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 O26662

[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_METTH
Primary accession number O26662
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
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: MTH_562
From
Methanobacterium thermoautotrophicum [TaxID: 187420] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Delta H;
PubMed=9371463 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.";
J. Bacteriol. 179:7135-7155(1997).
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
AE000666; AAB85068.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D69174; D69174.
RefSeq NP_275705.1; -.
3D structure databases
HSSP P04035; 1HWI. [HSSP ENTRY / PDB]
ModBase O26662.
Enzyme and pathway databases
BioCyc MTHE187420:MTH562-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; 2.
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; FALSE_NEG.
PS01192; HMG_COA_REDUCTASE_3; FALSE_NEG.
PS50065; HMG_COA_REDUCTASE_4; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1470523; -.
GenomeReviews AE000666_GR; MTH_562.
KEGG mth:MTH562; -.
NMPDR fig|187420.1.peg.560; -.
Phylogenomic databases
HOGENOM O26662; -.
Genome annotation databases
CMR O26662; MTH_562.
Other
ProtoNet O26662.
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   397  397     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114462
ACT_SITE   96    96        Charge relay system (By similarity). 
ACT_SITE   301   301        Charge relay system (By similarity). 
ACT_SITE   391   391        Proton donor (By similarity). 
Sequence information
Length: 397 AA [This is the length of the unprocessed precursor] Molecular weight: 42160 Da [This is the MW of the unprocessed precursor] CRC64: C4AA45A82EF211E4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSIMDDLMEG RIKLYEIERH VPVDEAVRIR REFIERTCGV KLEHVSNYSI DMERASRRNI 

        70         80         90        100        110        120 
ENPIGVVQIP LGVAGPLRVR GEHADGEYYV PLATSEGALV ASVNRGCSVI TRAGGATVRV 

       130        140        150        160        170        180 
TGDSMTRAPV IRTGSVVEAL QLREWIYENM DALREEAEST TRHGKLVKID PIIVAGSYVY 

       190        200        210        220        230        240 
PRFVYTTGDS MGMNMVTIAT ERALELLTRE TGAHVIALSG NLCTDKKPAA VNLIEGRGKS 

       250        260        270        280        290        300 
ITAEITVPGE MVESVLKTTP EAVVEVNTAK NLIGSAAAGS MGFNAHYANI IGAIFLATGQ 

       310        320        330        340        350        360 
DEAHIVEGSL GVTIAEERKG DLYFAVNLPD VPLATVGGGT GLETASECLD IMGVRGGGRV 

       370        380        390 
HAFAEIVGGA VLAGELSLMG ALAAGHLARA HSELGRG
O26662 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 kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!