ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9YAS4


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HMDH_AERPE
Primary accession number Q9YAS4
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
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: APE_1869
From
Aeropyrum pernix [TaxID: 56636] [HAMAP proteome]
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Desulfurococcaceae; Aeropyrum.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K1;
DOI=10.1093/dnares/6.2.83; PubMed=10382966 [NCBI, ExPASy, EBI, Israel, Japan]
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.";
DNA Res. 6:83-101(1999).
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
BA000002; BAA80874.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E72573; E72573.
RefSeq NP_148225.1; -.
3D structure databases
HSSP P04035; 1HWI. [HSSP ENTRY / PDB]
ModBase Q9YAS4.
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 1446303; -.
GenomeReviews BA000002_GR; APE_1869.
KEGG ape:APE_1869; -.
NMPDR fig|272557.1.peg.1333; -.
Phylogenomic databases
HOGENOM Q9YAS4; -.
Genome annotation databases
CMR Q9YAS4; APE_1869.
Other
ProtoNet Q9YAS4.
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   421  421     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114458
ACT_SITE   109   109        Charge relay system (By similarity). 
ACT_SITE   240   240        Charge relay system (By similarity). 
ACT_SITE   315   315        Charge relay system (By similarity). 
ACT_SITE   410   410        Proton donor (By similarity). 
Sequence information
Length: 421 AA [This is the length of the unprocessed precursor] Molecular weight: 44625 Da [This is the MW of the unprocessed precursor] CRC64: 9F67AF57FA651822 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGSSSGQKPR RLEDLVDKLA SGSLSHSRLE KELGNANEAA LVRRLYLERL TGASLSSVAS 

        70         80         90        100        110        120 
TILDFQELYG RNIENPIGAV QVPVGVAGPL RINGDYARGD FYIPLATTEG ALVASVNRGA 

       130        140        150        160        170        180 
KAITLSGGAR AKVIKDGMTR APLLWTPSVY EAHRLAMWVE DRIEDLRSVV AGVTRHGRLQ 

       190        200        210        220        230        240 
HIYPYIIGNL VWLRLSFSTG DAMGMNMVTI SSDRICRYIE ENYDGDAKCI ALSGNMCTDK 

       250        260        270        280        290        300 
KPAAINKILG RGKYVVAEAV IKGEVVKNVL KTTPQNINLV NVTKNLLGSA AAGSHSFNAH 

       310        320        330        340        350        360 
FANIIAAIFI ATGQDAAQVV ESSMGYTWTE VRGEDLYISV TLPSLEVGTV GGGTRLPTQR 

       370        380        390        400        410        420 
ELLALLGVAG GGNPPGSNAL KLAEIIASAV LAGELNLLSA IAAGQLARAH ELLGRGGLKI 


S 

Q9YAS4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!