.
DR   EnsemblBacteria; BAB33827; BAB33827; BAB33827.
DR   GeneID; 914506; -.
DR   KEGG; ece:Z0447; -.
DR   KEGG; ecs:ECs0404; -.
DR   PATRIC; fig|386585.9.peg.499; -.
DR   eggNOG; ENOG4106HB6; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000028063; -.
DR   KO; K05714; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0052823; F:2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018771; F:2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01654; MhpC; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR023791; MhpC_alpha/beta_hydrolase.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X5K0.
DR   SWISS-2DPAGE; Q8X5K0.
KW   Aromatic hydrocarbons catabolism; Complete proteome; Hydrolase.
FT   CHAIN         1    288       2-hydroxy-6-oxononadienedioate/2-hydroxy-
FT                                6-oxononatrienedioate hydrolase.
FT                                /FTId=PRO_0000337781.
FT   DOMAIN       38    273       AB hydrolase-1. {ECO:0000255}.
FT   ACT_SITE    267    267       Proton acceptor. {ECO:0000250}.
FT   SITE        114    114       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   SITE        192    192       Catalytic role in ketonization of the
FT                                dienol substrate (substrate
FT                                destabilization). {ECO:0000250}.
SQ   SEQUENCE   288 AA;  31911 MW;  DA89CEE82DBA57CD CRC64;
     MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG WANFSRNIDP
     LVEAGYRVIL LDCPGWGKSD SIVNSGSRSD LNARILKSVV DQLDIAKIHL LGNSMGGHSS
     VAFTLNWPER VGKLVLMGGG TGGMSLFTPM PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD
     TSDLTDALFE ARLNNMLSRR DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR
     FVPMDAGLRL LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARA
//

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