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P12683 (HMDH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
Short name=HMG-CoA reductase 1
EC=1.1.1.34
Gene names
Name:HMG1
Ordered Locus Names:YML075C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1054 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of the sterol biosynthesis.

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.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the HMG-CoA reductase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HMG2P126843EBI-8377,EBI-8384

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 105410543-hydroxy-3-methylglutaryl-coenzyme A reductase 1
PRO_0000114456

Regions

Transmembrane27 – 5327Helical; Potential
Transmembrane187 – 21125Helical; Potential
Transmembrane242 – 26625Helical; Potential
Transmembrane300 – 32425Helical; Potential
Transmembrane332 – 35726Helical; Potential
Transmembrane398 – 42225Helical; Potential
Transmembrane499 – 52426Helical; Potential
Region525 – 61793Linker
Region618 – 1054437Catalytic

Sites

Active site7141Charge relay system By similarity
Active site8481Charge relay system By similarity
Active site9241Charge relay system By similarity
Active site10201Proton donor By similarity

Amino acid modifications

Modified residue5521Phosphothreonine Ref.5 Ref.7
Modified residue5801Phosphoserine Ref.6
Modified residue5811Phosphoserine Ref.6
Modified residue6091Phosphoserine Ref.7
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Glycosylation5571N-linked (GlcNAc...) Potential
Glycosylation7781N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P12683 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 2B624944FB7B2DD0

FASTA1,054115,626
        10         20         30         40         50         60 
MPPLFKGLKQ MAKPIAYVSR FSAKRPIHII LFSLIISAFA YLSVIQYYFN GWQLDSNSVF 

        70         80         90        100        110        120 
ETAPNKDSNT LFQECSHYYR DSSLDGWVSI TAHEASELPA PHHYYLLNLN FNSPNETDSI 

       130        140        150        160        170        180 
PELANTVFEK DNTKYILQED LSVSKEISST DGTKWRLRSD RKSLFDVKTL AYSLYDVFSE 

       190        200        210        220        230        240 
NVTQADPFDV LIMVTAYLMM FYTIFGLFND MRKTGSNFWL SASTVVNSAS SLFLALYVTQ 

       250        260        270        280        290        300 
CILGKEVSAL TLFEGLPFIV VVVGFKHKIK IAQYALEKFE RVGLSKRITT DEIVFESVSE 

       310        320        330        340        350        360 
EGGRLIQDHL LCIFAFIGCS MYAHQLKTLT NFCILSAFIL IFELILTPTF YSAILALRLE 

       370        380        390        400        410        420 
MNVIHRSTII KQTLEEDGVV PSTARIISKA EKKSVSSFLN LSVVVIIMKL SVILLFVFIN 

       430        440        450        460        470        480 
FYNFGANWVN DAFNSLYFDK ERVSLPDFIT SNASENFKEQ AIVSVTPLLY YKPIKSYQRI 

       490        500        510        520        530        540 
EDMVLLLLRN VSVAIRDRFV SKLVLSALVC SAVINVYLLN AARIHTSYTA DQLVKTEVTK 

       550        560        570        580        590        600 
KSFTAPVQKA STPVLTNKTV ISGSKVKSLS SAQSSSSGPS SSSEEDDSRD IESLDKKIRP 

       610        620        630        640        650        660 
LEELEALLSS GNTKQLKNKE VAALVIHGKL PLYALEKKLG DTTRAVAVRR KALSILAEAP 

       670        680        690        700        710        720 
VLASDRLPYK NYDYDRVFGA CCENVIGYMP LPVGVIGPLV IDGTSYHIPM ATTEGCLVAS 

       730        740        750        760        770        780 
AMRGCKAINA GGGATTVLTK DGMTRGPVVR FPTLKRSGAC KIWLDSEEGQ NAIKKAFNST 

       790        800        810        820        830        840 
SRFARLQHIQ TCLAGDLLFM RFRTTTGDAM GMNMISKGVE YSLKQMVEEY GWEDMEVVSV 

       850        860        870        880        890        900 
SGNYCTDKKP AAINWIEGRG KSVVAEATIP GDVVRKVLKS DVSALVELNI AKNLVGSAMA 

       910        920        930        940        950        960 
GSVGGFNAHA ANLVTAVFLA LGQDPAQNVE SSNCITLMKE VDGDLRISVS MPSIEVGTIG 

       970        980        990       1000       1010       1020 
GGTVLEPQGA MLDLLGVRGP HATAPGTNAR QLARIVACAV LAGELSLCAA LAAGHLVQSH 

      1030       1040       1050 
MTHNRKPAEP TKPNNLDATD INRLKDGSVT CIKS

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis."
Basson M.E., Thorsness M., Finer-Moore J., Stroud R.M., Rine J.
Mol. Cell. Biol. 8:3797-3808(1988) [PubMed: 3065625] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed: 9169872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase."
Basson M.E., Thorsness M., Rine J.
Proc. Natl. Acad. Sci. U.S.A. 83:5563-5567(1986) [PubMed: 3526336] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 776-965.
[5]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-552, MASS SPECTROMETRY.
Strain: ADR376.
[6]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND SER-581, MASS SPECTROMETRY.
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-552 AND SER-609, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M22002 Genomic DNA. Translation: AAA34676.1.
Z46373 Genomic DNA. Translation: CAA86503.1.
BK006946 Genomic DNA. Translation: DAA09822.1.
PIRA30239.
RefSeqNP_013636.1. NM_001182434.1.

3D structure databases

ProteinModelPortalP12683.
SMRP12683. Positions 597-1018.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4529N.
IntActP12683. 30 interactions.
MINTMINT-516133.
STRINGP12683.

Proteomic databases

PeptideAtlasP12683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML075C; YML075C; YML075C.
GeneID854900.
KEGGsce:YML075C.
NMPDRfig|4932.3.peg.4673.

Organism-specific databases

CYGDYML075c.
SGDS000004540. HMG1.

Phylogenomic databases

eggNOGfuNOG05469.
GeneTreeEFGT00050000005412.
HOGENOMHBG355150.
OMANAARIHT.
OrthoDBEOG43FM5D.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-649.

Gene expression databases

ArrayExpressP12683.
GenevestigatorP12683.
GermOnlineYML075C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002202. HMG_CoA_Rdtase.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR004554. HMG_CoA_Rdtase_eu_arc.
IPR023282. HMG_CoA_Rdtase_N.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd.
IPR009029. HMG_CoA_Rdtase_sub-bd.
IPR000731. SSD.
[Graphical view]
Gene3DG3DSA:3.30.70.420. G3DSA:3.30.70.420. 1 hit.
G3DSA:3.90.770.10. HMG-CoA_red. 2 hits.
G3DSA:1.10.3270.10. HMG_CoA_Rdtase_N. 1 hit.
KOK00021.
PANTHERPTHR10572. HMG-CoA_red. 1 hit.
PfamPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
PRINTSPR00071. HMGCOARDTASE.
SUPFAMSSF55035. HMG_CoA_NAD_bind. 1 hit.
SSF56542. HMG_CoA_sub_bind. 1 hit.
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. 1 hit.
PS50065. HMG_COA_REDUCTASE_4. 1 hit.
PS50156. SSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977876.

Entry information

Entry nameHMDH1_YEAST
AccessionPrimary (citable) accession number: P12683
Secondary accession number(s): D6W0K8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 14, 2011
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents