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 P34135


[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 HMDH1_DICDI
Primary accession number P34135
Secondary accession number Q55CJ2
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 55)
Name and origin of the protein
Protein name 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
Synonyms HMG-CoA reductase 1
EC 1.1.1.34
Gene name
Name: hmgA
ORFNames: DDB_0191125
From
Dictyostelium discoideum (Slime mold) [TaxID: 44689] 
Taxonomy Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AX3;
De Lozanne A.;
"The dictyostelium HMGCoA reductase genes.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
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
L19349; AAA33214.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AAFI02000005; EAL71921.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_646489.1; -.
3D structure databases
HSSP P04035; 1HWI. [HSSP ENTRY / PDB]
ModBase P34135.
Organism-specific databases
dictyBase DDB0191125; hmgA.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
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; 1.
PS50065; HMG_COA_REDUCTASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P34135.
Genome annotation databases
GeneID 3397705; -.
KEGG ddi:DDB_0191125; -.
Other
ProtoNet P34135.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Complete proteome; Endoplasmic reticulum; Glycoprotein; Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   552  552     3-hydroxy-3-methylglutaryl-coenzyme A reductase 1. PRO_0000114427
ACT_SITE   237   237        Charge relay system (By similarity). 
ACT_SITE   369   369        Charge relay system (By similarity). 
ACT_SITE   445   445        Charge relay system (By similarity). 
ACT_SITE   543   543        Proton donor (By similarity). 
CARBOHYD   288   288        N-linked (GlcNAc...) (Potential). 
CARBOHYD   375   375        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 552 AA [This is the length of the unprocessed precursor] Molecular weight: 60387 Da [This is the MW of the unprocessed precursor] CRC64: 3535CF268CDCE693 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLFAPPNLET KELFWIIYIL ILIPKVFAKV MSVRELFPFF KWGFNIRRSN FLVPILSNNV 

        70         80         90        100        110        120 
IVTGEEAVQY EKPLPYIPQH NQQQQQKQQP SQDYIQQPQN DNNINSGKEQ EQQQQQQQQQ 

       130        140        150        160        170        180 
QQTPDITNQP TKTNKKIPIK ELSNEEILIK LEKGEVLAYR LENELGDCSR AVEIRRMLLE 

       190        200        210        220        230        240 
KQLSKKIEPI PHEGFDFAKV QGQCCENVIG YVPIPVGTAG PIQLNGQLVT IPMATTEGCL 

       250        260        270        280        290        300 
VASTHRGCKA ITESGGAKCT ITSRGMTRAP VVRFSDIVKA SEFVSWINDT DNYQALKAVF 

       310        320        330        340        350        360 
DSTSRFARLS AIKCTIAGRS VYIRFKCDTG DAMGMNMVSK GVEAVLEHLK IIFDDMTLLS 

       370        380        390        400        410        420 
ISGNMCTDKK PSSINWTEGR GRSVVCEAMI TGDVVQRVLK TNVQALVDLN IAKNLIGSAM 

       430        440        450        460        470        480 
AGSIGGFNAH ASNIVTAIFL ATGQDCAQNV ESSNCITQME ACNDGQDLYI TVTMPSIEVG 

       490        500        510        520        530        540 
TVGGGTSLPA QSACLDIIGV KGSSSSKPGA NADQLAKTIA SAVMAGELSL MSALSAGHLM 

       550 
KSHLQYNRAK TN 

P34135 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 ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!