3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P12684 (HMDH2_YEAST)

Last modified June 16, 2009. Version 97. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3-hydroxy-3-methylglutaryl-coenzyme A reductase 2
      Short name=HMG-CoA reductase 2
    EC=1.1.1.34

Gene names

Name:	HMG2
Ordered Locus Names:	YLR450W
ORF Names:	L9324.2

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	1045 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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; mevalonic acid biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Miscellaneous	Present with 149 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the HMG-CoA reductase family.

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Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW coenzyme A metabolic process Inferred from electronic annotation. Source: InterPro isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Traceable author statement. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope Traceable author statement. Source: SGD
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-8384,EBI-8384
AGP1	P25376	1	EBI-8384,EBI-2357
HMG1	P12683	1	EBI-8384,EBI-8377
NSG1	P38837	1	EBI-8384,EBI-24733
PHO84	P25297	1	EBI-8384,EBI-13320
PMP2	P40975	1	EBI-8384,EBI-2043041
UME1	Q03010	1	EBI-8384,EBI-20070

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1045

1045

3-hydroxy-3-methylglutaryl-coenzyme A reductase 2

PRO_0000114457

Regions

Topological domain

1 – 26

Lumenal Potential

Transmembrane

27 – 53

Potential

Topological domain

54 – 185

132

Cytoplasmic Potential

Transmembrane

186 – 210

Potential

Topological domain

211 – 240

Lumenal Potential

Transmembrane

241 – 265

Potential

Topological domain

266 – 298

Cytoplasmic Potential

Transmembrane

299 – 323

Potential

Topological domain

324 – 330

Lumenal Potential

Transmembrane

331 – 356

Potential

Topological domain

357 – 396

Cytoplasmic Potential

Transmembrane

397 – 421

Potential

Topological domain

422 – 497

Lumenal Potential

Transmembrane

498 – 523

Potential

Topological domain

524 – 1045

522

Cytoplasmic Potential

Region

524 – 613

Linker

Region

614 – 1045

432

Catalytic

Sites

Active site

710

Charge relay system By similarity

Active site

844

Charge relay system By similarity

Active site

920

Charge relay system By similarity

Active site

1016

Proton donor By similarity

Amino acid modifications

Modified residue

548

Phosphothreonine Ref.7

Modified residue

565

Phosphothreonine Ref.7 Ref.6

Modified residue

568

Phosphothreonine Ref.7

Modified residue

655

Phosphoserine Ref.7

Glycosylation

428

N-linked (GlcNAc...) Potential

Glycosylation

455

N-linked (GlcNAc...) Potential

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Sequences

Sequence

Length

Mass (Da)

Tools

P12684-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 1FD9DCD3AC01B15E
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FASTA

1,045

115,692

        10         20         30         40         50         60 
MSLPLKTIVH LVKPFACTAR FSARYPIHVI VVAVLLSAAA YLSVTQSYLN EWKLDSNQYS 

        70         80         90        100        110        120 
TYLSIKPDEL FEKCTHYYRS PVSDTWKLLS SKEAADIYTP FHYYLSTISF QSKDNSTTLP 

       130        140        150        160        170        180 
SLDDVIYSVD HTRYLLSEEP KIPTELVSEN GTKWRLRNNS NFILDLHNIY RNMVKQFSNK 

       190        200        210        220        230        240 
TSEFDQFDLF IILAAYLTLF YTLCCLFNDM RKIGSKFWLS FSALSNSACA LYLSLYTTHS 

       250        260        270        280        290        300 
LLKKPASLLS LVIGLPFIVV IIGFKHKVRL AAFSLQKFHR ISIDKKITVS NIIYEAMFQE 

       310        320        330        340        350        360 
GAYLIRDYLF YISSFIGCAI YARHLPGLVN FCILSTFMLV FDLLLSATFY SAILSMKLEI 

       370        380        390        400        410        420 
NIIHRSTVIR QTLEEDGVVP TTADIIYKDE TASEPHFLRS NVAIILGKAS VIGLLLLINL 

       430        440        450        460        470        480 
YVFTDKLNAT ILNTVYFDST IYSLPNFINY KDIGNLSNQV IISVLPKQYY TPLKKYHQIE 

       490        500        510        520        530        540 
DSVLLIIDSV SNAIRDQFIS KLLFFAFAVS ISINVYLLNA AKIHTGYMNF QPQSNKIDDL 

       550        560        570        580        590        600 
VVQQKSATIE FSETRSMPAS SGLETPVTAK DIIISEEIQN NECVYALSSQ DEPIRPLSNL 

       610        620        630        640        650        660 
VELMEKEQLK NMNNTEVSNL VVNGKLPLYS LEKKLEDTTR AVLVRRKALS TLAESPILVS 

       670        680        690        700        710        720 
EKLPFRNYDY DRVFGACCEN VIGYMPIPVG VIGPLIIDGT SYHIPMATTE GCLVASAMRG 

       730        740        750        760        770        780 
CKAINAGGGA TTVLTKDGMT RGPVVRFPTL IRSGACKIWL DSEEGQNSIK KAFNSTSRFA 

       790        800        810        820        830        840 
RLQHIQTCLA GDLLFMRFRT TTGDAMGMNM ISKGVEYSLK QMVEEYGWED MEVVSVSGNY 

       850        860        870        880        890        900 
CTDKKPAAIN WIEGRGKSVV AEATIPGDVV KSVLKSDVSA LVELNISKNL VGSAMAGSVG 

       910        920        930        940        950        960 
GFNAHAANLV TALFLALGQD PAQNVESSNC ITLMKEVDGD LRISVSMPSI EVGTIGGGTV 

       970        980        990       1000       1010       1020 
LEPQGAMLDL LGVRGPHPTE PGANARQLAR IIACAVLAGE LSLCSALAAG HLVQSHMTHN 

      1030       1040 
RKTNKANELP QPSNKGPPCK TSALL

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References

	« Hide 'large scale' referencesShow '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 XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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 772-961.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
[6]	"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-565, 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-548; THR-565; THR-568 AND SER-655, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M22255 Genomic DNA. Translation: AAA34677.1. U22382 Genomic DNA. Translation: AAB67527.1.
PIR	B30239.
RefSeq	NP_013555.1.
3D structure databases
HSSP	HSSP built from PDB template 1DQA based on UniProtKB P04035.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6277N.
IntAct	P12684. 44 interactions.
Proteomic databases
PRIDE	P12684.
Genome annotation databases
Ensembl	YLR450W. Saccharomyces cerevisiae. [Contig view]
GeneID	851171.
GenomeReviews	Gene locus YLR450W in contig Y13138_GR.
KEGG	sce:YLR450W.
NMPDR	fig\|4932.3.peg.4586.
Organism-specific databases
CYGD	YLR450w.
SGD	S000004442. HMG2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P12684.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-650.
BRENDA	1.1.1.34. 250.
Gene expression databases
ArrayExpress	P12684.
GermOnline	YLR450W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002202. HMG_CoA_Rdtase_cat. IPR004554. HMG_CoA_Rdtase_I_cat. IPR000731. SSD_5TM. [Graphical view]
Gene3D	G3DSA:3.90.770.10. HMG-CoA_red. 1 hit.
PANTHER	PTHR10572. HMG-CoA_red. 1 hit.
Pfam	PF00368. HMG-CoA_red. 1 hit. [Graphical view]
PRINTS	PR00071. HMGCOARDTASE.
TIGRFAMs	TIGR00533. HMG_CoA_R_NADP. 1 hit.
PROSITE	PS00066. 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]
ProtoNet	Search...
Other Resources
NextBio	967981.

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Entry information

Entry name

HMDH2_YEAST

Accession

Primary (citable) accession number: P12684

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents