NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1036551446|ref|NP_957379|]
View 

hydroxymethylglutaryl-CoA synthase, cytoplasmic [Danio rerio]

Protein Classification

HMG-CoA-S_euk family protein (domain architecture ID 11493194)

HMG-CoA-S_euk family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
20-477 0e+00

3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes.


:

Pssm-ID: 273826 [Multi-domain]  Cd Length: 457  Bit Score: 901.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  20 WPKDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEV 99
Cdd:TIGR01833   1 WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNIDYDQIGRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 100 GTETIIDKSKSTKTVLMQLFEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDGRYALVVAGDIAVYATGSARPTG 179
Cdd:TIGR01833  81 GTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRYALVVAGDIAVYAKGNARPTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 180 GAGAVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIHARWQREGTEGR 259
Cdd:TIGR01833 161 GAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSIQCYLSALDRCYKSYCKKIEKQWGKSGSDRK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 CSLEDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSpNMESGPFSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKT 339
Cdd:TIGR01833 241 FTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPS-STDTSLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 340 KASLLISNQNGNMYTPSVYGCLASVLAQHTPQQLAGQRIGVFSYGSGFAATLYSIKVTQDGTPGSALDKLVSSLCDLPAR 419
Cdd:TIGR01833 320 KPSLLVPTQVGNMYTASLYGCLASLLSSKSAQELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNR 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1036551446 420 LDSRQKVSPGVFAETMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARR 477
Cdd:TIGR01833 400 LDSRHCVAPEEFEETMELREQAHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK 457
 
Name Accession Description Interval E-value
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
20-477 0e+00

3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes.


Pssm-ID: 273826 [Multi-domain]  Cd Length: 457  Bit Score: 901.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  20 WPKDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEV 99
Cdd:TIGR01833   1 WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNIDYDQIGRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 100 GTETIIDKSKSTKTVLMQLFEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDGRYALVVAGDIAVYATGSARPTG 179
Cdd:TIGR01833  81 GTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRYALVVAGDIAVYAKGNARPTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 180 GAGAVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIHARWQREGTEGR 259
Cdd:TIGR01833 161 GAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSIQCYLSALDRCYKSYCKKIEKQWGKSGSDRK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 CSLEDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSpNMESGPFSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKT 339
Cdd:TIGR01833 241 FTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPS-STDTSLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 340 KASLLISNQNGNMYTPSVYGCLASVLAQHTPQQLAGQRIGVFSYGSGFAATLYSIKVTQDGTPGSALDKLVSSLCDLPAR 419
Cdd:TIGR01833 320 KPSLLVPTQVGNMYTASLYGCLASLLSSKSAQELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNR 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1036551446 420 LDSRQKVSPGVFAETMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARR 477
Cdd:TIGR01833 400 LDSRHCVAPEEFEETMELREQAHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK 457
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
21-482 0e+00

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 633.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  21 PKDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEVG 100
Cdd:PLN02577    2 PKNVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKYNIDPKQIGRLEVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 101 TETIIDKSKSTKTVLMQLFEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDGRYALVVAGDIAVYATGSARPTGG 180
Cdd:PLN02577   82 SETVIDKSKSIKTFLMQLFEESGNTDIEGVDSTNACYGGTAALLNCVNWVESSSWDGRYGLVVAADSAVYAEGPARPTGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 181 AGAVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIharwqrEGTEGR- 259
Cdd:PLN02577  162 AGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLASEYPVVDGKLSQTCYLMALDSCYKRFCEKY------EKLEGKq 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 CSLEDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSPNMESGPfSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKT 339
Cdd:PLN02577  236 FSISDADYFVFHAPYNKLVQKSFARLVYNDFQRNASSVDEDAK-EKLAPFAGLSSDESYQNRDLEKVSQQVAKPLYDAKV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 340 KASLLISNQNGNMYTPSVYGCLASVLaQHTPQQLAGQRIGVFSYGSGFAATLYSIKVtQDGTPGSALDKLVSSLcDLPAR 419
Cdd:PLN02577  315 QPTTLIPKQVGNMYTASLYAALASLV-HNKHSELAGKRILMFSYGSGLTATMFSLRL-HEGQHPFSLSNIAKVM-DVSEK 391
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036551446 420 LDSRQKVSPGVFAETMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARRSMNDD 482
Cdd:PLN02577  392 LKSRHEVSPEKFVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYRRFYDRKALNGS 454
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
194-477 9.52e-154

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 439.99  E-value: 9.52e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 194 LAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIHARWQREGTEGrcSLEDFGFMVFHSP 273
Cdd:pfam08540   1 IVFDRGLRGSHMEHAYDFYKPDLTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRITKDGDKIF--GLNDFDYMIFHSP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 274 YCKLVQKSLARLMLNDFLCHPSPNMESGPFSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKTKASLLISNQNGNMY 353
Cdd:pfam08540  79 TCKLVQKSLARLLYNDFLSNPSSDKFNGVDEKLTAFGGLTLDESYTDKDLEKAFMKLSKPFFKKKVQPSLLVPTNNGNMY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 354 TPSVYGCLASVLAQHTPQQLAGQRIGVFSYGSGFAATLYSIKVTQDGTPGSALDklVSSLCDLPARLDSRQKVSPGVFAE 433
Cdd:pfam08540 159 TASLYAALASLLSHVSADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILD--IASVLDLGKRLDSRICVTPEEFTE 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1036551446 434 TMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARR 477
Cdd:pfam08540 237 AMELREQAHLKKNFKPQGSIDSLFPGTYYLTNVDDKFRRSYARK 280
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism];
24-474 1.53e-104

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism];


Pssm-ID: 225959 [Multi-domain]  Cd Length: 377  Bit Score: 318.09  E-value: 1.53e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  24 VGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEVGTET 103
Cdd:COG3425     3 IGIVGIGAYIPRYRIKLEELARAWGVDPEKIKKGLGVEEKSVPPWDEDAVTMAVEAARNALKRADIDPSKIGAVIVGSES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 104 IIDKSKSTKTVLMQLFEesGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDgrYALVVAGDIAVYATGSA-RPTGGAG 182
Cdd:COG3425    83 GPDAVKPTATIVAEALG--LNPSARAADVEFACYAGTAALQAAIGWVESGMIS--YGLVIGADTAQYAPGDAlEYTAGAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 183 AVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMvSEYPVVDGKLSIQCYLSALDQCYSVYKnkiharwQREGTegrcSL 262
Cdd:COG3425   159 AVAFLIGKNPPIVAEFEGTGSYTTDTPDFWRPDG-QPYPYVDGRFSEPAYFKHVENAAKGYM-------EKTGL----SP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 263 EDFGFMVFHSPYCKLVQKSLARLMLNdflchpspnmesgpfsgLEAFRDvkiedtyfdrdvekafmkasselfddktkaS 342
Cdd:COG3425   227 DDFDYIVFHQPNGKFPKKAAKSLGFK-----------------EEQVKP------------------------------G 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 343 LLISNQNGNMYTPSVYGCLASVLAQHTpqqLAGQRIGVFSYGSGFAATLYSIKVTQDGTpgSALDKLvsslcDLPARLDS 422
Cdd:COG3425   260 LVYPQRIGNTYTGSLLLGLASLLDNAK---LPGDRILLFSYGSGAGSEAFSITVTDGIE--ERRKKL-----APTVLLEQ 329
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036551446 423 RQKVSPGVFAETMKLREETHHLANYIPQGSvdelfpGTWYLTRVDEKHRRQY 474
Cdd:COG3425   330 RNRLSYIDYELYFKRRKKIRLGKDNEFYDS------GDYYLEEIDDHFRRYR 375
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
23-394 2.96e-94

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423  Cd Length: 324  Bit Score: 289.72  E-value: 2.96e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  23 DVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCsdREDINSLCLTVVQRLMERNGLSYESVGRLEVGTE 102
Cdd:cd00827     1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGD--DEDVPTMAVEAARRALERAGIDPDDIGLLIVATE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 103 TIIDKSKSTKTVLMQLFeesGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWdgRYALVVAGDIAVYAT---GSARPTG 179
Cdd:cd00827    79 SPIDKGKSAATYLAELL---GLTNAEAFDLKQACYGGTAALQLAANLVESGPW--RYALVVASDIASYLLdegSALEPTL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 180 GAGAVAMLVGPNAPLAFeRGLRGTHMQHAYDFYKpdmvSEYPVVDGKLSIQCYlsaldqcysvYKNKIHARWQREGtegr 259
Cdd:cd00827   154 GDGAAAMLVSRNPGILA-AGIVSTHSTSDPGYDF----SPYPVMDGGYPKPCK----------LAYAIRLTAEPAG---- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 csleDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSPNMESGPfsgleafrdvKIEDTYFDRdVEKAFMKASSELFDdkt 339
Cdd:cd00827   215 ----RAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGK----------KILEAVAKK-LGGPPEKASQTRWI--- 276
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1036551446 340 kasllISNQNGNMYTPSVYGCLASVLAQHTPQqlAGQRIGVFSYGSGFAATLYSI 394
Cdd:cd00827   277 -----LLRRVGNMYAASILLGLASLLESGKLK--AGDRVLLFSYGSGFTAEAFVL 324
 
Name Accession Description Interval E-value
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
20-477 0e+00

3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes.


Pssm-ID: 273826 [Multi-domain]  Cd Length: 457  Bit Score: 901.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  20 WPKDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEV 99
Cdd:TIGR01833   1 WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNIDYDQIGRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 100 GTETIIDKSKSTKTVLMQLFEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDGRYALVVAGDIAVYATGSARPTG 179
Cdd:TIGR01833  81 GTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRYALVVAGDIAVYAKGNARPTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 180 GAGAVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIHARWQREGTEGR 259
Cdd:TIGR01833 161 GAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSIQCYLSALDRCYKSYCKKIEKQWGKSGSDRK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 CSLEDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSpNMESGPFSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKT 339
Cdd:TIGR01833 241 FTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPS-STDTSLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 340 KASLLISNQNGNMYTPSVYGCLASVLAQHTPQQLAGQRIGVFSYGSGFAATLYSIKVTQDGTPGSALDKLVSSLCDLPAR 419
Cdd:TIGR01833 320 KPSLLVPTQVGNMYTASLYGCLASLLSSKSAQELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNR 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1036551446 420 LDSRQKVSPGVFAETMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARR 477
Cdd:TIGR01833 400 LDSRHCVAPEEFEETMELREQAHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK 457
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
21-482 0e+00

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 633.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  21 PKDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEVG 100
Cdd:PLN02577    2 PKNVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKYNIDPKQIGRLEVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 101 TETIIDKSKSTKTVLMQLFEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDGRYALVVAGDIAVYATGSARPTGG 180
Cdd:PLN02577   82 SETVIDKSKSIKTFLMQLFEESGNTDIEGVDSTNACYGGTAALLNCVNWVESSSWDGRYGLVVAADSAVYAEGPARPTGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 181 AGAVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIharwqrEGTEGR- 259
Cdd:PLN02577  162 AGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLASEYPVVDGKLSQTCYLMALDSCYKRFCEKY------EKLEGKq 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 CSLEDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSPNMESGPfSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKT 339
Cdd:PLN02577  236 FSISDADYFVFHAPYNKLVQKSFARLVYNDFQRNASSVDEDAK-EKLAPFAGLSSDESYQNRDLEKVSQQVAKPLYDAKV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 340 KASLLISNQNGNMYTPSVYGCLASVLaQHTPQQLAGQRIGVFSYGSGFAATLYSIKVtQDGTPGSALDKLVSSLcDLPAR 419
Cdd:PLN02577  315 QPTTLIPKQVGNMYTASLYAALASLV-HNKHSELAGKRILMFSYGSGLTATMFSLRL-HEGQHPFSLSNIAKVM-DVSEK 391
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036551446 420 LDSRQKVSPGVFAETMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARRSMNDD 482
Cdd:PLN02577  392 LKSRHEVSPEKFVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYRRFYDRKALNGS 454
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
194-477 9.52e-154

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 439.99  E-value: 9.52e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 194 LAFERGLRGTHMQHAYDFYKPDMVSEYPVVDGKLSIQCYLSALDQCYSVYKNKIHARWQREGTEGrcSLEDFGFMVFHSP 273
Cdd:pfam08540   1 IVFDRGLRGSHMEHAYDFYKPDLTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRITKDGDKIF--GLNDFDYMIFHSP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 274 YCKLVQKSLARLMLNDFLCHPSPNMESGPFSGLEAFRDVKIEDTYFDRDVEKAFMKASSELFDDKTKASLLISNQNGNMY 353
Cdd:pfam08540  79 TCKLVQKSLARLLYNDFLSNPSSDKFNGVDEKLTAFGGLTLDESYTDKDLEKAFMKLSKPFFKKKVQPSLLVPTNNGNMY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 354 TPSVYGCLASVLAQHTPQQLAGQRIGVFSYGSGFAATLYSIKVTQDGTPGSALDklVSSLCDLPARLDSRQKVSPGVFAE 433
Cdd:pfam08540 159 TASLYAALASLLSHVSADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILD--IASVLDLGKRLDSRICVTPEEFTE 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1036551446 434 TMKLREETHHLANYIPQGSVDELFPGTWYLTRVDEKHRRQYARR 477
Cdd:pfam08540 237 AMELREQAHLKKNFKPQGSIDSLFPGTYYLTNVDDKFRRSYARK 280
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
21-193 2.90e-120

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348  Cd Length: 173  Bit Score: 350.77  E-value: 2.90e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  21 PKDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEVG 100
Cdd:pfam01154   1 PKDVGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMERYNLPWDKIGRLEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 101 TETIIDKSKSTKTVLMQLFEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDGRYALVVAGDIAVYATGSARPTGG 180
Cdd:pfam01154  81 TETIIDKSKSVKSVLMQLFQESGNTDIEGIDTTNACYGGTAALFNAANWIESSSWDGRYALVVCGDIAIYPSGNARPTGG 160
                         170
                  ....*....|...
gi 1036551446 181 AGAVAMLVGPNAP 193
Cdd:pfam01154 161 AGAVAMLIGPKAP 173
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism];
24-474 1.53e-104

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism];


Pssm-ID: 225959 [Multi-domain]  Cd Length: 377  Bit Score: 318.09  E-value: 1.53e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  24 VGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEVGTET 103
Cdd:COG3425     3 IGIVGIGAYIPRYRIKLEELARAWGVDPEKIKKGLGVEEKSVPPWDEDAVTMAVEAARNALKRADIDPSKIGAVIVGSES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 104 IIDKSKSTKTVLMQLFEesGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWDgrYALVVAGDIAVYATGSA-RPTGGAG 182
Cdd:COG3425    83 GPDAVKPTATIVAEALG--LNPSARAADVEFACYAGTAALQAAIGWVESGMIS--YGLVIGADTAQYAPGDAlEYTAGAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 183 AVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMvSEYPVVDGKLSIQCYLSALDQCYSVYKnkiharwQREGTegrcSL 262
Cdd:COG3425   159 AVAFLIGKNPPIVAEFEGTGSYTTDTPDFWRPDG-QPYPYVDGRFSEPAYFKHVENAAKGYM-------EKTGL----SP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 263 EDFGFMVFHSPYCKLVQKSLARLMLNdflchpspnmesgpfsgLEAFRDvkiedtyfdrdvekafmkasselfddktkaS 342
Cdd:COG3425   227 DDFDYIVFHQPNGKFPKKAAKSLGFK-----------------EEQVKP------------------------------G 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 343 LLISNQNGNMYTPSVYGCLASVLAQHTpqqLAGQRIGVFSYGSGFAATLYSIKVTQDGTpgSALDKLvsslcDLPARLDS 422
Cdd:COG3425   260 LVYPQRIGNTYTGSLLLGLASLLDNAK---LPGDRILLFSYGSGAGSEAFSITVTDGIE--ERRKKL-----APTVLLEQ 329
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036551446 423 RQKVSPGVFAETMKLREETHHLANYIPQGSvdelfpGTWYLTRVDEKHRRQY 474
Cdd:COG3425   330 RNRLSYIDYELYFKRRKKIRLGKDNEFYDS------GDYYLEEIDDHFRRYR 375
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
23-394 2.96e-94

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423  Cd Length: 324  Bit Score: 289.72  E-value: 2.96e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  23 DVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCsdREDINSLCLTVVQRLMERNGLSYESVGRLEVGTE 102
Cdd:cd00827     1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGD--DEDVPTMAVEAARRALERAGIDPDDIGLLIVATE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 103 TIIDKSKSTKTVLMQLFeesGNTDVEGVDTTNACYGGTAALFNAVNWVESSSWdgRYALVVAGDIAVYAT---GSARPTG 179
Cdd:cd00827    79 SPIDKGKSAATYLAELL---GLTNAEAFDLKQACYGGTAALQLAANLVESGPW--RYALVVASDIASYLLdegSALEPTL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 180 GAGAVAMLVGPNAPLAFeRGLRGTHMQHAYDFYKpdmvSEYPVVDGKLSIQCYlsaldqcysvYKNKIHARWQREGtegr 259
Cdd:cd00827   154 GDGAAAMLVSRNPGILA-AGIVSTHSTSDPGYDF----SPYPVMDGGYPKPCK----------LAYAIRLTAEPAG---- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 260 csleDFGFMVFHSPYCKLVQKSLARLMLNDFLCHPSPNMESGPfsgleafrdvKIEDTYFDRdVEKAFMKASSELFDdkt 339
Cdd:cd00827   215 ----RAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGK----------KILEAVAKK-LGGPPEKASQTRWI--- 276
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1036551446 340 kasllISNQNGNMYTPSVYGCLASVLAQHTPQqlAGQRIGVFSYGSGFAATLYSI 394
Cdd:cd00827   277 -----LLRRVGNMYAASILLGLASLLESGKLK--AGDRVLLFSYGSGFTAEAFVL 324
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
24-441 1.26e-57

3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.


Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 196.12  E-value: 1.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  24 VGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSyeSVGRLEVGTET 103
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQ--KIDMVIFGTES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 104 IIDKSKSTKTVLMQLFEESGNTDVegVDTTNACYGGTAALFNAVNWVESSSwdGRYALVVAGDIAVYATGS-ARPTGGAG 182
Cdd:TIGR01835  79 GIDQSKAAAVYVHGLLGLQPFCRS--FELKQACYGATAALQMAKGHVALSP--DRKVLVIASDIAKYGLESpGEPTQGAG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 183 AVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDMvSEYPVVDGKLSIQCYLSALDQCYSVYKnkihARWQRegtegrcSL 262
Cdd:TIGR01835 155 AVAMLVSADPKLLAINEDSVLYTDDIMDFWRPNY-STTALVDGQYSNEQYLNAFENAWNDYA----KRTGL-------SL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 263 EDFGFMVFHSPYCKLVQKSLARLMlndflchpspnmesgpfsgleafrDVKIEDTyfDRDVEKAFMKasselfddktkaS 342
Cdd:TIGR01835 223 ADFAAFCFHVPFTKMGLKALRHIL------------------------KKNYEDE--DESVQNAYLE------------S 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 343 LLISNQNGNMYTPSVYGCLASVLAQhTPQQLAGQRIGVFSYGSGFAATLYSIKVTQdgtpgSALDKLvsSLCDLPARLDS 422
Cdd:TIGR01835 265 IIYNREVGNLYTGSLYLGLASLLEN-AFEDTTGDKIGLFSYGSGAVAEFFSGTLVA-----GYRDHL--KKERHLALLKN 336
                         410
                  ....*....|....*....
gi 1036551446 423 RQKVSpgvFAETMKLREET 441
Cdd:TIGR01835 337 RTNLS---YAEYEALFEET 352
PRK04262 PRK04262
hypothetical protein; Provisional
22-397 6.58e-09

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 57.61  E-value: 6.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  22 KDVGIIAMEVYVPSQYVDQAELEEYDGVGAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEVGT 101
Cdd:PRK04262    1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 102 ETIIDKSKSTKTVLMqlfEESGNT-DVEGVDTTNACYGGTAALFNAVNWVESSSwdGRYALVVAGDIAVYATGSA-RPTG 179
Cdd:PRK04262   81 ESHPYAVKPTATIVA---EALGATpDLTAADLEFACKAGTAALQAAMGLVKSGM--IKYALAIGADTAQGAPGDAlEYTA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 180 GAGAVAMLVGPNAPLA-FErglrgthmqHAY-------DFYKPDMvSEYPVVDGKLSiqcylsaLDQCYsvYKNKIHAR- 250
Cdd:PRK04262  156 AAGGAAFIIGKEEVIAeIE---------ATYsyttdtpDFWRREG-EPYPRHGGRFT-------GEPAY--FKHIISAAk 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 251 --WQREGTegrcSLEDFGFMVFHSPYCKLVQKsLARlMLNdflchpspnmesgpfsgleaFRDVKIEDTyfdrdvekafm 328
Cdd:PRK04262  217 glMEKLGL----KPSDYDYAVFHQPNGKFPLR-VAK-MLG--------------------FTKEQVKPG----------- 259
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036551446 329 kasselfddktkaslLISNQNGNMYTPSVYGCLASVLAQHTPqqlaGQRIGVFSYGSGFAATLYSIKVT 397
Cdd:PRK04262  260 ---------------LLTPYIGNTYSGSALLGLAAVLDVAKP----GDRILVVSFGSGAGSDAFSITVT 309
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
24-205 5.05e-05

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426  Cd Length: 320  Bit Score: 45.22  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446  24 VGIIAMEVYVPSQYVDQAELEEY----DGVGAGKytVGLGQARmgFCSDREDINSLCLTVVQRLMERNGLSYESVGRLEV 99
Cdd:cd00830     2 ARILGIGSYLPERVVTNDELEKRldtsDEWIRTR--TGIRERR--IADPGETTSDLAVEAAKKALEDAGIDADDIDLIIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036551446 100 GTETIIDKSKSTKTVLmQlfEESGNTDVEGVDTTNACYGGTAALFNAVNWVESSSwdGRYALVVAGDIAV----YATGSA 175
Cdd:cd00830    78 ATSTPDYLFPATACLV-Q--ARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGG--AKNVLVVGAETLSrildWTDRST 152
                         170       180       190
                  ....*....|....*....|....*....|
gi 1036551446 176 RPTGGAGAVAMLVGPNAPlafERGLRGTHM 205
Cdd:cd00830   153 AVLFGDGAGAVVLEATEE---DPGILDSVL 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH