MHPD_ECO81
ID MHPD_ECO81 Reviewed; 269 AA.
AC B7MPB7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=2-keto-4-pentenoate hydratase {ECO:0000255|HAMAP-Rule:MF_01655};
DE EC=4.2.1.80 {ECO:0000255|HAMAP-Rule:MF_01655};
DE AltName: Full=2-hydroxypentadienoic acid hydratase {ECO:0000255|HAMAP-Rule:MF_01655};
GN Name=mhpD {ECO:0000255|HAMAP-Rule:MF_01655}; OrderedLocusNames=ECED1_0378;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the conversion of 2-hydroxypentadienoic acid
CC (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01655};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01655};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01655}.
CC -!- SIMILARITY: Belongs to the hydratase/decarboxylase family. MhpD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01655}.
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DR EMBL; CU928162; CAR06589.1; -; Genomic_DNA.
DR RefSeq; WP_000160740.1; NC_011745.1.
DR AlphaFoldDB; B7MPB7; -.
DR SMR; B7MPB7; -.
DR EnsemblBacteria; CAR06589; CAR06589; ECED1_0378.
DR KEGG; ecq:ECED1_0378; -.
DR HOGENOM; CLU_060136_4_1_6; -.
DR OMA; IRDWSIG; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000000748; 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;
KW Aromatic hydrocarbons catabolism; Lyase.
FT CHAIN 1..269
FT /note="2-keto-4-pentenoate hydratase"
FT /id="PRO_1000187023"
SQ SEQUENCE 269 AA; 28887 MW; B1916D968B540321 CRC64;
MTKHTLEQLA ADLRRAAEQG EAIAPLRDLI GIDNAEAAYV ILHINVQYDV AQGRRVVGRK
VGLTHPKVQQ QLGVDQPDFG TLFADMCYGD NETIPFSRVL QPRIEAEIAL VLNRDLPATD
ITFDELYNAI EWVLPALEVV GSRIRDWSIQ FVDTVADNAS CGVYVIGGPA QRPAGLDLKN
CAMKMTRNNE EVSSGRGSEC LGHPLNAAVW LARKMASLGE PLRAGDIILT GALGPMVAVN
AGDRFEAHIE GIGSVAATFS SAAPKGSLS