3-hydroxy-3-methylglutaryl-coenzyme A reductase - Aspergillus terreus

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Reviewed, UniProtKB/Swiss-Prot Q9Y7D2 (HMDH_ASPTE)

Last modified November 4, 2008. Version 55. History...

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

Names and origin

Protein names	Recommended name: 3-hydroxy-3-methylglutaryl-coenzyme A reductase Short name=HMG-CoA reductase EC=1.1.1.34
Organism	Aspergillus terreus
Taxonomic identifier	33178 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	1048 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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. Contains 1 SSD (sterol-sensing) domain.
Sequence caution	The sequence AAD34556.1 differs from that shown. Reason: Erroneous gene model prediction.

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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1048

3-hydroxy-3-methylglutaryl-coenzyme A reductase

PRO_0000114451

Regions

Transmembrane

21

Potential

Transmembrane

21

Potential

Transmembrane

21

Potential

Transmembrane

21

Potential

Transmembrane

21

Potential

Transmembrane

21

Potential

Domain

182

SSD

Region

154

Linker

Region

426

Catalytic

Sites

Active site

1

Charge relay system By similarity

Active site

1

Charge relay system By similarity

Active site

1

Charge relay system By similarity

Active site

1

Proton donor By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y7D2-1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 8B7B3098ADA24BDE
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1,048

112,451

        10         20         30         40         50         60 
MDPVVRKPDP GGVQHRVTKA LRAIVGHACR HPIHTLLVTA LTAATTHLHV LEGTYQATHR 

        70         80         90        100        110        120 
GLAPWAKETP LNVQSFLWGS RTVSLGEASA WKWQIDDRPK VPEDGQSDFH WALVTLDLPG 

       130        140        150        160        170        180 
ASVDASIPFL SNTLSGFLGA EQTTPTPDSS PSPDHSALTF RVPYSQLDGF LQAVEIIPSE 

       190        200        210        220        230        240 
KEDDSWRLRS PREEGSPRSL GHWLGSSWLS FLHRVHHAET VDLVIIGLSY LAMNMTVVSL 

       250        260        270        280        290        300 
FRVMRHLGSR FWLAASVLLS GAFAFVLGLG ITTTCDVPVD MLLLFEGIPY LVLTVGFEKP 

       310        320        330        340        350        360 
IQLTRAVLCV SEELWGGGQR QVPNGASSDD SRQNQLIPNI IQLAVDREGW YIVRSYLLEI 

       370        380        390        400        410        420 
GALALGAVLR PKDSLGHFCF LAAWTLLIDA VLLFTFYATI LCVKLEITRI RSPGGLGQVN 

       430        440        450        460        470        480 
AKHPSGIFGH KVKSTNITWW KLLTVGGFVL CHFLQLSPFF YRVMGEYMAN GTLPPTAVSP 

       490        500        510        520        530        540 
FKEAANGLNE IYLTARVEGF ETRVTVLPPL QYVLESAGFN ISATKRSTFD GVLDGLESPL 

       550        560        570        580        590        600 
GRLCLMGALV VSLVLNNHLI HAARWHAWPQ ARESAVPDGS YLSVPCSATA PEVCTRPPEE 

       610        620        630        640        650        660 
TEALLKSNQA ESLTDDELVE LCLRGKIAGY SLEKTLERIA AGSSRSVTRL EAFTRAVRIR 

       670        680        690        700        710        720 
RAAVSKTPST QNLCSGLAES LLPYRDYNYE LVHGACCENV VGYLPLPLGV AGPMVIDGQA 

       730        740        750        760        770        780 
LFIPMATTEG VLVASASRGC KAINAGGGAT TMLKGDGMTR GPCLRFPSAQ RAAEAQRWVE 

       790        800        810        820        830        840 
SPLGHEVLAA AFNATSRFAR LQTLTVAQAG IYLYIRFRTT TGDAMGMNMI SKGVEKALEA 

       850        860        870        880        890        900 
MAAEGGFPDM HTVTLSGNFC SDKKSAAINW IGGRGKSVIA EATIPAETVR QVLKTDVDAL 

       910        920        930        940        950        960 
VELNTAKNLV GSAMAGSLGG FNAHASNLVQ AVFLATGQDP AQNVESSSCI TTMKNIDGNL 

       970        980        990       1000       1010       1020 
HIAVSMPSME VGTIGGGTIL EAQGAMLDLL GVRGAHSTEP GANARRLARI VAAAVLAGEL 

      1030       1040 
STCAALAAGH LVNAHMQHNR SAGATVKK

References

[1]

"Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis."
Kennedy J., Auclair K., Kendrew S.G., Park C., Vederas J.C., Hutchinson C.R.
Science 284:1368-1372(1999) [PubMed: 10334994] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20542 / MF4845.

Cross-references

Sequence databases
	AF141925 Genomic DNA. Translation: AAD34556.1. Sequence problems.
3D structure databases
HSSP	HSSP built from PDB template 1DQA based on UniProtKB P04035.
ModBase	Search...
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]
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]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

HMDH_ASPTE

Accession

Primary (citable) accession number: Q9Y7D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	April 3, 2007
Last modified:	November 4, 2008
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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