P51020 (HOA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-2-oxovalerate aldolase
Short name=HOA
EC=4.1.3.39

Alternative name(s):
4-hydroxy-2-keto-pentanoic acid aldolase
4-hydroxy-2-oxopentanoate aldolase

Gene names

Name:	mhpE
Ordered Locus Names:	b0352, JW0343

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Ref.6
Catalytic activity	4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate. HAMAP MF_01656
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01656
Subunit structure	Interacts with mhpF. Ref.7
Miscellaneous	Presumably stereoselective for the 4S-enantiomer of 4-hydroxy-2-ketovalerate. HAMAP MF_01656
Sequence similarities	Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.25-6.75. Ref.6

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Manganese Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-hydroxy-2-oxovalerate aldolase activity Inferred from electronic annotation. Source: EC acetaldehyde dehydrogenase (acetylating) activity Inferred from direct assay. Source: EcoliWiki metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mhpF	P77580	1	EBI-1116093,EBI-1116083

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 337	337	4-hydroxy-2-oxovalerate aldolase HAMAP MF_01656		PRO_0000096470
Regions
	Region	14 – 15	2	Substrate binding By similarity
Sites
	Active site	18	1	Proton acceptor Potential
	Metal binding	15	1	Manganese By similarity
	Metal binding	197	1	Manganese; via tele nitrogen By similarity
	Metal binding	199	1	Manganese; via tele nitrogen By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Site	14	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51020 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: EDA263721721212F	FASTA	337	36,470
	10 20 30 40 50 60 MNGKKLYISD VTLRDGMHAI RHQYSLENVR QIAKALDDAR VDSIEVAHGD GLQGSSFNYG 70 80 90 100 110 120 FGAHSDLEWI EAAADVVKHA KIATLLLPGI GTIHDLKNAW QAGARVVRVA THCTEADVSA 130 140 150 160 170 180 QHIQYARELG MDTVGFLMMS HMTTPENLAK QAKLMEGYGA TCIYVVDSGG AMNMSDIRDR 190 200 210 220 230 240 FRALKAELKP ETQTGMHAHH NLSLGVANSI AAVEEGCDRI DASLAGMGAG AGNAPLEVFI 250 260 270 280 290 300 AAADKLGWQH GTDLYALMDA ADDLVRPLQD RPVRVDRETL ALGYAGVYSS FLRHCETAAA 310 320 330 RYGLSAVDIL VELGKRRMVG GQEDMIVDVA LDLRNNK

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]	"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.
[3]	"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.
[4]	"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.
[5]	Nashimoto H., Saito N. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-337. Strain: K12.
[6]	"Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli." Pollard J.R., Rialland D., Bugg T.D. Appl. Environ. Microbiol. 64:4093-4094(1998) [PubMed: 9758851] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBSTRATE SPECIFICITY.
[7]	"Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli." Lee S.J., Ko J.H., Kang H.Y., Lee Y. Biochem. Biophys. Res. Commun. 346:1009-1015(2006) [PubMed: 16782065] [Abstract] Cited for: INTERACTION WITH MHPF.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D86239 Genomic DNA. Translation: BAA13057.1. U73857 Genomic DNA. Translation: AAB18076.1. U00096 Genomic DNA. Translation: AAC73455.1. AP009048 Genomic DNA. Translation: BAE76134.1. D85613 Genomic DNA. No translation available.
PIR	H64762.
RefSeq	NP_414886.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P51020.
SMR	P51020. Positions 4-333.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10209N.
IntAct	P51020. 10 interactions.
Proteomic databases
PRIDE	P51020.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004643; EBESCP00000004643; EBESCG00000003786. EBESCT00000015032; EBESCP00000014323; EBESCG00000014092.
GeneID	945012.
GenomeReviews	Gene locus JW0343 in contig AP009048_GR. Gene locus b0352 in contig U00096_GR.
KEGG	ecj:JW0343. eco:b0352.
PATRIC	32115837. VBIEscCol129921_0360.
Organism-specific databases
EchoBASE	EB3077.
EcoGene	EG13292. mhpE.
Phylogenomic databases
eggNOG	COG0119.
GeneTree	EBGT00050000011169.
HOGENOM	HBG300122.
OMA	ATCVYVV.
PhylomeDB	P51020.
ProtClustDB	PRK08195.
Enzyme and pathway databases
BioCyc	EcoCyc:MHPELY-MONOMER. MetaCyc:MHPELY-MONOMER.
Gene expression databases
Genevestigator	P51020.
Family and domain databases
HAMAP	MF_01656. HOA. [Tree]
InterPro	IPR017629. 4OH_2_O-val_aldolase. IPR013785. Aldolase_TIM. IPR012425. DmpG_comm. IPR000891. PYR_CT. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K01666.
PANTHER	PTHR10277:SF3. PTHR10277:SF3. 1 hit.
Pfam	PF07836. DmpG_comm. 1 hit. PF00682. HMGL-like. 1 hit. [Graphical view]
ProDom	PD005364. DmpG_comm. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITE	PS50991. PYR_CT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HOA_ECOLI

Accession

Primary (citable) accession number: P51020
Secondary accession number(s): P77787, Q2MC72

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program