Q52011 (BPHD_PSEPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase
Short name=HOPDA hydrolase
EC=3.7.1.8

Alternative name(s):
2,6-dioxo-6-phenylhexa-3-enoate hydrolase

Gene names

Name:

bphD

Organism

Pseudomonas pseudoalcaligenes

Taxonomic identifier

330 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas oleovorans/pseudoalcaligenes group

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD). Ref.1
Catalytic activity	2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate. HAMAP-Rule MF_01688
Pathway	Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 4/4. HAMAP-Rule MF_01688
Subunit structure	Homodimer By similarity.
Induction	By biphenyl. Ref.1
Sequence similarities	Belongs to the AB hydrolase superfamily. BphD family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Molecular function	Hydrolase
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	2,6-dioxo-6-phenylhexa-3-enoate 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 – 286	286	2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase HAMAP-Rule MF_01688		PRO_0000373814
Regions
	Region	42 – 43	2	Substrate binding By similarity
Sites
	Active site	265	1	Proton acceptor By similarity
	Binding site	51	1	Substrate By similarity
	Binding site	111	1	Substrate By similarity
	Binding site	180	1	Substrate; via carbonyl oxygen By similarity
	Binding site	190	1	Substrate By similarity
	Binding site	266	1	Substrate By similarity
	Site	112	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q52011 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B204AADDC7AD31AA	FASTA	286	31,946
	10 20 30 40 50 60 MTALTESSTS KFVKINEKGF SDFNIHYNEA GNGETVIMLH GGGPGAGGWS NYYRNVGPFV 70 80 90 100 110 120 DAGYRVILKD SPGFNKSDAV VMDEQRGLVN ARAVKGLMDA LGIDRAHLVG NSMGGATALN 130 140 150 160 170 180 FAIEYPERIG KLILMGPGGP GPSMFAPMPM EGIKLLFKLY AEPSYENLKQ MIQVFLYDQS 190 200 210 220 230 240 LITEELLQGR WEAIQRQPEH LKNFLISAQK APLSTWDVTA RLGEIKAKTF ITWGRDDRFV 250 260 270 280 PLDHGLKLLW NIDDARLHVF SKCGHWAQWE HADEFNRLAI DFLRQA

References

[1]	"Versatile transcription of biphenyl catabolic bph operon in Pseudomonas pseudoalcaligenes KF707." Watanabe T., Inoue R., Kimura N., Furukawa K. J. Biol. Chem. 275:31016-31023(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION. Strain: KF707.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85851 Genomic DNA. Translation: BAA12881.1.
3D structure databases
HSSP	HSSP built from PDB template 1U2E based on UniProtKB P77044.
ProteinModelPortal	Q52011.
SMR	Q52011. Positions 2-286.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00155; UER00253.
Family and domain databases
HAMAP	MF_01688. Biphenyl_BphD.
InterPro	IPR000073. AB_hydrolase_1. IPR000639. Epox_hydrolase-like. IPR017727. HOPD_hydrolase_BphD. [Graphical view]
PRINTS	PR00111. ABHYDROLASE. PR00412. EPOXHYDRLASE.
TIGRFAMs	TIGR03343. biphenyl_bphD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BPHD_PSEPS

Accession

Primary (citable) accession number: Q52011

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program