Reviewed, UniProtKB/Swiss-Prot Q10283 (HMDH_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	hmg1
ORF Names:	SPCC162.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1053 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Sequence similarities	Belongs to the HMG-CoA reductase family.

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 Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: InterPro
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1053	1053	3-hydroxy-3-methylglutaryl-coenzyme A reductase		PRO_0000114455
Regions
	Transmembrane	9 – 29	21	Potential
	Transmembrane	204 – 224	21	Potential
	Transmembrane	233 – 253	21	Potential
	Transmembrane	259 – 279	21	Potential
	Transmembrane	321 – 341	21	Potential
	Transmembrane	342 – 362	21	Potential
	Transmembrane	418 – 438	21	Potential
	Transmembrane	527 – 547	21	Potential
	Region	548 – 615	68	Linker
	Region	616 – 1053	438	Catalytic
Sites
	Active site	712	1	Charge relay system By similarity
	Active site	846	1	Charge relay system By similarity
	Active site	922	1	Charge relay system By similarity
	Active site	1018	1	Proton donor By similarity
Amino acid modifications
	Modified residue	1024	1	Phosphoserine
	Modified residue	1028	1	Phosphothreonine
	Glycosylation	137	1	N-linked (GlcNAc...) Potential
	Glycosylation	399	1	N-linked (GlcNAc...) Potential
	Glycosylation	518	1	N-linked (GlcNAc...) Potential
	Glycosylation	578	1	N-linked (GlcNAc...) Potential
	Glycosylation	776	1	N-linked (GlcNAc...) Potential
	Glycosylation	1022	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	751	1	N → D in AAB39277. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10283-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 33E5C2365222D238	FASTA	1,053	114,877
	10 20 30 40 50 60 MIYKLAARYP IQVIAIVGIL VSMAYFSFLE ALTQEDFPVL IRALKRFGIL DGFPNTRLPN 70 80 90 100 110 120 EMILKLSSVQ GEDASVWEQI PAAELGGEGF VDFDITQWYY PANAKVDVAQ LVEPYRNDCI 130 140 150 160 170 180 FHDASGACHF FFKEVGNWTV SSIALPSNLA NPPIDYFLDS SSTVIQRILP AIREHGISWS 190 200 210 220 230 240 WLLQLIARTW MNTLKIASQA SKTELLIVGT AYACMLISIV SLYLKMRRLG SKFWLFFSVL 250 260 270 280 290 300 LSTLFSVQFA MTLVRASGVR ISLVSLIESL PFLINVVALD KAAELTRQVI TRCSVSDSHS 310 320 330 340 350 360 PMHEDIAKAC RNAAPPILRH FSFGIVVLAI FSYCNFGIKQ FFLFAAVMIY DLLLLFSFFV 370 380 390 400 410 420 AILTLKLEMR RYNAKDDVRK VLIEEGLSES TARHVADGND SSATTSAGSR YFKVRYGTKI 430 440 450 460 470 480 ILFIFIAFNL FELCSIPFKH YAATSAAAAR LIPLVRSQYP DFKSQRLLDD GVFDDVLSAI 490 500 510 520 530 540 SSMSNIESPS VRLLPAVFYG AELSSTSFLS TIHSFINNWS HYISASFLSK WIVCALSLSI 550 560 570 580 590 600 AVNVFLLNAA RLNSIKEEPE KKVVEKVVEV VKYIPSSNSS SIDDIQKDEI AQESVVRSLE 610 620 630 640 650 660 ECITLYNNGQ ISTLNDEEVV QLTLAKKIPL YALERVLKDV TRAVVIRRTV VSRSSRTKTL 670 680 690 700 710 720 ESSNCPVYHY DYSRVLNACC ENVIGYMPLP LGVAGPLIID GKPFYIPMAT TEGALVASTM 730 740 750 760 770 780 RGCKAINAGG GAVTVLTRDQ MSRGPCVAFP NLTRAGRAKI WLDSPEGQEV MKKAFNSTSR 790 800 810 820 830 840 FARLQHIKTA LAGTRLFIRF CTSTGDAMGM NMISKGVEHA LVVMSNDAGF DDMQVISVSG 850 860 870 880 890 900 NYCTDKKPAA INWIDGRGKS VIAEAIIPGD AVKSVLKTTV EDLVKLNVDK NLIGSAMAGS 910 920 930 940 950 960 VGGFNAHAAN IVTAVYLATG QDPAQNVESS NCITLMDNVD GNLQLSVSMP SIEVGTIGGG 970 980 990 1000 1010 1020 TVLEPQGAML DLLGVRGAHM TSPGDNSRQL ARVVAAAVMA GELSLCSALA SGHLVKSHIG 1030 1040 1050 LNRSALNTPA MDSSAKKPAT DALKSVNSRV PGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe." Lum P.Y., Edwards S., Wright R. Yeast 12:1107-1124(1996) [PubMed: 8896278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1024 AND THR-1028, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L76979 Genomic DNA. Translation: AAB39277.1. CU329672 Genomic DNA. Translation: CAA19589.1.
PIR	S72194.
RefSeq	NP_588235.1.
3D structure databases
HSSP	HSSP built from PDB template 1DQA based on UniProtKB P04035.
ModBase	Search...
Genome annotation databases
GeneID	2538999.
KEGG	spo:SPCC162.09c.
NMPDR	fig|4896.1.peg.573.
Organism-specific databases
GeneDB_Spombe	SPCC162.09c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000166-MON.
Gene expression databases
ArrayExpress	Q10283.
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. False negative. PS50065. HMG_COA_REDUCTASE_4. 1 hit. PS50156. SSD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMDH_SCHPO

Accession

Primary (citable) accession number: Q10283
Secondary accession number(s): O74425

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)