Reviewed, UniProtKB/Swiss-Prot P12625 (PHB_BURPI)

Names and origin

Protein names	Recommended name:     Poly(3-hydroxybutyrate) depolymerase       Short name=PHB depolymerase     EC=3.1.1.75
Organism	Burkholderia pickettii (Ralstonia pickettii) (Pseudomonas pickettii)
Taxonomic identifier	329 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This protein degrades water-insoluble and water-soluble PHB to monomeric D--3-hydroxybutyrate.
Catalytic activity	((R)-3-hydroxybutanoate)(n) + H2O = ((R)-3-hydroxybutanoate)(n-1 to 5) + ((R)-3-hydroxybutanoate)1-5.
Subcellular location	Secreted.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 fibronectin type-III domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	poly(3-hydroxybutyrate) depolymerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27
	Chain	28 – 488	461	Poly(3-hydroxybutyrate) depolymerase		PRO_0000017727
Regions
	Domain	343 – 424	82	Fibronectin type-III
Sites
	Active site	166	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12625-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: FE6E2BCA97C135EF	FASTA	488	49,935
	10 20 30 40 50 60 MVRRLWRRIA GWLAACVAIL CAFPLHAATA GPGAWSSQQT WAADSVNGGN LTGYFYWPAS 70 80 90 100 110 120 QPTTPNGKRA LVLVLHGCVQ TASGDVIDNA NGAGFNWKSV ADQYGAVILA PNATGNVYSN 130 140 150 160 170 180 HCWDYANASP SRTAGHVGVL LDLVNRFVTN SQYAIDPNQV YVAGLSSGGG MTMVLGCIAP 190 200 210 220 230 240 DIFAGIGINA GPPPGTTTAQ IGYVPSGFTA TTAANKCNAW AGSNAGKFST QIAGAVWGTS 250 260 270 280 290 300 DYTVAQAYGP MDAAAMRLVY GGNFTQGSQV SISGGGTNTP YTDSNGKVRT HEISVSGMAH 310 320 330 340 350 360 AWPAGTGGDN TNYVDATHIN YPVFVMDYWV KNNLRAGSGT GQAGSAPTGL AVTATTSTSV 370 380 390 400 410 420 SLSWNAVANA SSYGVYRNGS KVGSATATAY TDSGLIAGTT YSYTVTAVDP TAGESQPSAA 430 440 450 460 470 480 VSATTKSAFT CTATTASNYA HVQAGRAHDS GGIAYANGSN QSMGLDNLFY TSTLAQTAAG YYIVGNCP

References

[1]	"Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis." Saito T., Suzuki K., Yamamoto J., Fukui T., Miwa K., Tomita K., Nakanishi S., Odani S., Suzuki J., Ishikawa K. J. Bacteriol. 171:184-189(1989) [PubMed: 2644188] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: T1.
[2]	"Proposed acquisition of an animal protein domain by bacteria." Bork P., Doolittle R.F. Proc. Natl. Acad. Sci. U.S.A. 89:8990-8994(1992) [PubMed: 1409594] [Abstract] Cited for: DOMAIN FIBRONECTIN TYPE-III.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04223 Genomic DNA. Translation: AAA21974.1.
PIR	A32235.
3D structure databases
HSSP	HSSP built from PDB template 1K85 based on UniProtKB P20533.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.75. 276669.
Family and domain databases
InterPro	IPR010126. Esterase_phb. IPR008957. Fibronectin_typ-III-like_fold. IPR003961. FN_III. [Graphical view]
Gene3D	G3DSA:2.60.40.30. FN_III-like. 1 hit.
Pfam	PF10503. Esterase_phd. 1 hit. PF00041. fn3. 1 hit. [Graphical view]
SMART	SM00060. FN3. 1 hit. [Graphical view]
TIGRFAMs	TIGR01840. esterase_phb. 1 hit.
PROSITE	PS50853. FN3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHB_BURPI

Accession

Primary (citable) accession number: P12625

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)