Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2KIE6 (HMCS2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. 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, mitochondrial

Short name=HMG-CoA synthase
EC=2.3.3.10
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene names
Name:HMGCS2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the HMG-CoA synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Probable
Chain38 – 508471Hydroxymethylglutaryl-CoA synthase, mitochondrial
PRO_0000236276

Sites

Active site1321Proton donor/acceptor By similarity
Active site1661Acyl-thioester intermediate By similarity
Active site3011Proton donor/acceptor By similarity
Binding site801Substrate By similarity
Binding site2041Substrate By similarity
Binding site2581Substrate By similarity
Binding site3801Substrate By similarity

Amino acid modifications

Modified residue521N6-succinyllysine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine; alternate By similarity
Modified residue2561N6-succinyllysine; alternate By similarity
Modified residue3061N6-acetyllysine By similarity
Modified residue3101N6-acetyllysine; alternate By similarity
Modified residue3101N6-succinyllysine; alternate Ref.2
Modified residue3331N6-succinyllysine By similarity
Modified residue3421N6-acetyllysine; alternate By similarity
Modified residue3421N6-succinyllysine; alternate By similarity
Modified residue3501N6-acetyllysine; alternate By similarity
Modified residue3501N6-succinyllysine; alternate By similarity
Modified residue3541N6-acetyllysine; alternate By similarity
Modified residue3541N6-succinyllysine; alternate By similarity
Modified residue3581N6-acetyllysine; alternate By similarity
Modified residue3581N6-succinyllysine; alternate By similarity
Modified residue4371N6-acetyllysine By similarity
Modified residue4471N6-acetyllysine; alternate By similarity
Modified residue4471N6-succinyllysine; alternate By similarity
Modified residue4731N6-acetyllysine; alternate By similarity
Modified residue4731N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KIE6 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 12F31AAFBAE986BF

FASTA50856,895
        10         20         30         40         50         60 
MQRLLTPVRQ VLQVKRVMQE ASLLPARLLP AAHPSFSTVP AVPLAKTDTW PKDVGILAME 

        70         80         90        100        110        120 
VYFPAQYVDQ TELEKFNKVE AGRYTVGLGQ TQMGFCSVQE DVNSLCLTVV QQLMERTQLP 

       130        140        150        160        170        180 
WDSVGRLEVG TETIIDKSKA VKTVLMELFQ DSGNTDIEGI DTTNACYGGT ASLFNAANWM 

       190        200        210        220        230        240 
ESSSWDGRYA LVVCGDIAVY PSGNARPTGG AGAVAMLVGP EAPLVLERGL RGTHMENVYD 

       250        260        270        280        290        300 
FYKPDVTSEY PLVDGKLSIQ CYLRALDKCY AFYRQKIEKQ WKQAGIDRPF TLDDVQYMIF 

       310        320        330        340        350        360 
HTPFCKLVQK SLARLMFNDF LLASGDTQTG IYKGLEAFRG LKLEDTYTNK DVDKAFLKAS 

       370        380        390        400        410        420 
LNMFNKKTKN SLYLSTYNGN MYTSSLYGCL ASLLAHHSAQ DLAGSRIGAF SYGSGLAASF 

       430        440        450        460        470        480 
FSFRVSQDAS PGSPLEKLVS STSDLQKRLA SRKRVSPEEF TEIMNQREQY YHKMNFSPPG 

       490        500 
DKNSLFPGTW YLERVDELYR RKYARRPV 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Testis.
[2]"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-310.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC112666 mRNA. Translation: AAI12667.1.
RefSeqNP_001039348.1. NM_001045883.1.
UniGeneBt.9689.

3D structure databases

ProteinModelPortalQ2KIE6.
SMRQ2KIE6. Positions 53-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000005088.

Proteomic databases

PaxDbQ2KIE6.
PRIDEQ2KIE6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000005088; ENSBTAP00000005088; ENSBTAG00000003898.
GeneID503684.
KEGGbta:503684.

Organism-specific databases

CTD3158.

Phylogenomic databases

eggNOGCOG3425.
GeneTreeENSGT00390000006096.
HOGENOMHOG000012351.
HOVERGENHBG051912.
InParanoidQ2KIE6.
KOK01641.
OMAMLVGPEA.
OrthoDBEOG741Z1W.
TreeFamTF105361.

Enzyme and pathway databases

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

NextBio20866256.

Entry information

Entry nameHMCS2_BOVIN
AccessionPrimary (citable) accession number: Q2KIE6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 7, 2006
Last modified: June 11, 2014
This is version 64 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