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P54874 (HMCS_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxymethylglutaryl-CoA synthase
Short name=HMG-CoA synthase
EC=2.3.3.10
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene names
Name:hcs1
Synonyms:hcs
ORF Names:SPAC4F8.14c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase By similarity.

Catalytic activity

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.

Sequence similarities

Belongs to the HMG-CoA synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Hydroxymethylglutaryl-CoA synthase
PRO_0000213757

Sites

Active site1181 Potential

Amino acid modifications

Modified residue3981Phosphothreonine Ref.3

Sequences

Sequence LengthMass (Da)Tools
P54874 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 919BDDBD9207B886

FASTA44749,239
        10         20         30         40         50         60 
MSFDRKDIGI KGLVLYTPNQ YVEQAALEAH DGVSTGKYTI GLGLTKMAFV DDREDIYSFG 

        70         80         90        100        110        120 
LTALSQLIKR YQIDISKIGR LEVGTETIID KSKSVKSVLM QLFGDNHNVE GIDCVNACYG 

       130        140        150        160        170        180 
GVNALFNTID WIESSAWDGR DGIVVAGDIA LYAKGNARPT GGAGCVALLV GPNAPIVFEP 

       190        200        210        220        230        240 
GLRGTYMQHA YDFYKPDLTS EYPYVDGHFS LECYVKALDG AYANYNVRDV AKNGKSQGLG 

       250        260        270        280        290        300 
LDRFDYCIFH APTCKQVQKA YARLLYTDSA AEPSNPELEG VRELLSTLDA KKSLTDKALE 

       310        320        330        340        350        360 
KGLMAITKER FNKRVSPSVY APTNCGNMYT ASIFSCLTAL LSRVPADELK GKRVGAYSYG 

       370        380        390        400        410        420 
SGLAASFFSF VVKGDVSEIA KKTNLVNDLD NRHCLTPTQY EEAIELRHQA HLKKNFTPKG 

       430        440 
SIERLRSGTY YLTGIDDMFR RSYSVKP

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of the hcs gene, which encodes 3-hydroxy-3-methylglutaryl coenzyme A synthase of Schizosaccharomyces pombe."
Katayama S., Adachi N., Takao K., Nakagawa T., Matsuda H., Kawamukai M.
Yeast 11:1533-1537(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-398, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U32187 Genomic DNA. Translation: AAB17601.1.
CU329670 Genomic DNA. Translation: CAB11060.1.
PIRS61875.
RefSeqNP_593859.1. NM_001019288.2.

3D structure databases

ProteinModelPortalP54874.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC4F8.14c-1.

Proteomic databases

PaxDbP54874.
PRIDEP54874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC4F8.14c.1; SPAC4F8.14c.1:pep; SPAC4F8.14c.
GeneID2543141.
KEGGspo:SPAC4F8.14c.

Organism-specific databases

PomBaseSPAC4F8.14c.

Phylogenomic databases

eggNOGCOG3425.
HOGENOMHOG000012351.
KOK01641.
OMADSVTMAS.
OrthoDBEOG4G7G73.

Enzyme and pathway databases

BRENDA2.3.3.10. 5615.
UniPathwayUPA00058; UER00102.

Family and domain databases

Gene3D3.40.47.10. 1 hit.
InterProIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804168.

Entry information

Entry nameHMCS_SCHPO
AccessionPrimary (citable) accession number: P54874
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents