2-keto-4-pentenoate hydratase - Escherichia coli (strain K12)

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P77608 (MHPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2-keto-4-pentenoate hydratase
EC=4.2.1.80

Alternative name(s):
2-hydroxypentadienoic acid hydratase

Gene names

Name:	mhpD
Ordered Locus Names:	b0350, JW0341

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. Ref.6
Catalytic activity	4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H₂O. HAMAP MF_01655
Cofactor	Divalent metal ions. Optimum activity is obtained with Mn²⁺. Ref.6
Enzyme regulation	Inhibited by sodium oxalate. Ref.6
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01655
Sequence similarities	Belongs to the hydratase/decarboxylase family. MhpD subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=41 µM for 2-hydroxy-pentadienoic acid (at pH 6) Ref.6 pH dependence: Optimum pH is 5.5-8.0, but decreases linearly above pH 8.3, and shows an inflection at pH 5.5.
Sequence caution	The sequence AAB18074.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA13055.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2-oxopent-4-enoate hydratase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 269

269

2-keto-4-pentenoate hydratase HAMAP MF_01655

PRO_0000096469

Experimental info

Sequence conflict

202

G → E in BAA13055. Ref.1

Secondary structure

269

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P77608 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 34A81A8A4E236358
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FASTA

269

28,890

        10         20         30         40         50         60 
MTKHTLEQLA ADLRRAAEQG EAIAPLRDLI GIDNAEAAYA IQHINVQHDV AQGRRVVGRK 

        70         80         90        100        110        120 
VGLTHPKVQQ QLGVDQPDFG TLFADMCYGD NEIIPFSRVL QPRIEAEIAL VLNRDLPATD 

       130        140        150        160        170        180 
ITFDELYNAI EWVLPALEVV GSRIRDWSIQ FVDTVADNAS CGVYVIGGPA QRPAGLDLKN 

       190        200        210        220        230        240 
CAMKMTRNNE EVSSGRGSEC LGHPLNAAVW LARKMASLGE PLRTGDIILT GALGPMVAVN 

       250        260 
AGDRFEAHIE GIGSVAATFS SAAPKGSLS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	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: 9098055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli." Pollard J.R., Bugg T.D.H. Eur. J. Biochem. 251:98-106(1998) [PubMed: 9492273] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-6, COFACTOR, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Crystal structure of 2-hydroxypentadienoic acid hydratase from Escherichia coli." New York structural genomix research consortium (NYSGXRC) Submitted (JAN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86239 Genomic DNA. Translation: BAA13055.1. Different initiation.
Y09555 Genomic DNA. Translation: CAA70750.1.
U73857 Genomic DNA. Translation: AAB18074.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73453.2.
AP009048 Genomic DNA. Translation: BAE76132.1.

PIR

F64762.

RefSeq

NP_414884.2. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SV6	X-ray	2.90	A/B/C/D/E	1-269	[»]
2WQT	X-ray	2.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	1-269	[»]

ProteinModelPortal

P77608.

SMR

P77608. Positions 1-261.

ModBase

Search...

Protein-protein interaction databases

IntAct

P77608. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000250; EBESCP00000000250; EBESCG00000000206.
EBESCT00000016496; EBESCP00000015787; EBESCG00000015556.

GeneID

944768.

GenomeReviews

Gene locus JW0341 in contig AP009048_GR.
Gene locus b0350 in contig U00096_GR.

KEGG

ecj:JW0341.
eco:b0350.

PATRIC

32115833. VBIEscCol129921_0358.

Organism-specific databases

EchoBASE

EB4022.

EcoGene

EG14274. mhpD.

Phylogenomic databases

eggNOG

COG3971.

GeneTree

EBGT00050000009008.

HOGENOM

HBG483975.

OMA

YAIQRLN.

PhylomeDB

P77608.

ProtClustDB

PRK11342.

Enzyme and pathway databases

BioCyc

EcoCyc:MHPDHYDROL-MONOMER.
MetaCyc:MHPDHYDROL-MONOMER.

Gene expression databases

Genevestigator

P77608.

Family and domain databases

HAMAP

MF_01655. MhpD.
[Tree]

InterPro

IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR023793. keto_pentenoate-hydratase.
[Graphical view]

Gene3D

G3DSA:3.90.850.10. Fumarylacetoacetase_C-rel. 1 hit.

K02554.

Pfam

PF01557. FAA_hydrolase. 1 hit.
[Graphical view]

SUPFAM

SSF56529. Fumarylacetoacetase_C-rel. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MHPD_ECOLI

Accession

Primary (citable) accession number: P77608
Secondary accession number(s): P71205, P77045, Q2MC74

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1998
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents