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Reviewed, UniProtKB/Swiss-Prot P50203 (PHAB_ACISR)

Last modified November 25, 2008. Version 45. 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: phaB
OrganismAcinetobacter sp. (strain RA3849)
Taxonomic identifier68994 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length248 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

   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

poly-hydroxybutyrate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionacetoacetyl-CoA reductase activity

Inferred from electronic annotation. Source: InterPro

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Acetoacetyl-CoA reductase
PRO_0000054746

Regions

Nucleotide binding9 – 3325NADP By similarity

Sites

Active site1551Proton acceptor By similarity
Binding site1421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P50203-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 850E0DC659795123

FASTA24826,727
        10         20         30         40         50         60 
MSEQKVALVT GALGGIGSEI CRQLVTAGYK IIATVVPREE DREKQWLQSE GFQDSDVRFV 

        70         80         90        100        110        120 
LTDLNNHEAA TAAIQEAIAA EGRVDVLVNN AGITRDATFK KMSYEQWSQV IDTNLKTLFT 

       130        140        150        160        170        180 
VTQPVFNKML EQKSGRIVNI SSVNGLKGQF GQANYSASKA GIIGFTKALA QEGARSNICV 

       190        200        210        220        230        240 
NVVAPGYTAT PMVTAMREDV IKSIEAQIPL QRLAAPAEIA AAVMYLVSEH GAYVTGETLS 


INGGLYMH 

« Hide

References

[1]"Phosphate concentration regulates transcription of the Acinetobacter polyhydroxyalkanoic acid biosynthetic genes."
Schembri M.A., Bayly R.C., Davies J.K.
J. Bacteriol. 177:4501-4507(1995) [PubMed: 7635832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

L37761 Genomic DNA. Translation: AAA99472.1.

3D structure databases

HSSPHSSP built from PDB template 1E7W based on UniProtKB Q01782.
ModBaseSearch...

Family and domain databases

InterProIPR011283. Acetoacetyl-CoA_reductase.
IPR002198. DHase_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DHase.
IPR016040. NAD(P)-bd.
[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 namePHAB_ACISR
AccessionPrimary (citable) accession number: P50203
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 25, 2008
This is version 45 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