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P77044

- MHPC_ECOLI

UniProt

P77044 - MHPC_ECOLI

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Protein
2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase
Gene
mhpC, b0349, JW0340
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation
(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate.UniRule annotation

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.
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: Chromosome, UP000000625: 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 hydrolaseUniRule annotation
PRO_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

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP77044.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0596.
HOGENOMiHOG000028063.
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]
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

MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG    50
WANFSRNIDP LVEAGYRVIL LDCPGWGKSD SVVNSGSRSD LNARILKSVV 100
DQLDIAKIHL LGNSMGGHSS VAFTLKWPER VGKLVLMGGG TGGMSLFTPM 150
PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD TSDLTDALFE ARLNNMLSRR 200
DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR FVPMDAGLRL 250
LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARP 288
Length:288
Mass (Da):31,937
Last modified:December 14, 2011 - v4
Checksum:i8F7E5ADE584A45BA
GO

Sequence cautioni

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.

Mass spectrometryi

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

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi E64762.
RefSeqi NP_414883.5. NC_000913.3.
YP_488643.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U2E X-ray 2.10 A/B/C/D 1-288 [» ]
ProteinModelPortali P77044.
SMRi P77044. Positions 3-288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10207N.
IntActi P77044. 3 interactions.
STRINGi 511145.b0349.

Protein family/group databases

MEROPSi S33.995.

Proteomic databases

PaxDbi P77044.
PRIDEi P77044.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73452 ; AAC73452 ; b0349 .
BAE76131 ; BAE76131 ; BAE76131 .
GeneIDi 12931735.
944954.
KEGGi ecj:Y75_p0338.
eco:b0349.
PATRICi 32115831. VBIEscCol129921_0357.

Organism-specific databases

EchoBASEi EB4168.
EcoGenei EG20275. mhpC.

Phylogenomic databases

eggNOGi COG0596.
HOGENOMi HOG000028063.
KOi K05714.
OrthoDBi EOG6PS5TK.

Enzyme and pathway databases

UniPathwayi UPA00714 .
BioCyci EcoCyc:MHPCHYDROL-MONOMER.
ECOL316407:JW0340-MONOMER.
MetaCyc:MHPCHYDROL-MONOMER.

Miscellaneous databases

EvolutionaryTracei P77044.
PROi P77044.

Gene expression databases

Genevestigatori P77044.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
HAMAPi MF_01654. MhpC.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023791. MhpC_alpha/beta_hydrolase.
[Graphical view ]
PRINTSi PR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMHPC_ECOLI
AccessioniPrimary (citable) accession number: P77044
Secondary accession number(s): P71204, P77205, Q2MC75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 14, 2011
Last modified: June 11, 2014
This is version 123 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

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