Q0S006 (HOA5_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-2-oxovalerate aldolase 5
Short name=HOA 5
EC=4.1.3.39

Alternative name(s):
4-hydroxy-2-keto-pentanoic acid aldolase 5
4-hydroxy-2-oxopentanoate aldolase 5

Gene names

Ordered Locus Names:

RHA1_ro08083

Encoded on

Plasmid pRHL1

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus › Rhodococcus jostii

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 aromatic compounds By similarity. HAMAP-Rule MF_01656
Catalytic activity	4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate. HAMAP-Rule MF_01656
Sequence similarities	Belongs to the 4-hydroxy-2-oxovalerate aldolase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Manganese Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	4-hydroxy-2-oxovalerate aldolase activity Inferred from electronic annotation. Source: HAMAP manganese ion binding 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 – 342	342	4-hydroxy-2-oxovalerate aldolase 5 HAMAP-Rule MF_01656		PRO_0000387903
Regions
	Region	13 – 14	2	Substrate binding By similarity
Sites
	Active site	17	1	Proton acceptor Potential
	Metal binding	14	1	Manganese By similarity
	Metal binding	196	1	Manganese; via tele nitrogen By similarity
	Metal binding	198	1	Manganese; via tele nitrogen By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity
	Site	13	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0S006 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 91B8B6449D9A3F04	FASTA	342	36,405
	10 20 30 40 50 60 MTTRLFIQDV TLRDGMHAVR HRITPDDVGK IVAALDAAGV DGIEVAHGDG LAGGSLNYGP 70 80 90 100 110 120 GSNTDWEWIE AAADNLTHAR LTTLLLPGIG TIAELEHAYV LGVRSIRIAT HCTEADVSAQ 130 140 150 160 170 180 HIGKARELGM DVSGFLMMSH MASPAELAAQ AKLMESYGAH CVYVTDSGGR LTMDGVRERV 190 200 210 220 230 240 RAYRDVLDEA TEIGIHAHEN LSLSVANSVV AVEEGVTRVD ASLAGHGAGA GNCPIEPFIA 250 260 270 280 290 300 VADLQGWKHN SDLFALQDAA DDLVRPLQDR PVRVDRETLT LGYAGVYSSF LRHAEAASQR 310 320 330 340 YGIDVRTILL EVGRRGLVGG QEDLIVDIAL DLLAANSDSV AS

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000432 Genomic DNA. Translation: ABG99130.1.
RefSeq	YP_707288.1. NC_008269.1.
3D structure databases
ProteinModelPortal	Q0S006.
SMR	Q0S006. Positions 2-336.
ModBase	Search...
Protein-protein interaction databases
STRING	101510.RHA1_ro08083.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG99130; ABG99130; RHA1_ro08083.
GeneID	4225208.
KEGG	rha:RHA1_ro08083.
PATRIC	23213722. VBIRhoJos26306_7425.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0119.
HOGENOM	HOG000048047.
KO	K01666.
OMA	TTRLFIQ.
ProtClustDB	PRK08195.
Enzyme and pathway databases
BioCyc	RJOS101510:GJJ1-7362-MONOMER.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01656. HOA.
InterPro	IPR017629. 4OH_2_O-val_aldolase. IPR013785. Aldolase_TIM. IPR012425. DmpG_comm. IPR000891. PYR_CT. [Graphical view]
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

HOA5_RHOSR

Accession

Primary (citable) accession number: Q0S006

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 3, 2009
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program