Reviewed, UniProtKB/Swiss-Prot P34136 (HMDH2_DICDI)

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:	hmgB
ORF Names:	DDB_G0276615

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
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	integral to membrane Inferred from electronic annotation. Source: InterPro
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 – 526	526	3-hydroxy-3-methylglutaryl-coenzyme A reductase 2		PRO_0000114428
Sites
	Active site	193	1	Charge relay system By similarity
	Active site	325	1	Charge relay system By similarity
	Active site	401	1	Charge relay system By similarity
	Active site	499	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34136-1 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: 5C95CCBB7180EC92	FASTA	526	56,160
	10 20 30 40 50 60 MIRIGSNLIK QSIKNTNKSG ISRFFTTGSN NSTNYKPESC VKEEPKGKSV NVEDLKDQEI 70 80 90 100 110 120 IALVDKGEIQ PHNLETRLPN NFQRAVHIRR KLLARDLQKE HQRALHAQAV VAAAEKAATS 130 140 150 160 170 180 GEDPSSIQPV VPPTSNLDFE GSLTNLPVDH FDYTKVLGAC CENVIGYIPI PVGVAGPILL 190 200 210 220 230 240 DGKLVSIPMA TTEGCLVAST HRGAKAITKS GGAKTVLLQS GMTRAPVCRL PSSIRAGELK 250 260 270 280 290 300 QWIENQENFY QVASAFNSTS RFARLKSIKV VIAGRLVYLR FKSSTGDAMG MNMVSKGVEK 310 320 330 340 350 360 ALEVITEYFP EMEVLSLSGN VCTDKKPSSI NWLEGRGKSV VAEAVISGDI VRDVLKTTVE 370 380 390 400 410 420 ALVSLNIDKN LIGSAMAGSI GGFNAHASNI VTALYIATGQ DPAQNVESSN CITLMESING 430 440 450 460 470 480 GKDLYISVTM PSIEVGTVGG GTHLPAQSAC LDLLKIRGAN LERPGANSEQ LARVVAAAVL 490 500 510 520 SGELSLMSAL AAGHLVRSHL KHNRKTEAPA PQADTISMTH NLPHSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"The dictyostelium HMGCoA reductase genes." De Lozanne A. Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-526. Strain: AX3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000016 Genomic DNA. Translation: EAL69120.1. L19350 mRNA. Translation: AAA33215.1.
RefSeq	XP_643058.1.
3D structure databases
HSSP	HSSP built from PDB template 1HWI based on UniProtKB P04035.
ModBase	Search...
Genome annotation databases
GeneID	3394199.
KEGG	ddi:DDB_0215357.
Organism-specific databases
dictyBase	DDB_G0276615. hmgB.
Phylogenomic databases
OMA	P34136. AHFANII.
Enzyme and pathway databases
BRENDA	1.1.1.34. 424.
Family and domain databases
InterPro	IPR002202. HMG_CoA_Rdtase_cat. IPR004554. HMG_CoA_Rdtase_I_cat. [Graphical view]
Gene3D	G3DSA:3.90.770.10. HMG-CoA_red. 2 hits.
PANTHER	PTHR10572. HMG-CoA_red. 2 hits.
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMDH2_DICDI

Accession

Primary (citable) accession number: P34136
Secondary accession number(s): Q551D5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	December 4, 2007
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)