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P23228 (HMCS1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. 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:
Hydroxymethylglutaryl-CoA synthase, cytoplasmic

Short name=HMG-CoA synthase
EC=2.3.3.10
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene names
Name:HMGCS1
Synonyms:HMGCS
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length522 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.

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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the HMG-CoA synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Hydroxymethylglutaryl-CoA synthase, cytoplasmic
PRO_0000213751

Sites

Active site951Proton donor/acceptor By similarity
Active site1291Acyl-thioester intermediate By similarity
Active site2641Proton donor/acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
P23228 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: BFF7947C3E963C4C

FASTA52257,559
        10         20         30         40         50         60 
MPGSLPVNTE SCWPKDVGIV ALEIYFPSQY VDQTELEKYD GVDAGKYTIG LGQSKMGFCS 

        70         80         90        100        110        120 
DREDINSLCL TVVQKLMERN SLSYDCIGRL EVGTETIIDK SKSVKTVLMQ LFEESGNTDV 

       130        140        150        160        170        180 
EGIDTTNACY GGTAALFNAI NWIESSSWDG RYALVVAGDI AVYATGNARP TGGAGAVAML 

       190        200        210        220        230        240 
VGSNAPLIFE RGLRGTHMQH AYDFYKPDMV SEYPVVDGKL SIQCYLSALD RCYSVYRNKI 

       250        260        270        280        290        300 
HAQWQKEGTD RGFTLNDFGF MIFHSPYCKL VQKSVARLLL NDFLSDQNAE TANGVFSGLE 

       310        320        330        340        350        360 
AFRDVKLEDT YFDRDVEKAF MKASAELFNQ KTKASLLVSN QNGNMYTPSV YGCLASLLAQ 

       370        380        390        400        410        420 
YSPEHLAGQR ISEFSYGSGF AATLYSIRVT QDATPGSALD KITASLSDLK ARLDSRKCIA 

       430        440        450        460        470        480 
PDVFAENMKI RQETHHLANY IPQCSVEDLF EGTWYLVRVD EKHRRTYARR PVMGDGPLEA 

       490        500        510        520 
GVEVVHPGIV HEHIPSPAKK VPRIPATTES EGVTVAISNG VH 

« Hide

References

[1]"Avian liver 3-hydroxy-3-methylglutaryl-CoA synthase: distinct genes encode the cholesterogenic and ketogenic isozymes."
Kattar-Cooley P.A., Wang H.-H.L., Mende-Mueller L.M., Miziorko H.M.
Arch. Biochem. Biophys. 283:523-529(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Avian cytosolic 3-hydroxy-3-methylglutaryl-CoA synthase: evaluation of the role of cysteines in reaction chemistry."
Misra I., Charlier H.A. Jr., Miziorko H.M.
Biochim. Biophys. Acta 1247:253-259(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60657 mRNA. Translation: AAA62737.1.
PIRS13887.
RefSeqNP_990742.1. NM_205411.1.
UniGeneGga.4388.

3D structure databases

ProteinModelPortalP23228.
SMRP23228. Positions 16-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000038170.

Proteomic databases

PaxDbP23228.
PRIDEP23228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396379.
KEGGgga:396379.

Organism-specific databases

CTD3157.

Phylogenomic databases

eggNOGCOG3425.
HOGENOMHOG000012351.
HOVERGENHBG051912.
InParanoidP23228.
KOK01641.
PhylomeDBP23228.

Enzyme and pathway databases

BRENDA2.3.3.10. 1306.
SABIO-RKP23228.
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. SSF53901. 3 hits.
TIGRFAMsTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816421.
PROP23228.

Entry information

Entry nameHMCS1_CHICK
AccessionPrimary (citable) accession number: P23228
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 11, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways