ID E0J0Q1_ECOLW Unreviewed; 269 AA.
AC E0J0Q1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ADT73964.1};
GN OrderedLocusNames=ECW_m0428 {ECO:0000313|EMBL:ADT73964.1};
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT73964.1, ECO:0000313|Proteomes:UP000008525};
RN [1] {ECO:0000313|EMBL:ADT73964.1, ECO:0000313|Proteomes:UP000008525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
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: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 degradation.
CC {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; CP002185; ADT73964.1; -; Genomic_DNA.
DR RefSeq; WP_000160734.1; NZ_WBMH01000016.1.
DR AlphaFoldDB; E0J0Q1; -.
DR SMR; E0J0Q1; -.
DR KEGG; elw:ECW_m0428; -.
DR PATRIC; fig|566546.30.peg.437; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000008525; 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; Fumarylacetoacetase-like, C-terminal domain; 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 PANTHER; PTHR30143:SF0; 2-KETO-4-PENTENOATE HYDRATASE; 1.
DR PANTHER; PTHR30143; ACID HYDRATASE; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; FAH; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01655}; Lyase {ECO:0000256|HAMAP-Rule:MF_01655}.
FT DOMAIN 57..259
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 269 AA; 28914 MW; 4E9C4719F16BA83B CRC64;
MTKHTLEQLA ADLRRAAEQG EAIAPLRDLI GIDNAEAAYA IQHINVQYDV VQGRRVVGRK
VGLTHPKVQQ QLGVDQPDFG TLFADMCYGD NEIIPFSRVL QPRIEAEIAL VLNRDLPATD
ITFDELYNAI EWVLPALEVV GSRIRDWSIQ FVDTVADNAS CGVYVIGGPA QRPAGLDLKN
CAMKMTRNNE EVSSGRGSEC LGHPLNAAVW LARKMASLGE PLRAGDIILT GALGPMVAVN
AGDRFEAHIE GIGSVAATFS SAAPKGSLS
//
