ID MVAA_PSEMV Reviewed; 428 AA. AC P13702; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 25-NOV-2008, entry version 74. DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase; DE Short=HMG-CoA reductase; DE EC=1.1.1.88; GN Name=mvaA; OS Pseudomonas mevalonii. OC Bacteria; Proteobacteria. OX NCBI_TaxID=32044; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=89255053; PubMed=2656635; RA Beach M.J., Rodwell V.W.; RT "Cloning, sequencing, and overexpression of mvaA, which encodes RT Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A RT reductase."; RL J. Bacteriol. 171:2994-3001(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4. RX MEDLINE=90008795; PubMed=2477360; RA Wang Y., Beach M.J., Rodwell V.W.; RT "(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the RT mva operon of Pseudomonas mevalonii, is regulated at the RT transcriptional level."; RL J. Bacteriol. 171:5567-5571(1989). RN [3] RP MUTAGENESIS. RX MEDLINE=91072362; PubMed=2123872; RA Wang Y., Darnay B.G., Rodwell V.W.; RT "Identification of the principal catalytically important acidic RT residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase."; RL J. Biol. Chem. 265:21634-21641(1990). RN [4] RP ACTIVE SITE HIS-381. RX MEDLINE=92340555; PubMed=1634543; RA Darnay B.G., Wang Y., Rodwell V.W.; RT "Identification of the catalytically important histidine of 3-hydroxy- RT 3-methylglutaryl-coenzyme A reductase."; RL J. Biol. Chem. 267:15064-15070(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=99307381; PubMed=10377386; DOI=10.1073/pnas.96.13.7167; RA Tabernero L., Bochar D.A., Rodwell V.W., Stauffacher C.V.; RT "Substrate-induced closure of the flap domain in the ternary complex RT structures provides insights into the mechanism of catalysis by 3- RT hydroxy-3-methylglutaryl-CoA reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 96:7167-7171(1999). CC -!- FUNCTION: P.mevalonii can use mevalonate as sole carbon source. CC With this enzyme mevalonate is deacetylated to HMG-CoA. CC -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NAD(+) = 3-hydroxy-3- CC methylglutaryl-CoA + 2 NADH. CC -!- PATHWAY: Metabolic intermediate metabolism; mevalonic acid CC degradation; HMG-CoA from (R)-mevalonic acid: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- INDUCTION: Coinduction with mevalonate transport system. CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M24015; AAA25837.1; -; Genomic_DNA. DR EMBL; M29727; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PDB; 1QAX; X-ray; 2.80 A; A/B=1-428. DR PDB; 1QAY; X-ray; 2.80 A; A/B=1-428. DR PDB; 1R31; X-ray; 2.10 A; A/B=1-428. DR PDB; 1R7I; X-ray; 2.21 A; A/B=1-428. DR PDB; 1T02; X-ray; 2.60 A; A/B=1-428. DR PDBsum; 1QAX; -. DR PDBsum; 1QAY; -. DR PDBsum; 1R31; -. DR PDBsum; 1R7I; -. DR PDBsum; 1T02; -. DR BioCyc; MetaCyc:MON-11829; -. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:InterPro. DR GO; GO:0042282; F:hydroxymethylglutaryl-CoA reductase activity; IEA:EC. DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002202; HMG_CoA_Rdtase_cat. DR InterPro; IPR004553; HMG_CoA_Rdtase_II_bac/I_arc. DR Gene3D; G3DSA:3.90.770.10; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR TIGRFAMs; TIGR00532; HMG_CoA_R_NAD; 1. DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1. DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1. DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1. DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase. FT CHAIN 1 428 3-hydroxy-3-methylglutaryl-coenzyme A FT reductase. FT /FTId=PRO_0000114467. FT ACT_SITE 83 83 Charge relay system. FT ACT_SITE 267 267 Charge relay system. FT ACT_SITE 283 283 Charge relay system. FT ACT_SITE 381 381 Proton donor. FT MUTAGEN 52 52 E->Q: No loss of activity. FT MUTAGEN 83 83 E->Q: Greatly reduced activity. FT MUTAGEN 183 183 D->A,N: Reduced activity. FT MUTAGEN 381 381 H->A,N,Q,K: Reduced activity. FT HELIX 10 12 FT HELIX 15 26 FT HELIX 30 37 FT HELIX 44 50 FT STRAND 51 65 FT STRAND 77 80 FT HELIX 86 98 FT TURN 99 101 FT STRAND 103 107 FT STRAND 111 120 FT HELIX 124 133 FT HELIX 135 143 FT HELIX 147 151 FT STRAND 155 164 FT STRAND 172 180 FT HELIX 187 205 FT STRAND 207 214 FT STRAND 221 229 FT HELIX 231 234 FT STRAND 237 239 FT HELIX 241 257 FT HELIX 259 279 FT HELIX 284 295 FT TURN 296 298 FT STRAND 304 309 FT STRAND 315 322 FT STRAND 327 329 FT HELIX 331 334 FT HELIX 336 345 FT HELIX 350 373 FT HELIX 379 384 FT TURN 385 387 FT HELIX 388 393 FT TURN 398 400 FT HELIX 401 407 FT TURN 408 411 FT HELIX 415 418 FT HELIX 420 426 SQ SEQUENCE 428 AA; 45590 MW; 3302701FE6E1B1F3 CRC64; MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM IENVIGTFEL PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN GGFTTSSSAP LMHAQVQIVG IQDPLNARLS LLRRKDEIIE LANRKDQLLN SLGGGCRDIE VHTFADTPRG PMLVAHLIVD VRDAMGANTV NTMAEAVAPL MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS GEAVIEGILD AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA QALAEIAVAV GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV DWVARQLVEY HDVRADRAVA LLKQKRGQ //