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UniProtKB/Swiss-Prot entry O08424


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HMDH_SULSO
Primary accession number O08424
Secondary accession number Q9UWT6
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on June 20, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Synonyms HMG-CoA reductase
EC 1.1.1.34
Gene name
Name: hmgA
OrderedLocusNames: SSO0531
ORFNames: C22_020
From
Sulfolobus solfataricus [TaxID: 2287] [HAMAP proteome]
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Sulfolobus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=9171410 [NCBI, ExPASy, EBI, Israel, Japan]
Bochar D.A., Brown J.R., Doolittle W.F., Klenk H.-P., Lam W., Schenk M.E., Stauffacher C.V., Rodwell V.W.;
"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.";
J. Bacteriol. 179:3632-3638(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
DOI=10.1139/gen-43-1-116; PubMed=10701121 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
Genome 43:116-136(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
DOI=10.1073/pnas.141222098; PubMed=11427726 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U95360; AAC45370.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y18930; CAB57768.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006683; AAK40851.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D90199; D90199.
T51306; T51306.
RefSeq NP_342061.1; -.
3D structure databases
HSSP P04035; 1HWI. [HSSP ENTRY / PDB]
ModBase O08424.
Enzyme and pathway databases
BioCyc SSOL273057:SSO0531-MON; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0004420; Molecular function: hydroxymethylglutaryl-CoA reductase (NADPH) activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0015936; Biological process: coenzyme A metabolic process (inferred from electronic annotation from InterPro).
GO:0008299; Biological process: isoprenoid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.90.770.10; HMG-CoA_red; 1.
PANTHER PTHR10572; HMG-CoA_red; 1.
Pfam PF00368; HMG-CoA_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00071; HMGCOARDTASE.
TIGRFAMs TIGR00533; HMG_CoA_R_NADP; 1.
PROSITE PS00066; HMG_COA_REDUCTASE_1; 1.
PS00318; HMG_COA_REDUCTASE_2; 1.
PS01192; HMG_COA_REDUCTASE_3; FALSE_NEG.
PS50065; HMG_COA_REDUCTASE_4; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1454818; -.
GenomeReviews AE006641_GR; SSO0531.
KEGG sso:SSO0531; -.
NMPDR fig|273057.1.peg.484; -.
Phylogenomic databases
HOGENOM O08424; -.
Genome annotation databases
CMR O08424; SSO0531.
Other
ProtoNet O08424.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Isoprene biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   409  409     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114465
ACT_SITE   99    99        Charge relay system (By similarity). 
ACT_SITE   305   305        Charge relay system (By similarity). 
ACT_SITE   400   400        Proton donor (By similarity). 
CONFLICT   245   245        V -> L (in Ref. 1; AAC45370). 
Sequence information
Length: 409 AA [This is the length of the unprocessed precursor] Molecular weight: 44009 Da [This is the MW of the unprocessed precursor] CRC64: 8D1FA64E117CFF46 [This is a checksum on the sequence]
        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 

O08424 in FASTA format

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