ID HMDH_PHYBL Reviewed; 1176 AA. AC Q12649; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 16-JUN-2009, entry version 60. DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase; DE Short=HMG-CoA reductase; DE EC=1.1.1.34; GN Name=hmgA; OS Phycomyces blakesleeanus. OC Eukaryota; Fungi; Fungi incertae sedis; Basal fungal lineages; OC Mucoromycotina; Mucorales; Mucoraceae; Phycomyces. OX NCBI_TaxID=4837; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NRRL 1555; RA Ruiz-Albert J., Cerda-Olmedo E., Corrochano L.M.; RT "Genes for the metabolism of 3-hydroxy-3-methylglutaryl coenzyme A in RT the fungus Phycomyces."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 836-940. RC STRAIN=NRRL 1555; RA Corrochano L.M., Avalos J.; RT "Cloning a segment of the gene encoding 3-hydroxy-3-methyglutaryl RT coenzyme A reductase in Phycomyces blakesleeanus and Gibberella RT fujikuroi."; RL Exp. Mycol. 16:167-171(1992). CC -!- FUNCTION: Involved in the control of cholesterol biosynthesis. It CC is the rate-limiting enzyme of the sterol biosynthesis. CC -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3- CC hydroxy-3-methylglutaryl-CoA + 2 NADPH. CC -!- PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid CC biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. 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; X58371; CAB97179.1; -; Genomic_DNA. DR PIR; S17345; S17345. DR HSSP; P04035; 1HWI. DR BRENDA; 1.1.1.34; 278. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:EC. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002202; HMG_CoA_Rdtase_cat. DR InterPro; IPR004554; HMG_CoA_Rdtase_I_cat. DR InterPro; IPR000731; SSD_5TM. DR Gene3D; G3DSA:3.90.770.10; HMG-CoA_red; 1. DR PANTHER; PTHR10572; HMG-CoA_red; 1. DR Pfam; PF00368; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 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. DR PROSITE; PS50156; SSD; 1. PE 3: Inferred from homology; KW Cholesterol biosynthesis; Endoplasmic reticulum; Glycoprotein; KW Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; KW Sterol biosynthesis; Transmembrane. FT CHAIN 1 1176 3-hydroxy-3-methylglutaryl-coenzyme A FT reductase. FT /FTId=PRO_0000114453. FT TRANSMEM 35 55 Potential. FT TRANSMEM 300 320 Potential. FT TRANSMEM 331 351 Potential. FT TRANSMEM 623 643 Potential. FT REGION 647 744 Linker (By similarity). FT REGION 745 1176 Catalytic (By similarity). FT ACT_SITE 841 841 Charge relay system (By similarity). FT ACT_SITE 972 972 Charge relay system (By similarity). FT ACT_SITE 1048 1048 Charge relay system (By similarity). FT ACT_SITE 1146 1146 Proton donor (By similarity). FT CARBOHYD 224 224 N-linked (GlcNAc...) (Potential). FT CARBOHYD 238 238 N-linked (GlcNAc...) (Potential). FT CARBOHYD 553 553 N-linked (GlcNAc...) (Potential). FT CARBOHYD 596 596 N-linked (GlcNAc...) (Potential). FT CARBOHYD 670 670 N-linked (GlcNAc...) (Potential). FT CARBOHYD 904 904 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1013 1013 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1066 1066 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 1176 AA; 127819 MW; 6BA5C23E828DF35F CRC64; MSLPNHSGSS AFKSFSYIVG TGIKRAAKLS TRNPIEMIVV VLILSSFSYF YLFNLARTSD IFSGTVTRLY PTSVYAPTKD HSFSVVDRTA DSTIANNAVK VHLHQIVVSD PKHGVLSRQT LASVLRFQQM AENEIYVPDS TAVNRFAFNK DLCYKTTLPS SYSSHSSDSN SNSNLNSKTS PCFAHSPADI WQDEATLLAD KNIRSTIEAN LDTAKNVFGD LQLNATYASS VTLSYAFNTT GDYREHLADM WKHKVATLPP ADLVSLSNIG QQENVFAWLF IVTRNVIFRV KELIDLADNI DIIVILVGYI MMIATFISLY VNMRAMGSRY TLATAVVFNG FFSFMLALLT VRALGVDVYP VVLAEAIPFL AVTIGFERPF KLTKRVFQFS KETPLTKQEI RTTIMRAVDT VALPIARDCF MEIIVLVLGA KSGISGLEEF CLLSAILLAY DFIIMFTWYT AVLALKLELL RIREINGISA DDIKKGTKKS TGYIRRTVIK AFSDDHAAGA NTANQKADGP IIGRVKLLMI VGFVVMHIFK FCSAFQSVGP QVNITEPSIA VVLDQLLEQH KASSQASLPL FVQVFPAMPF HVATVNKSFV PDAITRPLEA LFDTYAVYIQ HPVISKWLTI ALFVSLFLNT YLFNVAKQPK QIVEQVNQDK KITNAIESTN NTHIEVTEKQ KPTIQSPGPV VSSAVVMSPN HKRSHNHHHS HSHSHNHHSN HHQSDIVRPI DECVALVRTP EMLNDEEVIS LVENGKMASY ALEKVLGDLQ RAVGIRRALI SRASITKTLE ASALPLENYH YDKVMGACCE NVIGYMPIPV GVAGPMNIDG DLIHIPMATT EGCLVASTAR GCKAINAGGG ASTIVIADGM TRGPCVEFPT ILRAAACKLW IENEGNDIVT NAFNSTSRFA RLRKLKIALA GKLVFIRFST TTGDAMGMNM ISKGCEKALS IITEHFPDMQ IISLSGNYCT DKKPAAINWI EGRGKSVVTE AVIPGAIVEK VLKTTVAALV ELNISKNLIG SAMAGSVGGF NAHAANILTA IYLATGQDPA QNVESSNCIT LMKAVNDTKD LHISCTMPSI EVGTIGGGTI LPPQQSMLDM LGVRGPHPTE PGKNAQRLAR IICAAVMAGE LSLCAALAAG HLVKAHMAHN RGTQAPTITS GPAPSTGTEP GTCIKS //