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Protein

2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase

Gene

mhpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain.2 Publications

Catalytic activityi

(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate.
(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate.

Kineticsi

  1. KM=2.1 µM for 2-hydroxy-6-oxononadienedioate (at pH 8)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei114 – 1141Transition state stabilizer
Sitei192 – 1921Catalytic role in ketonization of the dienol substrate (substrate destabilization)
Active sitei267 – 2671Proton acceptor

GO - Molecular functioni

  1. 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity Source: EcoCyc
  2. 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity Source: EcoCyc
  3. hydrolase activity Source: EcoliWiki

GO - Biological processi

  1. 3-(3-hydroxy)phenylpropionate catabolic process Source: EcoCyc
  2. 3-phenylpropionate catabolic process Source: UniProtKB-UniPathway
  3. aromatic compound catabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

BioCyciEcoCyc:MHPCHYDROL-MONOMER.
ECOL316407:JW0340-MONOMER.
MetaCyc:MHPCHYDROL-MONOMER.
BRENDAi3.7.1.14. 2026.
UniPathwayiUPA00714.

Protein family/group databases

MEROPSiS33.995.

Names & Taxonomyi

Protein namesi
Recommended name:
2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase (EC:3.7.1.14)
Alternative name(s):
2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase
2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase
2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase
Gene namesi
Name:mhpC
Ordered Locus Names:b0349, JW0340
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG20275. mhpC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441S → A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate. 1 Publication
Mutagenesisi113 – 1131N → A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication
Mutagenesisi113 – 1131N → H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication
Mutagenesisi114 – 1141S → A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. 1 Publication
Mutagenesisi114 – 1141S → G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. 1 Publication
Mutagenesisi118 – 1181H → A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity. 1 Publication
Mutagenesisi177 – 1771F → D: 100-fold decrease in catalytic activity. 1 Publication
Mutagenesisi177 – 1771F → G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively. 1 Publication
Mutagenesisi192 – 1921R → K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively. 1 Publication
Mutagenesisi192 – 1921R → Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively. 1 Publication
Mutagenesisi265 – 2651C → A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication
Mutagenesisi267 – 2671H → A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage. 1 Publication
Mutagenesisi268 – 2681W → G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 2882872-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolasePRO_0000207054Add
BLAST

Proteomic databases

PaxDbiP77044.
PRIDEiP77044.

Expressioni

Gene expression databases

GenevestigatoriP77044.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

DIPiDIP-10207N.
IntActiP77044. 3 interactions.
STRINGi511145.b0349.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Beta strandi12 – 198Combined sources
Beta strandi22 – 3110Combined sources
Beta strandi35 – 417Combined sources
Helixi50 – 534Combined sources
Turni54 – 574Combined sources
Helixi58 – 636Combined sources
Beta strandi67 – 715Combined sources
Helixi88 – 10215Combined sources
Beta strandi108 – 1136Combined sources
Helixi115 – 12612Combined sources
Helixi128 – 1303Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi146 – 1483Combined sources
Helixi153 – 16311Combined sources
Helixi167 – 1759Combined sources
Helixi186 – 19813Combined sources
Helixi200 – 21213Combined sources
Helixi221 – 2266Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi240 – 2423Combined sources
Helixi245 – 2539Combined sources
Beta strandi258 – 2647Combined sources
Helixi269 – 2724Combined sources
Helixi274 – 28512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U2EX-ray2.10A/B/C/D1-288[»]
ProteinModelPortaliP77044.
SMRiP77044. Positions 3-288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77044.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. MhpC family.Curated

Phylogenomic databases

eggNOGiCOG0596.
HOGENOMiHOG000028063.
InParanoidiP77044.
KOiK05714.
OrthoDBiEOG6PS5TK.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01654. MhpC.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023791. MhpC_alpha/beta_hydrolase.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P77044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG
60 70 80 90 100
WANFSRNIDP LVEAGYRVIL LDCPGWGKSD SVVNSGSRSD LNARILKSVV
110 120 130 140 150
DQLDIAKIHL LGNSMGGHSS VAFTLKWPER VGKLVLMGGG TGGMSLFTPM
160 170 180 190 200
PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD TSDLTDALFE ARLNNMLSRR
210 220 230 240 250
DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR FVPMDAGLRL
260 270 280
LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARP
Length:288
Mass (Da):31,937
Last modified:December 13, 2011 - v4
Checksum:i8F7E5ADE584A45BA
GO

Sequence cautioni

The sequence AAB18073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA13054.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE76131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA70749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531E → G in BAA13054 (Ref. 1) Curated

Mass spectrometryi

Molecular mass is 31717 Da from positions 8 - 288. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86239 Genomic DNA. Translation: BAA13054.1. Different initiation.
Y09555 Genomic DNA. Translation: CAA70749.1. Different initiation.
U73857 Genomic DNA. Translation: AAB18073.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73452.3.
AP009048 Genomic DNA. Translation: BAE76131.1. Different initiation.
PIRiE64762.
RefSeqiNP_414883.5. NC_000913.3.
YP_488643.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73452; AAC73452; b0349.
BAE76131; BAE76131; BAE76131.
GeneIDi12931735.
944954.
KEGGiecj:Y75_p0338.
eco:b0349.
PATRICi32115831. VBIEscCol129921_0357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86239 Genomic DNA. Translation: BAA13054.1. Different initiation.
Y09555 Genomic DNA. Translation: CAA70749.1. Different initiation.
U73857 Genomic DNA. Translation: AAB18073.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73452.3.
AP009048 Genomic DNA. Translation: BAE76131.1. Different initiation.
PIRiE64762.
RefSeqiNP_414883.5. NC_000913.3.
YP_488643.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U2EX-ray2.10A/B/C/D1-288[»]
ProteinModelPortaliP77044.
SMRiP77044. Positions 3-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10207N.
IntActiP77044. 3 interactions.
STRINGi511145.b0349.

Protein family/group databases

MEROPSiS33.995.

Proteomic databases

PaxDbiP77044.
PRIDEiP77044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73452; AAC73452; b0349.
BAE76131; BAE76131; BAE76131.
GeneIDi12931735.
944954.
KEGGiecj:Y75_p0338.
eco:b0349.
PATRICi32115831. VBIEscCol129921_0357.

Organism-specific databases

EchoBASEiEB4168.
EcoGeneiEG20275. mhpC.

Phylogenomic databases

eggNOGiCOG0596.
HOGENOMiHOG000028063.
InParanoidiP77044.
KOiK05714.
OrthoDBiEOG6PS5TK.

Enzyme and pathway databases

UniPathwayiUPA00714.
BioCyciEcoCyc:MHPCHYDROL-MONOMER.
ECOL316407:JW0340-MONOMER.
MetaCyc:MHPCHYDROL-MONOMER.
BRENDAi3.7.1.14. 2026.

Miscellaneous databases

EvolutionaryTraceiP77044.
PROiP77044.

Gene expression databases

GenevestigatoriP77044.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01654. MhpC.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023791. MhpC_alpha/beta_hydrolase.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence of the mhp operon."
    Kawamukai M.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12."
    Ferrandez A., Garcia J.L., Diaz E.
    J. Bacteriol. 179:2573-2581(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A HYDROLASE.
    Strain: K12 / CS520.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Purification, characterization, and stereochemical analysis of a C-C hydrolase: 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase."
    Lam W.W., Bugg T.D.
    Biochemistry 36:12242-12251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-18, FUNCTION AS A HYDROLASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  7. "Catalytic mechanism of C-C hydrolase MhpC from Escherichia coli: kinetic analysis of His263 and Ser110 site-directed mutants."
    Li C., Montgomery M.G., Mohammed F., Li J.-J., Wood S.P., Bugg T.D.H.
    J. Mol. Biol. 346:241-251(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-44; SER-114; HIS-118 AND HIS-267, CATALYTIC MECHANISM.
  8. "Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD."
    Li C., Li J.-J., Montgomery M.G., Wood S.P., Bugg T.D.H.
    Biochemistry 45:12470-12479(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-113; PHE-177; ARG-192; CYS-265 AND TRP-268, CATALYTIC MECHANISM.
  9. "The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism."
    Dunn G., Montgomery M.G., Mohammed F., Coker A., Cooper J.B., Robertson T., Garcia J.-L., Bugg T.D.H., Wood S.P.
    J. Mol. Biol. 346:253-265(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-288 IN COMPLEX WITH A NON-CLEAVABLE SUBSTRATE ANALOG, MASS SPECTROMETRY, SUBUNIT.

Entry informationi

Entry nameiMHPC_ECOLI
AccessioniPrimary (citable) accession number: P77044
Secondary accession number(s): P71204, P77205, Q2MC75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: December 13, 2011
Last modified: March 31, 2015
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

MhpC is not a serine hydrolase (catalytic triad), as Ser-114 is a non-nucleophilic catalytic residue and Asp-239 is not involved in the catalytic mechanism.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.