(data stored in SCRATCH zone)

SWISSPROT: C8U243_ECO10

ID   C8U243_ECO10            Unreviewed;       269 AA.
AC   C8U243;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=2-keto-4-pentenoate hydratase {ECO:0000256|HAMAP-Rule:MF_01655};
DE            EC=4.2.1.80 {ECO:0000256|HAMAP-Rule:MF_01655};
DE   AltName: Full=2-hydroxypentadienoic acid hydratase {ECO:0000256|HAMAP-Rule:MF_01655};
GN   Name=mhpD {ECO:0000256|HAMAP-Rule:MF_01655,
GN   ECO:0000313|EMBL:BAI29201.1};
GN   OrderedLocusNames=ECO103_0332 {ECO:0000313|EMBL:BAI29201.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29201.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29201.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the conversion of 2-hydroxypentadienoic acid
CC       (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic
CC       acid. {ECO:0000256|HAMAP-Rule:MF_01655}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-
CC         dienoate + H2O; Xref=Rhea:RHEA:22580, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:67152, ChEBI:CHEBI:73143; EC=4.2.1.80;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01655};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01655};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation. {ECO:0000256|HAMAP-Rule:MF_01655}.
CC   -!- SIMILARITY: Belongs to the hydratase/decarboxylase family. MhpD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01655}.
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DR   EMBL; AP010958; BAI29201.1; -; Genomic_DNA.
DR   RefSeq; WP_000160720.1; NC_013353.1.
DR   SMR; C8U243; -.
DR   EnsemblBacteria; BAI29201; BAI29201; ECO103_0332.
DR   KEGG; eoh:ECO103_0332; -.
DR   HOGENOM; HOG000179637; -.
DR   KO; K02554; -.
DR   OMA; IRDWSIG; -.
DR   BioCyc; ECOL585395:ECO103_RS01735-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0008684; F:2-oxopent-4-enoate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.850.10; -; 1.
DR   HAMAP; MF_01655; MhpD; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR023793; Keto_pentenoate-hydratase.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U243.
DR   SWISS-2DPAGE; C8U243.
KW   Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01655}.
FT   DOMAIN      100    259       FAA_hydrolase. {ECO:0000259|Pfam:
FT                                PF01557}.
SQ   SEQUENCE   269 AA;  28860 MW;  D45A141454878C59 CRC64;
     MTKHTLEQLA ADLRRAAEQG EAIAPLRDLI GIDNAEAAYA IQHINVQYDV AQGRRVVGRK
     VGLTHPKVQQ QLGVDQPDFG TLFADMCYGD NEIIPFSRVL QARIEAEIAL VLNRDLPATD
     ITFDELYNAI EWVLPALEVV GSRIRDWSIQ FVDTVADNAS CGVYVIGGPA QRPAGLDLKN
     CAMKMTRNNE EVSSGRGSEC LGHPLNAAVW LARKMASLGE PLRAGDIILT GALGPMVAVN
     AGDRFEAHIE GIGSVAATFS SAAPKGSLS
//

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