MHPD_ECOLI
ID MHPD_ECOLI Reviewed; 269 AA.
AC P77608; P71205; P77045; Q2MC74;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=2-keto-4-pentenoate hydratase;
DE EC=4.2.1.80 {ECO:0000269|PubMed:9492273};
DE AltName: Full=2-hydroxypentadienoic acid hydratase {ECO:0000303|PubMed:9492273};
GN Name=mhpD {ECO:0000303|PubMed:9492273}; OrderedLocusNames=b0350, JW0341;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Kawamukai M.;
RT "Complete sequence of the mhp operon.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS520;
RX PubMed=9098055; DOI=10.1128/jb.179.8.2573-2581.1997;
RA Ferrandez A., Garcia J.L., Diaz E.;
RT "Genetic characterization and expression in heterologous hosts of the 3-(3-
RT hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.";
RL J. Bacteriol. 179:2573-2581(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-6, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9492273; DOI=10.1046/j.1432-1327.1998.2510098.x;
RA Pollard J.R., Bugg T.D.H.;
RT "Purification, characterisation and reaction mechanism of monofunctional 2-
RT hydroxypentadienoic acid hydratase from Escherichia coli.";
RL Eur. J. Biochem. 251:98-106(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of 2-hydroxypentadienoic acid hydratase from Escherichia
RT coli.";
RL Submitted (JAN-2005) to the PDB data bank.
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:0000269|PubMed:9492273}.
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:0000269|PubMed:9492273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9492273};
CC Note=Divalent metal ions. Optimum activity is obtained with Mn(2+).
CC {ECO:0000269|PubMed:9492273};
CC -!- ACTIVITY REGULATION: Inhibited by sodium oxalate.
CC {ECO:0000269|PubMed:9492273}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41 uM for 2-hydroxy-pentadienoic acid (at pH 6)
CC {ECO:0000269|PubMed:9492273};
CC Note=kcat is 450 sec(-1). {ECO:0000269|PubMed:9492273};
CC pH dependence:
CC Optimum pH is 5.5-8.0, but decreases linearly above pH 8.3, and shows
CC an inflection at pH 5.5. {ECO:0000269|PubMed:9492273};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000305|PubMed:9492273}.
CC -!- SIMILARITY: Belongs to the hydratase/decarboxylase family. MhpD
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18074.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13055.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86239; BAA13055.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y09555; CAA70750.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18074.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73453.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76132.1; -; Genomic_DNA.
DR PIR; F64762; F64762.
DR RefSeq; NP_414884.2; NC_000913.3.
DR RefSeq; WP_000160710.1; NZ_SSZK01000061.1.
DR PDB; 1SV6; X-ray; 2.90 A; A/B/C/D/E=1-269.
DR PDB; 2WQT; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-269.
DR PDBsum; 1SV6; -.
DR PDBsum; 2WQT; -.
DR AlphaFoldDB; P77608; -.
DR SMR; P77608; -.
DR BioGRID; 4260731; 5.
DR IntAct; P77608; 3.
DR STRING; 511145.b0350; -.
DR SwissLipids; SLP:000001886; -.
DR jPOST; P77608; -.
DR PaxDb; P77608; -.
DR PRIDE; P77608; -.
DR EnsemblBacteria; AAC73453; AAC73453; b0350.
DR EnsemblBacteria; BAE76132; BAE76132; BAE76132.
DR GeneID; 944768; -.
DR KEGG; ecj:JW0341; -.
DR KEGG; eco:b0350; -.
DR PATRIC; fig|1411691.4.peg.1928; -.
DR EchoBASE; EB4022; -.
DR eggNOG; COG3971; Bacteria.
DR HOGENOM; CLU_060136_4_1_6; -.
DR InParanoid; P77608; -.
DR OMA; IRDWSIG; -.
DR PhylomeDB; P77608; -.
DR BioCyc; EcoCyc:MHPDHYDROL-MON; -.
DR BioCyc; MetaCyc:MHPDHYDROL-MON; -.
DR BRENDA; 4.2.1.80; 2165.
DR SABIO-RK; P77608; -.
DR UniPathway; UPA00714; -.
DR EvolutionaryTrace; P77608; -.
DR PRO; PR:P77608; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0008684; F:2-oxopent-4-enoate hydratase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019439; P:aromatic compound catabolic process; NAS:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Lyase; Reference proteome.
FT CHAIN 1..269
FT /note="2-keto-4-pentenoate hydratase"
FT /id="PRO_0000096469"
FT CONFLICT 202
FT /note="G -> E (in Ref. 1; BAA13055)"
FT /evidence="ECO:0000305"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:2WQT"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2WQT"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2WQT"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2WQT"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:2WQT"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:2WQT"
SQ SEQUENCE 269 AA; 28890 MW; 34A81A8A4E236358 CRC64;
MTKHTLEQLA ADLRRAAEQG EAIAPLRDLI GIDNAEAAYA IQHINVQHDV AQGRRVVGRK
VGLTHPKVQQ QLGVDQPDFG TLFADMCYGD NEIIPFSRVL QPRIEAEIAL VLNRDLPATD
ITFDELYNAI EWVLPALEVV GSRIRDWSIQ FVDTVADNAS CGVYVIGGPA QRPAGLDLKN
CAMKMTRNNE EVSSGRGSEC LGHPLNAAVW LARKMASLGE PLRTGDIILT GALGPMVAVN
AGDRFEAHIE GIGSVAATFS SAAPKGSLS
