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Reviewed, UniProtKB/Swiss-Prot P14697 (PHBB_RALEH)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetoacetyl-CoA reductase
    EC=1.1.1.36
Gene names
Name: phbB
Ordered Locus Names: H16_A1439
OrganismRalstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH.

Pathway

Biopolymer metabolism; poly-(R)-3-hydroxybutyric acid biosynthesis.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processPHB biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

poly-hydroxybutyrate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetoacetyl-CoA reductase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Acetoacetyl-CoA reductase
PRO_0000054748

Regions

Nucleotide binding8 – 3225NADP By similarity

Sites

Active site1531Proton acceptor By similarity
Binding site1401Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P14697-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: AD6739E0F5C93C06

FASTA24626,370
        10         20         30         40         50         60 
MTQRIAYVTG GMGGIGTAIC QRLAKDGFRV VAGCGPNSPR REKWLEQQKA LGFDFIASEG 

        70         80         90        100        110        120 
NVADWDSTKT AFDKVKSEVG EVDVLINNAG ITRDVVFRKM TRADWDAVID TNLTSLFNVT 

       130        140        150        160        170        180 
KQVIDGMADR GWGRIVNISS VNGQKGQFGQ TNYSTAKAGL HGFTMALAQE VATKGVTVNT 

       190        200        210        220        230        240 
VSPGYIATDM VKAIRQDVLD KIVATIPVKR LGLPEEIASI CAWLSSEESG FSTGADFSLN 


GGLHMG 

« Hide

References

« Hide 'large scale' references
[1]"Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase."
Peoples O.P., Sinskey A.J.
J. Biol. Chem. 264:15293-15297(1989) [PubMed: 2670935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

J04987 Genomic DNA. Translation: AAA21973.1.
AM260479 Genomic DNA. Translation: CAJ92574.1.
PIRRDALAE. B34340.
RefSeqYP_725942.1.

3D structure databases

HSSPHSSP built from PDB template 1GZ6 based on UniProtKB P97852.
ModBaseSearch...

Genome annotation databases

GeneID4249784.
GenomeReviewsGene locus H16_A1439 in contig AM260479_GR.
KEGGreh:H16_A1439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP14697.
OMAP14697. ICAWLSS.

Family and domain databases

InterProIPR011283. Acetoacetyl-CoA_reductase.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01829. AcAcCoA_reduct. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHBB_RALEH
AccessionPrimary (citable) accession number: P14697
Secondary accession number(s): Q0KBP7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents