Reviewed, UniProtKB/Swiss-Prot O76819 (HMDH_AGRIP)

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:

HMGR

Organism

Agrotis ipsilon (Black cutworm moth)

Taxonomic identifier

56364 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Noctuoidea › Noctuidae › Noctuinae › Agrotis

Protein attributes

Sequence length	833 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation By similarity.
Catalytic activity	(R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH.
Enzyme regulation	The activity of HMG-CoA-reductase is suppressed by exogenous mevalonate.
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	Isoprene biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	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: InterPro 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 – 833	833	3-hydroxy-3-methylglutaryl-coenzyme A reductase		PRO_0000114429
Regions
	Transmembrane	10 – 32	23	Potential
	Transmembrane	91 – 117	27	Potential
	Transmembrane	160 – 180	21	Potential
	Transmembrane	301 – 321	21	Potential
	Region	322 – 419	98	Linker
	Region	420 – 833	414	Catalytic
Sites
	Active site	504	1	Charge relay system By similarity
	Active site	635	1	Charge relay system By similarity
	Active site	711	1	Charge relay system By similarity
	Active site	809	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	680	1	N-linked (GlcNAc...) Potential
	Glycosylation	715	1	N-linked (GlcNAc...) Potential
	Glycosylation	720	1	N-linked (GlcNAc...) Potential
	Glycosylation	813	1	N-linked (GlcNAc...) Potential
	Glycosylation	825	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O76819-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 7E9ADD4B4439A035	FASTA	833	89,790
	10 20 30 40 50 60 MKVWGAHGEF CARHQWEVIV ATLALLACAA SVERNGPGNR SEHCAGWARA CPGLEAEYQA 70 80 90 100 110 120 ADAVIMTFVR CAALLYAYYQ ISNLHKIASK YLLIIAGVFS TFASFIFTSA VASLFWSELA 130 140 150 160 170 180 SIKDAPFLFL LVADVARGAR MAKAGWSAGE DQGKRVGRAL ALLGPTATLD TLLAVLLVGV 190 200 210 220 230 240 GALSGVPRLE HMCTFACLAL LVDYLVFVTF YPACLSLVAD FASGRKEMSP DSPFSEADLK 250 260 270 280 290 300 PNPVVQRVKM IMAAGLLCVH LTSRWPWSSD NGIIEGPTDT LTPTSNDNIL LHSYVKWFSV 310 320 330 340 350 360 SADYIVIATL LCALIIKFVF FEEQRNWVID MNDMTVKEVV QEQARSKPKF SVGDDSNSEV 370 380 390 400 410 420 STQTEGVLED EWPTLSPSSS AAKLNSKKRP MAECLEIYRS EGACVSLSDE EVVMLVEQSH 430 440 450 460 470 480 IPLHRLEAVL GDPLRGVRLR RKVVGARFQT ELAIKQLPYL NYDYSKVLNA CCENVIGYVG 490 500 510 520 530 540 VPVGYAGPLV VDGKPYMIPM ATTEGALVAS TNRGAKAIGI RGVTSVVEDV GMTRAPAIKL 550 560 570 580 590 600 PNVVRAHECR QWIDNKDNYA VIKEAFDSTS RFARLQEIHI GVDGATLYLR FRATTGDAMG 610 620 630 640 650 660 MNMVSKGAEN ALKLLKNYFP DMEVISLSGN YCSDKKAAAI NWVKGRGKRV VCETTITSDS 670 680 690 700 710 720 LRTIFKTDAK TLARCNKIKN LSGSALAGSI GGNNAHAANM VTAIYIATGQ DPAQNVTSSN 730 740 750 760 770 780 CSTNMEVCGE NGEDLYVTCT MPSLEVGTVG GGTILTGQGA CLDILGVKGA GARPAENSAR 790 800 810 820 830 LASLICATVL AGELSLMAAL VNSDLVKSHM RHNRSTVNVQ VQAENITLKV PTL

References

[1]	"Molecular cloning and structural analysis of 3-hydroxy-3-methylglutaryl coenzyme A reductase of the moth Agrotis ipsilon." Duportets L., Belles X., Rossignol F., Couillaud F. Insect Mol. Biol. 9:385-392(2000) [PubMed: 10971716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ009675 mRNA. Translation: CAA08775.1.
3D structure databases
HSSP	HSSP built from PDB template 1HWI based on UniProtKB P04035.
ModBase	Search...
Family and domain databases
InterPro	IPR002202. HMG_CoA_Rdtase_cat. IPR004554. HMG_CoA_Rdtase_I_cat. IPR004816. HMG_CoA_Rdtase_I_metazoan. 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	TIGR00920. 2A060605. 1 hit. 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_AGRIP

Accession

Primary (citable) accession number: O76819

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	November 25, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)