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P50174 (THIL_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. 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:
Acetyl-CoA acetyltransferase

EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene names
Name:phbA
Ordered Locus Names:R03262
ORF Names:SMc03879
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processPHB biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   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 functionacetyl-CoA C-acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Acetyl-CoA acetyltransferase
PRO_0000206461

Sites

Active site901Acyl-thioester intermediate By similarity
Active site3491Proton acceptor By similarity
Active site3791Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
P50174 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B3162E72A9DB2A0D

FASTA39340,851
        10         20         30         40         50         60 
MSNPSIVIAS AARTAVGSFN GAFGNTLAHE LGAAAIKAVL ERAGVEAGEV DEVILGQVLP 

        70         80         90        100        110        120 
AGEGQNPARQ AAMKAGLPQE KTAWGMNQLC GSGLRAVALG MQQIATGDAK VIVAGGMESM 

       130        140        150        160        170        180 
SMAPHCAHLR GGVKMGDYKM IDTMIKDGLT DAFYGYHMGI TAENVARKWQ LTREEQDEFA 

       190        200        210        220        230        240 
LASQNKAEAA QKAGRFADEI VPFVVKTRKG DVNVDQDEYI RHGATLDSIA KLRPAFDKEG 

       250        260        270        280        290        300 
TVTAGNASGL NDGAAAALLM TEAEAARRGI QPLARIVSWA TAGVDPQIMG TGPIPASRKA 

       310        320        330        340        350        360 
LEKAGWSVAD IELVEANEAF AAQACAVNKD LGWDPSIVNV NGGAIAIGHP IGASGARVLN 

       370        380        390 
TLLFEMKRRG VSKGLATLCI GGGMGVAMCV ERL 

« 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: 7582015] [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: 11481430] [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: 11474104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17226 Genomic DNA. Translation: AAA90982.1.
AL591688 Genomic DNA. Translation: CAC47841.1.
RefSeqNP_387368.1. NC_003047.1.

3D structure databases

ProteinModelPortalP50174.
SMRP50174. Positions 5-393.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1234956.
GenomeReviewsGene locus R03262 in contig AL591688_GR.
KEGGsme:SMc03879.
NMPDRfig|266834.1.peg.4556.
PATRIC23636190. VBISinMel96828_4817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG370930.
OMADANTHDG.
ProtClustDBPRK05790.

Enzyme and pathway databases

BioCycSMEL266834:SMC03879-MONOMER.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KOK00626.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHIL_RHIME
AccessionPrimary (citable) accession number: P50174
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families