B7M2Z7 (MHPC_ECO8A) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	mhpC
Ordered Locus Names:	ECIAI1_0350

Organism

Escherichia coli O8 (strain IAI1) [Complete proteome] [HAMAP]

Taxonomic identifier

585034 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity. HAMAP-Rule MF_01654
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 By similarity. HAMAP-Rule MF_01654
Sequence similarities	Belongs to the MhpC alpha/beta hydrolase family.
Sequence caution	The sequence CAQ97224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	3-phenylpropionate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity Inferred from electronic annotation. Source: EC 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 288	288	2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase HAMAP-Rule MF_01654		PRO_1000187015
Sites
	Active site	267	1	Proton acceptor By similarity
	Site	114	1	Transition state stabilizer By similarity
	Site	192	1	Catalytic role in ketonization of the dienol substrate (substrate destabilization) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7M2Z7 [UniParc]. Last modified December 14, 2011. Version 2. Checksum: C039CEE82DBA57CD	FASTA	288	31,937
	10 20 30 40 50 60 MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG WANFSRNIDP 70 80 90 100 110 120 LVEAGYRVIL LDCPGWGKSD SIVNSGSRSD LNARILKSVV DQLDIAKIHL LGNSMGGHSS 130 140 150 160 170 180 VAFTLNWPER 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

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IAI1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928160 Genomic DNA. Translation: CAQ97224.1. Different initiation.
RefSeq	YP_002385828.1. NC_011741.1.
3D structure databases
ProteinModelPortal	B7M2Z7.
SMR	B7M2Z7. Positions 3-288.
ModBase	Search...
Protein-protein interaction databases
STRING	585034.ECIAI1_0350.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ97224; CAQ97224; ECIAI1_0350.
GeneID	7124263.
KEGG	ecr:ECIAI1_0350.
PATRIC	18319970. VBIEscCol26572_0343.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0596.
HOGENOM	HOG000028063.
KO	K05714.
ProtClustDB	CLSK879654.
Enzyme and pathway databases
BioCyc	ECOL585034:GJ84-351-MONOMER.
UniPathway	UPA00714.
Family and domain databases
HAMAP	MF_01654. MhpC.
InterPro	IPR000073. AB_hydrolase_1. IPR000639. Epox_hydrolase-like. IPR023791. MhpC_alpha/beta_hydrolase. [Graphical view]
PRINTS	PR00111. ABHYDROLASE. PR00412. EPOXHYDRLASE.
ProtoNet	Search...

Entry information

Entry name

MHPC_ECO8A

Accession

Primary (citable) accession number: B7M2Z7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	December 14, 2011
Last modified:	May 1, 2013
This is version 33 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program