O05151 (BPHF_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	bphF
Synonyms:	etbF
Ordered Locus Names:	RHA1_ro10138

Encoded on

Plasmid pRHL2

Organism

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

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-oxovalerate to pyruvate and acetaldehyde Probable.
Catalytic activity	4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate.
Pathway	Xenobiotic degradation; biphenyl degradation.
Induction	By growth on ethylbenzene or biphenyl. Ref.1
Sequence similarities	Belongs to the HpcH/HpaI aldolase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Plasmid
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 258	258	4-hydroxy-2-oxovalerate aldolase		PRO_0000207097
Sites
	Active site	48	1	Proton acceptor By similarity
	Metal binding	151	1	Magnesium By similarity
	Metal binding	177	1	Magnesium By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	176	1	Substrate; via amide nitrogen By similarity
	Binding site	177	1	Substrate By similarity
	Site	74	1	Transition state stabilizer By similarity
	Site	88	1	Increases basicity of active site His By similarity

Sequences

	Sequence		Length	Mass (Da)
	O05151 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: A539C46C4DA0190F	FASTA	258	27,159
	10 20 30 40 50 60 MQSPINSFKK ALAEGRTQIG FWLALGDAYS AEVCAGAGFD WLLIDGEHAP QDLRSVLAQL 70 80 90 100 110 120 QVIGAYRDCH AAVRVPSADT TVIKQYLDLG AQSLLVPMVD TADEAAAVVR ACRYPPGGIR 130 140 150 160 170 180 GVGGARASRW GRYPRYLHEA DEQVCVVVQA ETALALSNLE AIAEVDGIDG VFIGTADLAA 190 200 210 220 230 240 SLGFPGNPAH PEVQDAILDA LQRVRAAGKA PGVLTPVEDL AQKYLAHGAV FVAVGIDTHL 250 LAKQTSALAA RFAQVAYS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA1." Masai E., Sugiyama K., Iwashita N., Shimizu S., Hauschild J.E., Hatta T., Kimbara K., Yano K., Fukuda M. Gene 187:141-149(1997) [PubMed: 9073078] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[2]	"Diversity and characterization of aromatic ring hydroxylation dioxygenase genes in Rhodococcus sp. strain RHA1." Iwasaki T., Miyauchi K., Masai E., Fukuda M. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78322 Genomic DNA. Translation: BAA18937.1. AB120955 Genomic DNA. Translation: BAC92717.1. CP000433 Genomic DNA. Translation: ABH00331.1.
PIR	JC6327.
RefSeq	YP_708489.1. NC_008270.1.
3D structure databases
ProteinModelPortal	O05151.
SMR	O05151. Positions 6-238.
ModBase	Search...
Protein-protein interaction databases
STRING	O05151.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4226121.
GenomeReviews	Gene locus RHA1_ro10138 in contig CP000433_GR.
KEGG	rha:RHA1_ro10138.
PATRIC	23215963. VBIRhoJos26306_8544.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3836.
HOGENOM	HBG747616.
OMA	DYLHRAN.
PhylomeDB	O05151.
ProtClustDB	CLSK956881.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO10138-MONOMER.
Family and domain databases
InterPro	IPR005000. Aldehyde-lyase_domain. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KO	K02510.
Pfam	PF03328. HpcH_HpaI. 1 hit. [Graphical view]
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BPHF_RHOSR

Accession

Primary (citable) accession number: O05151
Secondary accession number(s): Q75WN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program