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P50205 (PHBB_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetoacetyl-CoA reductase

EC=1.1.1.36
Gene names
Name:phbB
Ordered Locus Names:R03261
ORF Names:SMc03878
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

Biopolymer metabolism; poly-(R)-3-hydroxybutanoate 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_processpoly-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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Acetoacetyl-CoA reductase
PRO_0000054750

Regions

Nucleotide binding12 – 143NADP By similarity
Nucleotide binding82 – 865NADP By similarity
Nucleotide binding177 – 1804NADP By similarity
Region141 – 1444Substrate binding By similarity
Region178 – 1792Substrate binding By similarity

Sites

Active site1471Proton acceptor By similarity
Binding site391NADP By similarity
Binding site881Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P50205 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 025C43AF1900B1F0

FASTA24125,370
        10         20         30         40         50         60 
MSRVALVTGG SRGIGAAICV ALKAAGYKVA ANYAGNDERA KAFEQESGIP VYKWDVSSYQ 

        70         80         90        100        110        120 
ACVDGIARVE ADLGPVDILV NNAGITRDAM FHKMTPEQWG EVIGTNLTGV FNMTHPLWSG 

       130        140        150        160        170        180 
MRDRGFGRIV NISSINGQKG QMGQVNYSAA KAGDLGLTKA LAQEGAAKGI TVNAICPGYI 

       190        200        210        220        230        240 
GTEMVRAVPE KVLNERIIPQ IPVGRLGEPE EVARCVVFLA SDDAGFITGS TISANGGQYF 


A 

« Hide

References

« Hide 'large scale' references
[1]"Poly-beta-hydroxybutyrate (PHB) biosynthetic genes in Rhizobium meliloti 41."
Tombolini R., Povolo S., Buson A., Squartini A., Nuti M.P.
Microbiology 141:2553-2559(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 41.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17226 Genomic DNA. Translation: AAA90983.1.
AL591688 Genomic DNA. Translation: CAC47840.1.
RefSeqNP_387367.1. NC_003047.1.

3D structure databases

ProteinModelPortalP50205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc03878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC47840; CAC47840; SMc03878.
GeneID1234955.
KEGGsme:SMc03878.
PATRIC23636186. VBISinMel96828_4815.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1028.
KOK00023.
OMAGINEHET.
OrthoDBEOG6N3CR8.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-3352-MONOMER.
UniPathwayUPA00917.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR011283. Acetoacetyl-CoA_reductase.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
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_RHIME
AccessionPrimary (citable) accession number: P50205
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways