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P77044 (MHPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:mhpC
Ordered Locus Names:b0349, JW0340
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.6

Catalytic activity

(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate. HAMAP-Rule MF_01654

(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate. HAMAP-Rule MF_01654

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01654

Subunit structure

Homodimer. Ref.6 Ref.9

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.

Sequence similarities

Belongs to the AB hydrolase superfamily. MhpC family.

Biophysicochemical properties

Kinetic parameters:

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

Mass spectrometry

Molecular mass is 31717 Da from positions 8 - 288. Determined by ESI. Ref.9

Sequence caution

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

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

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 2882872-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase HAMAP-Rule MF_01654
PRO_0000207054

Sites

Active site2671Proton acceptor
Site1141Transition state stabilizer
Site1921Catalytic role in ketonization of the dienol substrate (substrate destabilization)

Experimental info

Mutagenesis441S → A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate. Ref.7
Mutagenesis1131N → A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity. Ref.8
Mutagenesis1131N → H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity. Ref.8
Mutagenesis1141S → A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. Ref.7
Mutagenesis1141S → G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. Ref.7
Mutagenesis1181H → A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity. Ref.7
Mutagenesis1771F → D: 100-fold decrease in catalytic activity. Ref.8
Mutagenesis1771F → G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively. Ref.8
Mutagenesis1921R → K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively. Ref.8
Mutagenesis1921R → Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively. Ref.8
Mutagenesis2651C → A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity. Ref.8
Mutagenesis2671H → A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage. Ref.7
Mutagenesis2681W → G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively. Ref.8
Sequence conflict1531E → G in BAA13054. Ref.1

Secondary structure

............................................... 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77044 [UniParc].

Last modified December 14, 2011. Version 4.
Checksum: 8F7E5ADE584A45BA

FASTA28831,937
        10         20         30         40         50         60 
MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG WANFSRNIDP 

        70         80         90        100        110        120 
LVEAGYRVIL LDCPGWGKSD SVVNSGSRSD LNARILKSVV DQLDIAKIHL LGNSMGGHSS 

       130        140        150        160        170        180 
VAFTLKWPER VGKLVLMGGG TGGMSLFTPM PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD 

       190        200        210        220        230        240 
TSDLTDALFE ARLNNMLSRR DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR 

       250        260        270        280 
FVPMDAGLRL LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARP 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the mhp operon."
Kawamukai M.
Submitted (JUN-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(1997) [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 (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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(2006) [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(1997) [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(2005) [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(2006) [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(2005) [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRE64762.
RefSeqNP_414883.5. NC_000913.3.
YP_488643.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U2EX-ray2.10A/B/C/D1-288[»]
ProteinModelPortalP77044.
SMRP77044. Positions 3-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10207N.
IntActP77044. 3 interactions.
STRING511145.b0349.

Protein family/group databases

MEROPSS33.995.

Proteomic databases

PaxDbP77044.
PRIDEP77044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73452; AAC73452; b0349.
BAE76131; BAE76131; BAE76131.
GeneID12931735.
944954.
KEGGecj:Y75_p0338.
eco:b0349.
PATRIC32115831. VBIEscCol129921_0357.

Organism-specific databases

EchoBASEEB4168.
EcoGeneEG20275. mhpC.

Phylogenomic databases

eggNOGCOG0596.
HOGENOMHOG000028063.
KOK05714.
OrthoDBEOG6PS5TK.
ProtClustDBCLSK879654.

Enzyme and pathway databases

BioCycEcoCyc:MHPCHYDROL-MONOMER.
ECOL316407:JW0340-MONOMER.
MetaCyc:MHPCHYDROL-MONOMER.
UniPathwayUPA00714.

Gene expression databases

GenevestigatorP77044.

Family and domain databases

HAMAPMF_01654. MhpC.
InterProIPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023791. MhpC_alpha/beta_hydrolase.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
ProtoNetSearch...

Other

EvolutionaryTraceP77044.
PROP77044.

Entry information

Entry nameMHPC_ECOLI
AccessionPrimary (citable) accession number: P77044
Secondary accession number(s): P71204, P77205, Q2MC75
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 14, 2011
Last modified: April 16, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene