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Protein

D-(-)-3-hydroxybutyrate oligomer hydrolase

Gene

Bpro_4732

Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D--3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.UniRule annotation

Catalytic activityi

(R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O = 2 (R)-3-hydroxybutanoate.UniRule annotation

Pathwayi: butanoate metabolism

This protein is involved in the pathway butanoate metabolism, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway butanoate metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei311 – 3111Charge relay systemUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciPSP296591:GHI4-5450-MONOMER.
UniPathwayiUPA00863.

Names & Taxonomyi

Protein namesi
Recommended name:
D-(-)-3-hydroxybutyrate oligomer hydrolaseUniRule annotation (EC:3.1.1.22UniRule annotation)
Short name:
3HB-oligomer hydrolaseUniRule annotation
Short name:
3HBOHUniRule annotation
Gene namesi
Ordered Locus Names:Bpro_4732
OrganismiPolaromonas sp. (strain JS666 / ATCC BAA-500)
Taxonomic identifieri296591 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas
Proteomesi
  • UP000001983 Componenti: Chromosome

Subcellular locationi

  • Secreted UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232UniRule annotationAdd
BLAST
Chaini33 – 706674D-(-)-3-hydroxybutyrate oligomer hydrolasePRO_5000117312Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi296591.Bpro_4732.

Family & Domainsi

Sequence similaritiesi

Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106BE1. Bacteria.
ENOG410XSMB. LUCA.
HOGENOMiHOG000263490.
KOiK07518.
OMAiNPEKDWG.
OrthoDBiEOG6F293S.

Family and domain databases

HAMAPiMF_01906. 3HBOH.
InterProiIPR016582. OHBut_olig_hydro_put.
[Graphical view]
PfamiPF10605. 3HBOH. 1 hit.
[Graphical view]
PIRSFiPIRSF011409. HObutyrate_olig_hydrol. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q122D1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTSKNCLT LTSIAAAVAA VLVLSACGGG SAGENINRKP TYLGTVVSVN
60 70 80 90 100
YDGASDDLLT AGLGKTGLGA TAPVAADPLN PTAAELRRIA IFNNYRALLD
110 120 130 140 150
ISVAGGYGSL YGPNVDASGV ITTSEGKIAG TEYMAYSDDG TGNQNITMLV
160 170 180 190 200
QVPTTFNPAS PCIVTGTSSG SRGVYGAIGT SGEWGLKNGC AVAYTDKGTG
210 220 230 240 250
TGIHDLQNDT VNLQRGERAT ATAAGKASNF TASLTSTERA AFNTATPNRF
260 270 280 290 300
AVKHAHSQQN TEKDWGKWTL QAVEFAYFVL NENYGDAAKD GVSRLVKLKP
310 320 330 340 350
ANTIVIASSA SNGAGAALAA AELDTKGLIT GVAVAEPQIQ VVPDTRLSVR
360 370 380 390 400
RGASTLGGTG RSLFDYASLG NLLQPCAALA SPTTNVFNTV NTTIATNRCN
410 420 430 440 450
ALQASGLIVG NTTAELAADA MARLLAAGHQ PESSVLQASH YSFATPAVAV
460 470 480 490 500
TFANSYGRFS VKDNLCGFSF AATGAAGSAT PNAPVAASAA ALATSFGASN
510 520 530 540 550
GIPPTVGINI VNNNSVGGPL LDAASLSAGS VLDYNIAGAL CLRELLGGSS
560 570 580 590 600
ANALKVQQGI NEVLRTGDLQ GKPALIVHGR ADAQVPVAFS SRPYFGRNKI
610 620 630 640 650
VEGANSRLSY IEVTNAQHFD AFLAFPGYGE RFVPAHRYFI QAMDMMYANL
660 670 680 690 700
KTGAALPASQ VVRTVPRGLT GAVVNPITPA NVPPIKTVPA VADQITFANN

VVTVAD
Length:706
Mass (Da):72,212
Last modified:August 22, 2006 - v1
Checksum:i92792A8B4905943B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000316 Genomic DNA. Translation: ABE46611.1.
RefSeqiWP_011485596.1. NC_007948.1.

Genome annotation databases

EnsemblBacteriaiABE46611; ABE46611; Bpro_4732.
KEGGipol:Bpro_4732.
PATRICi22962784. VBIPolSp102244_4837.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000316 Genomic DNA. Translation: ABE46611.1.
RefSeqiWP_011485596.1. NC_007948.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi296591.Bpro_4732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE46611; ABE46611; Bpro_4732.
KEGGipol:Bpro_4732.
PATRICi22962784. VBIPolSp102244_4837.

Phylogenomic databases

eggNOGiENOG4106BE1. Bacteria.
ENOG410XSMB. LUCA.
HOGENOMiHOG000263490.
KOiK07518.
OMAiNPEKDWG.
OrthoDBiEOG6F293S.

Enzyme and pathway databases

UniPathwayiUPA00863.
BioCyciPSP296591:GHI4-5450-MONOMER.

Family and domain databases

HAMAPiMF_01906. 3HBOH.
InterProiIPR016582. OHBut_olig_hydro_put.
[Graphical view]
PfamiPF10605. 3HBOH. 1 hit.
[Graphical view]
PIRSFiPIRSF011409. HObutyrate_olig_hydrol. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JS666 / ATCC BAA-500.

Entry informationi

Entry nameiHBOH_POLSJ
AccessioniPrimary (citable) accession number: Q122D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: July 6, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.