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Reviewed, UniProtKB/Swiss-Prot O08424 (HMDH_SULSO)

Last modified November 3, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-hydroxy-3-methylglutaryl-coenzyme A reductase
      Short name=HMG-CoA reductase
    EC=1.1.1.34
Gene names
Name: hmgA
Ordered Locus Names: SSO0531
ORF Names: C22_020
OrganismSulfolobus solfataricus [Complete proteome] [HAMAP]
Taxonomic identifier2287 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Converts HMG-CoA to mevalonate.

Catalytic activity

(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH.

Pathway

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

Sequence similarities

Belongs to the HMG-CoA reductase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5.

Temperature dependence:

Optimum temperature is 85 degrees Celsius. Stable at 90 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4094093-hydroxy-3-methylglutaryl-coenzyme A reductase
PRO_0000114465

Sites

Active site991Charge relay system By similarity
Active site3051Charge relay system By similarity
Active site4001Proton donor By similarity

Experimental info

Sequence conflict2451V → L in AAC45370. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08424-1 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: 8D1FA64E117CFF46

FASTA40944,009
        10         20         30         40         50         60 
MKIDEVVEKL VKGEISFHEV DNLLEANAAM VARRLALEKI VGVGLPSIGS TVIDYSEIKN 

        70         80         90        100        110        120 
KNAENVIGAI QIPLGIVGPI RVNGDYAKGD FYVPMATTEG ALIASVNRGI KAVTLSGGVR 

       130        140        150        160        170        180 
AKVLKDEMTR APVFKFDSIE QIPNFLKFIE ENLEKIRNIA NSTSHHGKLK SITPFVLGNN 

       190        200        210        220        230        240 
VWLRFSFETG DAMGMNMVTI AVEKVCEFIE ENFPSADCLA VSGNMCSDKK QTNVNSLFGR 

       250        260        270        280        290        300 
GKTVVAEALI KKDVIRNILH SNAQLIHDIN LRKNWLGTAR AGSLSQFNAH FANIVTAIFI 

       310        320        330        340        350        360 
ATGQDVAQIV ESSSGYTWTE VRGEDLYISV TLPSLEVGTV GGGTRLPTQK EALSIMGVYG 

       370        380        390        400 
SGNPPGSNAK KLAEIIASTV LSGELNLLAA LSNKELGKAH AKLGRAMKV 

« Hide

References

« Hide 'large scale' references
[1]"3-hydroxy-3-methylglutaryl coenzyme A reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic characterization of the gene product."
Bochar D.A., Brown J.R., Doolittle W.F., Klenk H.-P., Lam W., Schenk M.E., Stauffacher C.V., Rodwell V.W.
J. Bacteriol. 179:3632-3638(1997) [PubMed: 9171410] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2."
Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C., Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E., Medina N. expand/collapse author list , Peng X., Penny S.L., She Q., St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.
Genome 43:116-136(2000) [PubMed: 10701121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Cross-references

Sequence databases

U95360 Genomic DNA. Translation: AAC45370.1.
Y18930 Genomic DNA. Translation: CAB57768.1.
AE006641 Genomic DNA. Translation: AAK40851.1.
PIRD90199.
T51306.
RefSeqNP_342061.1.

3D structure databases

HSSPHSSP built from PDB template 1HWI based on UniProtKB P04035.
ModBaseSearch...

Genome annotation databases

GeneID1454818.
GenomeReviewsGene locus SSO0531 in contig AE006641_GR.
KEGGsso:SSO0531.
NMPDRfig|273057.1.peg.484.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO08424.
OMAAHFANII.

Enzyme and pathway databases

BioCycSSOL273057:SSO0531-MON.
BRENDA1.1.1.34. 2070.

Family and domain databases

InterProIPR002202. HMG_CoA_Rdtase_cat.
IPR004554. HMG_CoA_Rdtase_I_cat.
[Graphical view]
Gene3DG3DSA:3.90.770.10. HMG-CoA_red. 1 hit.
PANTHERPTHR10572. HMG-CoA_red. 1 hit.
PfamPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
PRINTSPR00071. HMGCOARDTASE.
TIGRFAMsTIGR00533. HMG_CoA_R_NADP. 1 hit.
PROSITEPS00066. HMG_COA_REDUCTASE_1. 1 hit.
PS00318. HMG_COA_REDUCTASE_2. 1 hit.
PS01192. HMG_COA_REDUCTASE_3. False negative.
PS50065. HMG_COA_REDUCTASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMDH_SULSO
AccessionPrimary (citable) accession number: O08424
Secondary accession number(s): Q9UWT6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2001
Last modified: November 3, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents