Reviewed, UniProtKB/Swiss-Prot O74164 (HMDH_PICJA)

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:

HMG

Organism

Pichia jadinii (Yeast) (Candida utilis)

Taxonomic identifier

4903 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	934 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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
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: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 934	934	3-hydroxy-3-methylglutaryl-coenzyme A reductase		PRO_0000114454
Regions
	Transmembrane	112 – 132	21	Potential
	Transmembrane	142 – 162	21	Potential
	Transmembrane	257 – 277	21	Potential
	Transmembrane	335 – 355	21	Potential
	Transmembrane	422 – 442	21	Potential
	Region	443 – 521	79	Linker
	Region	522 – 934	413	Catalytic
Sites
	Active site	618	1	Charge relay system By similarity
	Active site	752	1	Charge relay system By similarity
	Active site	828	1	Charge relay system By similarity
	Active site	924	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	361	1	N-linked (GlcNAc...) Potential
	Glycosylation	364	1	N-linked (GlcNAc...) Potential
	Glycosylation	382	1	N-linked (GlcNAc...) Potential
	Glycosylation	682	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O74164-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 3C3E43FC5623601C	FASTA	934	101,234
	10 20 30 40 50 60 MFYHGASANQ HWIAVDDLSK VPVDVDHYNV VPFQFRRAGE YKEPVLSGIV ELDEVKFVVS 70 80 90 100 110 120 QSDAAEQWQQ LTAEDGTVWR SRAYHGKLGK YSDMAVGAFN KVLNLVRGAE TFDIALVTCA 130 140 150 160 170 180 YIAMFYTLFN LFARMRAVGS KVWLGLSTLV SSFFAFLFAL YITTRVLDLS IPFLSLSEGI 190 200 210 220 230 240 PFFVAVVGFN NKILLAEKVL QNQLNAQSSK NDAPTVLYQA LREQGPLLLR DHLFMITAFL 250 260 270 280 290 300 GCSFYASYLD GLKNFCILAA LILAFDILTT STFLSAILSL KLEINQIHRS TLLREQLEDD 310 320 330 340 350 360 GLTETTVDDV LKSNSLAGTK TFTDAPSTLV TVAKVAGVSV FFGLHFYGFG SAWLSDLSAG 370 380 390 400 410 420 NETNDTFTLY DAVADQIPIG SNGTLVTLFP TRFFLPEKLS TQIEAVVLSF IGLISTAARD 430 440 450 460 470 480 KYISKFILFA FAVSASINVY LLNVARIHTT RLEDAIELKK PKKKASKTAV SVPKAVVVKD 490 500 510 520 530 540 SETTKSSEIL HSSSESESEQ SSRPLEQVIE LYKDGKVKTL VDDEVVSLVT AGKLPLYALE 550 560 570 580 590 600 KQLGDNLRAV AIRRKAISDL ADAPVLRSNK LPYLHYDYDR VFGACCENVI GYMPLPVGVA 610 620 630 640 650 660 GPLIIDGKPY HIPMATTEGC LVASAMRGCK AINLGGGVTT VLTKDGMTRG PCVKFPSLKR 670 680 690 700 710 720 AGQCKLWLDS DEGQEEMKKA FNSTSRFARL QHLQTALAGD LLFIRFRTVT GDAMGMNMIS 730 740 750 760 770 780 KGVEYALKQM TEVFGWDDMM VVSVSGNYCT DKKPAAVNWI NGRGKSVVAE ASIPKDAVVK 790 800 810 820 830 840 VLKSSVKAVV DVNVNKNLIG SAMAGSVGGF NAQAANMVTA VYLALGQDPA QNVESSNCIT 850 860 870 880 890 900 LMTETEDGDL KVSVSMPSIE VGTIGGGTIL DPQGSMLELL GVRGPADVPG ENARQLAKIV 910 920 930 ASIVLSGELS LVSALAAGHL VQSHMQHNRA AAKK

References

[1]

"Increased carotenoid production by the food yeast Candida utilis through metabolic engineering of the isoprenoid pathway." Shimada H., Kondo K., Fraser P.D., Miura Y., Saito T., Misawa N. Appl. Environ. Microbiol. 64:2676-2680(1998) [PubMed: 9647847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB012603 mRNA. Translation: BAA31937.1.
3D structure databases
HSSP	HSSP built from PDB template 1DQA based on UniProtKB P04035.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.34. 288941.
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...

Entry information

Entry name

HMDH_PICJA

Accession

Primary (citable) accession number: O74164

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)