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P54874

- HMCS_SCHPO

UniProt

P54874 - HMCS_SCHPO

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Protein

Hydroxymethylglutaryl-CoA synthase

Gene

hcs1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Proton donor/acceptorPROSITE-ProRule annotation
Active sitei118 – 1181Acyl-thioester intermediatePROSITE-ProRule annotation
Active sitei250 – 2501Proton donor/acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. hydroxymethylglutaryl-CoA synthase activity Source: PomBase

GO - Biological processi

  1. acetyl-CoA metabolic process Source: PomBase
  2. cellular response to nitrogen starvation Source: PomBase
  3. ergosterol biosynthetic process Source: PomBase
  4. farnesyl diphosphate biosynthetic process, mevalonate pathway Source: PomBase
  5. negative regulation of G0 to G1 transition Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

BRENDAi2.3.3.10. 5615.
ReactomeiREACT_188314. PPARA activates gene expression.
REACT_188316. Activation of gene expression by SREBF (SREBP).
REACT_223245. Synthesis of Ketone Bodies.
REACT_258783. Cholesterol biosynthesis.
UniPathwayiUPA00058; UER00102.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylglutaryl-CoA synthase (EC:2.3.3.10)
Short name:
HMG-CoA synthase
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene namesi
Name:hcs1
Synonyms:hcs
ORF Names:SPAC4F8.14c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC4F8.14c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. endoplasmic reticulum Source: PomBase
  3. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Hydroxymethylglutaryl-CoA synthasePRO_0000213757Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP54874.
PaxDbiP54874.

Interactioni

Protein-protein interaction databases

BioGridi279573. 1 interaction.
MINTiMINT-4690976.
STRINGi4896.SPAC4F8.14c-1.

Structurei

3D structure databases

ProteinModelPortaliP54874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA synthase family.Curated

Phylogenomic databases

eggNOGiCOG3425.
HOGENOMiHOG000012351.
KOiK01641.
OMAiPHVFQID.
PhylomeDBiP54874.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEiPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54874-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFDRKDIGI KGLVLYTPNQ YVEQAALEAH DGVSTGKYTI GLGLTKMAFV
60 70 80 90 100
DDREDIYSFG LTALSQLIKR YQIDISKIGR LEVGTETIID KSKSVKSVLM
110 120 130 140 150
QLFGDNHNVE GIDCVNACYG GVNALFNTID WIESSAWDGR DGIVVAGDIA
160 170 180 190 200
LYAKGNARPT GGAGCVALLV GPNAPIVFEP GLRGTYMQHA YDFYKPDLTS
210 220 230 240 250
EYPYVDGHFS LECYVKALDG AYANYNVRDV AKNGKSQGLG LDRFDYCIFH
260 270 280 290 300
APTCKQVQKA YARLLYTDSA AEPSNPELEG VRELLSTLDA KKSLTDKALE
310 320 330 340 350
KGLMAITKER FNKRVSPSVY APTNCGNMYT ASIFSCLTAL LSRVPADELK
360 370 380 390 400
GKRVGAYSYG SGLAASFFSF VVKGDVSEIA KKTNLVNDLD NRHCLTPTQY
410 420 430 440
EEAIELRHQA HLKKNFTPKG SIERLRSGTY YLTGIDDMFR RSYSVKP
Length:447
Mass (Da):49,239
Last modified:October 1, 1996 - v1
Checksum:i919BDDBD9207B886
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32187 Genomic DNA. Translation: AAB17601.1.
CU329670 Genomic DNA. Translation: CAB11060.1.
PIRiS61875.
RefSeqiNP_593859.1. NM_001019288.2.

Genome annotation databases

EnsemblFungiiSPAC4F8.14c.1; SPAC4F8.14c.1:pep; SPAC4F8.14c.
GeneIDi2543141.
KEGGispo:SPAC4F8.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32187 Genomic DNA. Translation: AAB17601.1 .
CU329670 Genomic DNA. Translation: CAB11060.1 .
PIRi S61875.
RefSeqi NP_593859.1. NM_001019288.2.

3D structure databases

ProteinModelPortali P54874.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 279573. 1 interaction.
MINTi MINT-4690976.
STRINGi 4896.SPAC4F8.14c-1.

Proteomic databases

MaxQBi P54874.
PaxDbi P54874.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC4F8.14c.1 ; SPAC4F8.14c.1:pep ; SPAC4F8.14c .
GeneIDi 2543141.
KEGGi spo:SPAC4F8.14c.

Organism-specific databases

PomBasei SPAC4F8.14c.

Phylogenomic databases

eggNOGi COG3425.
HOGENOMi HOG000012351.
KOi K01641.
OMAi PHVFQID.
PhylomeDBi P54874.

Enzyme and pathway databases

UniPathwayi UPA00058 ; UER00102 .
BRENDAi 2.3.3.10. 5615.
Reactomei REACT_188314. PPARA activates gene expression.
REACT_188316. Activation of gene expression by SREBF (SREBP).
REACT_223245. Synthesis of Ketone Bodies.
REACT_258783. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi 20804168.

Family and domain databases

Gene3Di 3.40.47.10. 1 hit.
InterProi IPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 3 hits.
TIGRFAMsi TIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEi PS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-398, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiHMCS_SCHPO
AccessioniPrimary (citable) accession number: P54874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3