MHPD_ECO55
ID MHPD_ECO55 Reviewed; 269 AA.
AC B7L506;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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};
GN OrderedLocusNames=EC55989_0357;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
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; CU928145; CAU96234.1; -; Genomic_DNA.
DR RefSeq; WP_000160720.1; NC_011748.1.
DR AlphaFoldDB; B7L506; -.
DR SMR; B7L506; -.
DR EnsemblBacteria; CAU96234; CAU96234; EC55989_0357.
DR KEGG; eck:EC55989_0357; -.
DR HOGENOM; CLU_060136_4_1_6; -.
DR OMA; IRDWSIG; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000000746; 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_1000187020"
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