Reviewed, UniProtKB/Swiss-Prot P13702 (MVAA_PSEMV)

Names and origin

Protein names

Recommended name:
    3-hydroxy-3-methylglutaryl-coenzyme A reductase
      Short name=HMG-CoA reductase
    EC=1.1.1.88

Gene names

Name:

mvaA

Organism

Pseudomonas mevalonii

Taxonomic identifier

32044 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.
Catalytic activity	(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH.
Pathway	Metabolic intermediate metabolism; mevalonic acid degradation; HMG-CoA from (R)-mevalonic acid: step 1/1.
Subunit structure	Homotetramer.
Induction	Coinduction with mevalonate transport system.
Sequence similarities	Belongs to the HMG-CoA reductase family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	coenzyme A metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase 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 – 428

428

3-hydroxy-3-methylglutaryl-coenzyme A reductase

PRO_0000114467

Sites

Active site

83

1

Charge relay system

Active site

267

1

Charge relay system

Active site

283

1

Charge relay system

Active site

381

1

Proton donor Ref.4

Experimental info

Mutagenesis

52

1

E → Q: No loss of activity.

Mutagenesis

83

1

E → Q: Greatly reduced activity.

Mutagenesis

183

1

D → A or N: Reduced activity.

Mutagenesis

381

1

H → A, N, Q or K: Reduced activity.

Secondary structure

1

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428

Helix Strand Turn

Details...

Helix

10 – 12

3

Helix

15 – 26

12

Helix

30 – 37

8

Helix

44 – 50

7

Beta strand

51 – 65

15

Beta strand

77 – 80

4

Helix

86 – 98

13

Turn

99 – 101

3

Beta strand

103 – 107

5

Beta strand

111 – 120

10

Helix

124 – 133

10

Helix

135 – 143

9

Helix

147 – 151

5

Beta strand

155 – 164

10

Beta strand

172 – 180

9

Helix

187 – 205

19

Beta strand

207 – 214

8

Beta strand

221 – 229

9

Helix

231 – 234

4

Beta strand

237 – 239

3

Helix

241 – 257

17

Helix

259 – 279

21

Helix

284 – 295

12

Turn

296 – 298

3

Beta strand

304 – 309

6

Beta strand

315 – 322

8

Beta strand

327 – 329

3

Helix

331 – 334

4

Helix

336 – 345

10

Helix

350 – 373

24

Helix

379 – 384

6

Turn

385 – 387

3

Helix

388 – 393

6

Turn

398 – 400

3

Helix

401 – 407

7

Turn

408 – 411

4

Helix

415 – 418

4

Helix

420 – 426

7

Sequences

	Sequence		Length	Mass (Da)
	P13702-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 3302701FE6E1B1F3	FASTA	428	45,590
	10 20 30 40 50 60 MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM IENVIGTFEL 70 80 90 100 110 120 PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN GGFTTSSSAP LMHAQVQIVG 130 140 150 160 170 180 IQDPLNARLS LLRRKDEIIE LANRKDQLLN SLGGGCRDIE VHTFADTPRG PMLVAHLIVD 190 200 210 220 230 240 VRDAMGANTV NTMAEAVAPL MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS 250 260 270 280 290 300 GEAVIEGILD AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH 310 320 330 340 350 360 YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA QALAEIAVAV 370 380 390 400 410 420 GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV DWVARQLVEY HDVRADRAVA LLKQKRGQ

References

[1]	"Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase." Beach M.J., Rodwell V.W. J. Bacteriol. 171:2994-3001(1989) [PubMed: 2656635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level." Wang Y., Beach M.J., Rodwell V.W. J. Bacteriol. 171:5567-5571(1989) [PubMed: 2477360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
[3]	"Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase." Wang Y., Darnay B.G., Rodwell V.W. J. Biol. Chem. 265:21634-21641(1990) [PubMed: 2123872] [Abstract] Cited for: MUTAGENESIS.
[4]	"Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase." Darnay B.G., Wang Y., Rodwell V.W. J. Biol. Chem. 267:15064-15070(1992) [PubMed: 1634543] [Abstract] Cited for: ACTIVE SITE HIS-381.
[5]	"Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase." Tabernero L., Bochar D.A., Rodwell V.W., Stauffacher C.V. Proc. Natl. Acad. Sci. U.S.A. 96:7167-7171(1999) [PubMed: 10377386] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QAX	X-ray	2.80	A/B	1-428	[»]
1QAY	X-ray	2.80	A/B	1-428	[»]
1R31	X-ray	2.10	A/B	1-428	[»]
1R7I	X-ray	2.21	A/B	1-428	[»]
1T02	X-ray	2.60	A/B	1-428	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11829.

BRENDA

1.1.1.88. 3627.

Family and domain databases

InterPro

IPR002202. HMG_CoA_Rdtase_cat.
IPR004553. HMG_CoA_Rdtase_II_bac/I_arc.
[Graphical view]

Gene3D

G3DSA:3.90.770.10. HMG-CoA_red. 1 hit.

TIGRFAMs

TIGR00532. HMG_CoA_R_NAD. 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

MVAA_PSEMV

Accession

Primary (citable) accession number: P13702

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	March 24, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)