ID E6BHH6_ECOLX Unreviewed; 271 AA.
AC E6BHH6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=HMPREF9350_01808 {ECO:0000313|EMBL:EFU36139.1};
OS Escherichia coli MS 85-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU36139.1, ECO:0000313|Proteomes:UP000005056};
RN [1] {ECO:0000313|EMBL:EFU36139.1, ECO:0000313|Proteomes:UP000005056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU36139.1,
RC ECO:0000313|Proteomes:UP000005056};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFU36139.1}.
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DR EMBL; ADWQ01000006; EFU36139.1; -; Genomic_DNA.
DR AlphaFoldDB; E6BHH6; -.
DR PATRIC; fig|679202.3.peg.1675; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000005056; Unassembled WGS sequence.
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 59..261
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 271 AA; 29144 MW; 8750A56A5C7A55E0 CRC64;
MVMTKHTLEQ LAADLRRAAE QGEAIAPLRD LIGIDNAEAA YAIQHINVQY DVVQGRRVVG
RKVGLTHPKV QQQLGVDQPD FGTLFADMCY GDNEIIPFSR VLQPRIEAEI ALVLNRDLPA
TDITFDELYN AIEWVLPALE VVGSRIRDWS IQFVDTVADN ASCGVYVIGG PAQRPAGLDL
KNCAMKMTRN NEEVSSGRGS ECLGHPLNAA VWLARKMASL GEPLRAGDII LTGALGPMVA
VNAGDRFEAH IEGIGSVAAT FSSAAPKGSL S
//
