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Conserved domains on  [gi|5542336|pdb|1QAY|B]
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Chain B, Ternary Complex Of Pseudomonas Mevalonii Hmg-coa Reductase With Mevalonate And Nad+

Protein Classification

hydroxymethylglutaryl-CoA reductase (domain architecture ID 10089851)

hydroxymethylglutaryl-CoA reductase catalyzes the deacetylation of mevalonate to form 3-hydroxy-3-methylglutaryl-CoA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HMG-CoA_reductase_classII cd00644
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
8-426 0e+00

Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.


:

Pssm-ID: 153082  Cd Length: 417  Bit Score: 663.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        8 PAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIV 87
Cdd:cd00644   1 KGFYKLSPEERLQILAEFAGLSEEDVQLLKSGGALPLELADQMIENVIGTFSLPLGVATNFLVNGKDYLVPMATEEPSVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       88 AAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHTFaDT 167
Cdd:cd00644  81 AAASNAAKIARKSGGFKTSSSDRLMIGQIQLVDVSDPAKARAFILAHKDEILEIANEAHPSLVKRGGGARDIEVRVL-DA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      168 PRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEAVIEG 247
Cdd:cd00644 160 DLGDFLSVHLLVDTKDAMGANIVNTMLEAVAPLLEEITGGEVLLRILSNYATERLVRAKVSIPVEALGTKGGSGEEVAKK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      248 ILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDnNGHLVGTLEMPMPVGL 327
Cdd:cd00644 240 IALASAFAQVDPYRAATHNKGIMNGIDAVVLATGNDWRAVEAGAHAYAARSGQYRSLSTWEID-DGKLVGELELPLAVGT 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      328 VGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQL 407
Cdd:cd00644 319 VGGSTKVHPLAKLALKILGVPSAKELAEIIAAVGLAQNFAALRALATEGIQKGHMKLHARNLAIAAGATGEEIDKVVKQL 398
                       410
                ....*....|....*....
1QAY_B      408 VEYHDVRADRAVALLKQKR 426
Cdd:cd00644 399 IEEKTVNLERAKEILKELR 417
 
Name Accession Description Interval E-value
HMG-CoA_reductase_classII cd00644
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
8-426 0e+00

Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.


Pssm-ID: 153082  Cd Length: 417  Bit Score: 663.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        8 PAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIV 87
Cdd:cd00644   1 KGFYKLSPEERLQILAEFAGLSEEDVQLLKSGGALPLELADQMIENVIGTFSLPLGVATNFLVNGKDYLVPMATEEPSVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       88 AAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHTFaDT 167
Cdd:cd00644  81 AAASNAAKIARKSGGFKTSSSDRLMIGQIQLVDVSDPAKARAFILAHKDEILEIANEAHPSLVKRGGGARDIEVRVL-DA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      168 PRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEAVIEG 247
Cdd:cd00644 160 DLGDFLSVHLLVDTKDAMGANIVNTMLEAVAPLLEEITGGEVLLRILSNYATERLVRAKVSIPVEALGTKGGSGEEVAKK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      248 ILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDnNGHLVGTLEMPMPVGL 327
Cdd:cd00644 240 IALASAFAQVDPYRAATHNKGIMNGIDAVVLATGNDWRAVEAGAHAYAARSGQYRSLSTWEID-DGKLVGELELPLAVGT 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      328 VGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQL 407
Cdd:cd00644 319 VGGSTKVHPLAKLALKILGVPSAKELAEIIAAVGLAQNFAALRALATEGIQKGHMKLHARNLAIAAGATGEEIDKVVKQL 398
                       410
                ....*....|....*....
1QAY_B      408 VEYHDVRADRAVALLKQKR 426
Cdd:cd00644 399 IEEKTVNLERAKEILKELR 417
HMG-CoA_red pfam00368
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
14-386 3.49e-136

Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels.


Pssm-ID: 334039  Cd Length: 369  Bit Score: 394.87  E-value: 3.49e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         14 SPAARLDHIGQLLGlshDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAASYM 93
Cdd:pfam00368   1 AVEERREFLEELTG---EELEHLGDGSLDYSEVADANIENVIGYVQLPLGVAGPLLINGKDYYVPMATTEGSLVASASRG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         94 AKLARANGGFTTSSSA-PLMHAQVQIVG-IQDPLNARLSlLRRKDEIIELANRKDQllNSLGGGCRDIEVHTFadtprGP 171
Cdd:pfam00368  78 AKAITASGGFTTTVLGdGMTRGPVFLFPsVADAAEAKQW-IENKENLLEIANAAEP--TSRGGGLRDIEVYIA-----GR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        172 MLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQL-ETAE-FSGEAVIEGIL 249
Cdd:pfam00368 150 MLYLRFTVDTGDAMGANMVNKATEAAAPLIEEEFGGMVLLSILSNLCTDKKPSAINWIEGRGKsVVAEaTIPEEVVKKIL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        250 DAYAFAAVDPYRA---ATHNKGI-------MNGIDPLIVATGNDWRAVEAGAHAYAcrsghygSLTTWEkdnNGHLVGTL 319
Cdd:pfam00368 230 KASPEALVDPYRAkniGTHNKGIiggnahaANGIAAVFLATGQDPAAVEESSHAYA-------ALETWE---DGDLYGSV 299
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1QAY_B        320 EMP-MPVGLVGGATKTHPLAQLsLRILGVKTA---QALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHA 386
Cdd:pfam00368 300 TLPsLEVGTVGGGTGLPPQAEC-LKLLGVKGAgkpRELAEIIAAVGLAGELSALRALATGGIQKGHMKLGR 369
HMG_CoA_R_NAD TIGR00532
hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of ...
5-386 2.39e-133

hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of hydroxymethylglutaryl-CoA reductase are NADP-dependent (EC 1.1.1.34) from eukaryotes and archaea, involved in the biosynthesis of mevalonate from 3-hydroxy-3-methylglutaryl-CoA. This model, in contrast, is built from the two examples in completed genomes of sequences closely related to the degradative, NAD-dependent hydroxymethylglutaryl-CoA reductase of Pseudomonas mevalonii, a bacterium that can use mevalonate as its sole carbon source. [Energy metabolism, Other]


Pssm-ID: 129623  Cd Length: 393  Bit Score: 388.62  E-value: 2.39e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B          5 SRLPAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGAlPMDIA-NGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEE 83
Cdd:TIGR00532  13 SKIFGFYHKSVEEKLKEIAEFAELSDEEVKAFFSNGA-NEDFAfDRMIENVIGTFEFPIGIAKNFKIDGKDYLIPIAIEE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         84 PSIVAAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHT 163
Cdd:TIGR00532  92 PSVVAAANFAAKIAEEADGFTSDGEGLGIIGQIQQIKIKNEKAAKFEFLDLGDEIIERAEECDPMLNNLGGGCKDIEARV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        164 FaDTPRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEA 243
Cdd:TIGR00532 172 I-DIIEGGILILHIIVDTCDAMGANALNSIAEKVAEFIELEFGGECVLKIISNDAAEFTAKARAKADFDHDLIGGEDSWN 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        244 VIEGILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDNNGHLVGTLEMPM 323
Cdd:TIGR00532 251 LAEGIELASAFAAADEERAATHNKGIMNGISALCIATFNDFRAIEAGAHKFAAIGGKYFPLSKFEVDRDGALVGEIEIPL 330
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
1QAY_B        324 PVGLVGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHA 386
Cdd:TIGR00532 331 AVGTIGGAIKFNEAAIISFKILGVNSAEEFAGIAAALGLAQNFAALRALAFEGIQKGHMELHA 393
HMG1 COG1257
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism];
12-426 2.48e-132

Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism];


Pssm-ID: 224177  Cd Length: 436  Bit Score: 387.46  E-value: 2.48e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       12 NLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAAS 91
Cdd:COG1257  23 NKAVEERRQALERFTGLSLEEIGSLSIDGSLPIDVANRNIENVIGTVQLPLGIAGPLLINGKEYYIPMATTEGALVASAS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       92 YMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDqllNSLGGGCRDIEVHTFadtPRGP 171
Cdd:COG1257 103 RGAKLITASGGATARVTEDGMTRQPVFRFVSLPEAAKFAIWVKKKEIIELAKEAA---PSTGRGGKLIHIEPF---VEGN 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      172 MLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAIT-GGQVRLRILSNLADLR--LARAQVRITPQQLETAEFSGEAVIEGI 248
Cdd:COG1257 177 LLYLRFYVDTGDAMGMNMVNIATEAVAPFIEEETfGGAVLLAISSNLCTDKkpAAINSIEGRGKTVVAEATIPEEVVKKI 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      249 LDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDNN-GHLVGTLEMPMPVGL 327
Cdd:COG1257 257 LKATPEAIVDVNRAKTLNGGAMNGIDGFNAHTANDVRAIEAATGQDAAQVGEYSPLITWMEDQRdGDLYGSVTLPSLVVG 336
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      328 VGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQL 407
Cdd:COG1257 337 TGGGGTVLPTQREALKILGVAGAGELAGVLAAVGLAQNAAALAALVAEGILAGEMSLLAALAAGHLGAAHDELGRVVERL 416
                       410
                ....*....|....*....
1QAY_B      408 VEYHDVRADRAVALLKQKR 426
Cdd:COG1257 417 IREKNINLEVAKKILEKLR 435
 
Name Accession Description Interval E-value
HMG-CoA_reductase_classII cd00644
Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
8-426 0e+00

Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.


Pssm-ID: 153082  Cd Length: 417  Bit Score: 663.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        8 PAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIV 87
Cdd:cd00644   1 KGFYKLSPEERLQILAEFAGLSEEDVQLLKSGGALPLELADQMIENVIGTFSLPLGVATNFLVNGKDYLVPMATEEPSVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       88 AAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHTFaDT 167
Cdd:cd00644  81 AAASNAAKIARKSGGFKTSSSDRLMIGQIQLVDVSDPAKARAFILAHKDEILEIANEAHPSLVKRGGGARDIEVRVL-DA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      168 PRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEAVIEG 247
Cdd:cd00644 160 DLGDFLSVHLLVDTKDAMGANIVNTMLEAVAPLLEEITGGEVLLRILSNYATERLVRAKVSIPVEALGTKGGSGEEVAKK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      248 ILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDnNGHLVGTLEMPMPVGL 327
Cdd:cd00644 240 IALASAFAQVDPYRAATHNKGIMNGIDAVVLATGNDWRAVEAGAHAYAARSGQYRSLSTWEID-DGKLVGELELPLAVGT 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      328 VGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQL 407
Cdd:cd00644 319 VGGSTKVHPLAKLALKILGVPSAKELAEIIAAVGLAQNFAALRALATEGIQKGHMKLHARNLAIAAGATGEEIDKVVKQL 398
                       410
                ....*....|....*....
1QAY_B      408 VEYHDVRADRAVALLKQKR 426
Cdd:cd00644 399 IEEKTVNLERAKEILKELR 417
HMG-CoA_reductase cd00365
Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A ...
8-386 1.31e-180

Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) is a tightly regulated enzyme, which catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals, this is the rate limiting committed step in cholesterol biosynthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. There are two classes of HMGR: class I enzymes which are found predominantly in eukaryotes and contain N-terminal membrane regions and class II enzymes which are found primarily in prokaryotes and are soluble as they lack the membrane region. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture. While the prokaryotic enzyme is a homodimer, the eukaryotic enzyme is a homotetramer.


Pssm-ID: 153080  Cd Length: 376  Bit Score: 507.99  E-value: 1.31e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        8 PAFRNLSPAA-RLDHIGQLLGLSHDDVSLLANAgALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSI 86
Cdd:cd00365   1 PAFRTLSPHAaRLDHIGQLLGLSHDDVQLLANA-ALPMDIANGMIENVIGTFELPYAVASNFQIDGRDVLVPLVTEEPSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       87 VAAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRR-KDEIIELANRKDQLLNSLGGGCRDIEVHTFa 165
Cdd:cd00365  80 VAAASYMAKLARAGGGFTTSSSAPLMHAQVQIVLIQDPLNAKLSLLRSgKDEIIELANRKDQLLNSLGGGCRDIEVHTF- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      166 dtprGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGG-QVRLRILSNL-ADLRLARAQVRITPQQLETAEFSGEA 243
Cdd:cd00365 159 ----GPMLVAHLIVDVGDAMGANMINTMAEAVAPLMEAYTGGmQVRLRSLSNLtGDGRLARAQARITPQQLETAEFSGEA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      244 VIEGILDAYAF-AAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRsgHYGSLTTWEKDNNGHLVGTLEMP 322
Cdd:cd00365 235 VIEGILDAYAFkAAVDSYRAATHNKGIMNGVDPLIVACGQDWRAVEVGAHAYACR--HYGSLTTWEKDNNGHLVITLEMS 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1QAY_B      323 MPVGLVGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHA 386
Cdd:cd00365 313 MPVGLVGGATKTHPLAQASLRILGVKTAQALARIAVAVGLAQNLGAMRALATEGIQRGHMALHA 376
HMG-CoA_red pfam00368
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
14-386 3.49e-136

Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels.


Pssm-ID: 334039  Cd Length: 369  Bit Score: 394.87  E-value: 3.49e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         14 SPAARLDHIGQLLGlshDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAASYM 93
Cdd:pfam00368   1 AVEERREFLEELTG---EELEHLGDGSLDYSEVADANIENVIGYVQLPLGVAGPLLINGKDYYVPMATTEGSLVASASRG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         94 AKLARANGGFTTSSSA-PLMHAQVQIVG-IQDPLNARLSlLRRKDEIIELANRKDQllNSLGGGCRDIEVHTFadtprGP 171
Cdd:pfam00368  78 AKAITASGGFTTTVLGdGMTRGPVFLFPsVADAAEAKQW-IENKENLLEIANAAEP--TSRGGGLRDIEVYIA-----GR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        172 MLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQL-ETAE-FSGEAVIEGIL 249
Cdd:pfam00368 150 MLYLRFTVDTGDAMGANMVNKATEAAAPLIEEEFGGMVLLSILSNLCTDKKPSAINWIEGRGKsVVAEaTIPEEVVKKIL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        250 DAYAFAAVDPYRA---ATHNKGI-------MNGIDPLIVATGNDWRAVEAGAHAYAcrsghygSLTTWEkdnNGHLVGTL 319
Cdd:pfam00368 230 KASPEALVDPYRAkniGTHNKGIiggnahaANGIAAVFLATGQDPAAVEESSHAYA-------ALETWE---DGDLYGSV 299
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1QAY_B        320 EMP-MPVGLVGGATKTHPLAQLsLRILGVKTA---QALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHA 386
Cdd:pfam00368 300 TLPsLEVGTVGGGTGLPPQAEC-LKLLGVKGAgkpRELAEIIAAVGLAGELSALRALATGGIQKGHMKLGR 369
HMG_CoA_R_NAD TIGR00532
hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of ...
5-386 2.39e-133

hydroxymethylglutaryl-CoA reductase, degradative; Most known examples of hydroxymethylglutaryl-CoA reductase are NADP-dependent (EC 1.1.1.34) from eukaryotes and archaea, involved in the biosynthesis of mevalonate from 3-hydroxy-3-methylglutaryl-CoA. This model, in contrast, is built from the two examples in completed genomes of sequences closely related to the degradative, NAD-dependent hydroxymethylglutaryl-CoA reductase of Pseudomonas mevalonii, a bacterium that can use mevalonate as its sole carbon source. [Energy metabolism, Other]


Pssm-ID: 129623  Cd Length: 393  Bit Score: 388.62  E-value: 2.39e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B          5 SRLPAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGAlPMDIA-NGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEE 83
Cdd:TIGR00532  13 SKIFGFYHKSVEEKLKEIAEFAELSDEEVKAFFSNGA-NEDFAfDRMIENVIGTFEFPIGIAKNFKIDGKDYLIPIAIEE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         84 PSIVAAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHT 163
Cdd:TIGR00532  92 PSVVAAANFAAKIAEEADGFTSDGEGLGIIGQIQQIKIKNEKAAKFEFLDLGDEIIERAEECDPMLNNLGGGCKDIEARV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        164 FaDTPRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEA 243
Cdd:TIGR00532 172 I-DIIEGGILILHIIVDTCDAMGANALNSIAEKVAEFIELEFGGECVLKIISNDAAEFTAKARAKADFDHDLIGGEDSWN 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        244 VIEGILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDNNGHLVGTLEMPM 323
Cdd:TIGR00532 251 LAEGIELASAFAAADEERAATHNKGIMNGISALCIATFNDFRAIEAGAHKFAAIGGKYFPLSKFEVDRDGALVGEIEIPL 330
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
1QAY_B        324 PVGLVGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHA 386
Cdd:TIGR00532 331 AVGTIGGAIKFNEAAIISFKILGVNSAEEFAGIAAALGLAQNFAALRALAFEGIQKGHMELHA 393
HMG1 COG1257
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism];
12-426 2.48e-132

Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism];


Pssm-ID: 224177  Cd Length: 436  Bit Score: 387.46  E-value: 2.48e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       12 NLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAAS 91
Cdd:COG1257  23 NKAVEERRQALERFTGLSLEEIGSLSIDGSLPIDVANRNIENVIGTVQLPLGIAGPLLINGKEYYIPMATTEGALVASAS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       92 YMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDqllNSLGGGCRDIEVHTFadtPRGP 171
Cdd:COG1257 103 RGAKLITASGGATARVTEDGMTRQPVFRFVSLPEAAKFAIWVKKKEIIELAKEAA---PSTGRGGKLIHIEPF---VEGN 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      172 MLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAIT-GGQVRLRILSNLADLR--LARAQVRITPQQLETAEFSGEAVIEGI 248
Cdd:COG1257 177 LLYLRFYVDTGDAMGMNMVNIATEAVAPFIEEETfGGAVLLAISSNLCTDKkpAAINSIEGRGKTVVAEATIPEEVVKKI 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      249 LDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDNN-GHLVGTLEMPMPVGL 327
Cdd:COG1257 257 LKATPEAIVDVNRAKTLNGGAMNGIDGFNAHTANDVRAIEAATGQDAAQVGEYSPLITWMEDQRdGDLYGSVTLPSLVVG 336
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      328 VGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQL 407
Cdd:COG1257 337 TGGGGTVLPTQREALKILGVAGAGELAGVLAAVGLAQNAAALAALVAEGILAGEMSLLAALAAGHLGAAHDELGRVVERL 416
                       410
                ....*....|....*....
1QAY_B      408 VEYHDVRADRAVALLKQKR 426
Cdd:COG1257 417 IREKNINLEVAKKILEKLR 435
HMG-CoA_reductase_classI cd00643
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
45-384 5.75e-08

Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class I enzyme, homotetramer. Catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals this is the rate limiting committed step in cholesterol biosynthesis. Class I enzymes are found predominantly in eukaryotes and contain N-terminal membrane regions. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture.


Pssm-ID: 153081  Cd Length: 403  Bit Score: 54.10  E-value: 5.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B       45 DIANGMIENVIGTFELPYAVASNFQING----RDVLVPLVVEEPSIVAAASYMAKLARANGGFTTS------SSAPLMHA 114
Cdd:cd00643  55 EVLGRNIENVIGYVQVPVGVAGPLLINGeyagGEFYVPMATTEGALVASTNRGCKAINLSGGATTRvlgdgmTRAPVFRF 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      115 QvqivGIQDPLNARLSLLRRKDEIIELANrkdqllnSLGGGCRDIEVHTFADTPRgpmlvAHLIVDVR--DAMGANTVNT 192
Cdd:cd00643 135 P----SAREAAEFKAWIEENFEAIKEVAE-------STSRHARLQSIKPYIAGRS-----VYLRFEYTtgDAMGMNMVTK 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      193 MAEAVAPLMEAITGGQVRLRILSNL--------------------ADLRLARAQVR----ITPQQLETAEFSGEAVIEGI 248
Cdd:cd00643 199 ATEAACDWIEENFPDMEVISLSGNFctdkkpsainwiegrgksvvAEATIPREVVKevlkTTPEALVEVNIAKNLIGSAM 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B      249 LDAYAFAAvdpyRAAthnkgimNGIDPLIVATGNDWRAVEAGAHAyacrsghygsLTTWEKDNNGHLVGTLEMP-MPVGL 327
Cdd:cd00643 279 AGSGGFNA----HAA-------NIVAAIFIATGQDAAQVVESSNC----------ITTMELTADGDLYISVTMPsLEVGT 337
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1QAY_B      328 VGGATkTHPLAQLSLRILGVK--------TAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMAL 384
Cdd:cd00643 338 VGGGT-GLPTQRECLELLGCYgagdepgaNARKLAEIVAATVLAGELSLLAALAAGHLVRSHEKL 401
HMG_CoA_R_NADP TIGR00533
3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP); ...
51-384 9.45e-07

3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP); This model represents archaeal examples of the enzyme hydroxymethylglutaryl-CoA reductase (NADP) (EC 1.1.1.34) and the catalytic domain of eukaryotic examples, which also contain a hydrophobic N-terminal domain. This enzyme synthesizes mevalonate, a precursor of isopentenyl pyrophosphate (IPP), a building block for the synthesis of cholesterol, isoprenoids, and other molecules. A related hydroxymethylglutaryl-CoA reductase, typified by an example from Pseudomonas mevalonii, is NAD-dependent and catabolic. [Central intermediary metabolism, Other]


Pssm-ID: 129624  Cd Length: 402  Bit Score: 50.64  E-value: 9.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         51 IENVIGTFELPYAVASNFQINGRDVL----VPLVVEEPSIVAAASYMAKLARANGGFTTSSSAPLMHAQ--VQIVGIQDP 124
Cdd:TIGR00533  63 IENVIGYMQIPLGVAGPLKIDGEYAKgeyyIPLATTEGALVASVNRGCSAITAGGGATVRVTKDGMTRApvVRTPSVVRA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        125 LNARLSLLRRKDEIIELANRkdqllNSLGGGCRDIEVHTFAdtprGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAI 204
Cdd:TIGR00533 143 GACRIWIDENQNAIKEAAES-----TTRHGKLQKIQPICLA----GDLLYPRFVTTTGDAMGMNMVTIATEYALKQMVEE 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        205 TG--GQVRLRILSNL-ADLRLARAQVRITPQQLETAE-FSGEAVIEGILDAYAFAAVDPYRAATH-----------NKGI 269
Cdd:TIGR00533 214 YGweGMEVVAVSGNYcTDKKPAAINLIEGRGKSIVAEaTIPGDVVNKVLKTTVSALVEVNIAKNLigsamagsmgfNAHY 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        270 MNGIDPLIVATGNDwraveaGAHAYACRSGhygslTTWEKDNNGHLVGTLEMP-MPVGLVGGATKTHPLAQLsLRILGVK 348
Cdd:TIGR00533 294 ANIIGAIFLATGQD------EAHIVEGSLG-----ITLAEEVDGDLYFSVSLPdVPVGTVGGGTVLETQGEC-LDLLGVR 361
                         330       340       350
                  ....*....|....*....|....*....|....*....
1QAY_B        349 ---TAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMAL 384
Cdd:TIGR00533 362 ggnNARQFAEIVGCAVLAGELSLCGALAAGHLVQAHMEL 400
2A060605 TIGR00920
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, ...
52-387 1.04e-03

3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273339 [Multi-domain]  Cd Length: 886  Bit Score: 41.38  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B         52 ENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAASYMAKLARANGGfttsssaplMHAQVQIVGIQDPLNARLSL 131
Cdd:TIGR00920 525 ENVIGYMPIPVGVAGPLLLDGKEYQVPMATTEGCLVASTNRGCRALMLGGG---------VRSRVLADGMTRGPVVRLPS 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        132 LRRKDEI---IELANRKDQLLNSLGGGCRDIEVHTFADTPRGPMLVAHLIVDVRDAMGANTVNTMAE-AVAPLMEAITGG 207
Cdd:TIGR00920 596 ACRAAEAkawLEVPENFAVIKDAFDSTSRFARLKKIHIAMAGRNLYIRFQAKTGDAMGMNMISKGTEqALAELQEHFPDM 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        208 QVrLRILSNLADLRlaraqvriTPQQLETAEFSGEAVI-EGILDAYAFAAVDPYRAAT---------------------H 265
Cdd:TIGR00920 676 QI-LSLSGNYCTDK--------KPAAINWIEGRGKSVVcEATIPAKIVRSVLKTSAEAlvdvninknligsamagsiggF 746
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QAY_B        266 NKGIMNGIDPLIVATGNDwraveagaHAYACRSGHYGSLTTWEKDNNGHLVGTLEMP-MPVGLVGGATKTHPlAQLSLRI 344
Cdd:TIGR00920 747 NAHAANIVTAIYIATGQD--------AAQNVGSSNCMTLMEAWGPTGEDLYISCTMPsIEIGTVGGGTVLPP-QSACLQM 817
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
1QAY_B        345 LGVKTAQA---------LAEIAVAVGLAQNLGAMRALATEGIQRGHMaLHAR 387
Cdd:TIGR00920 818 LGVRGANAtrpgenakqLARIVCATVMAGELSLMAALAAGHLVKSHM-RHNR 868
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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