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Conserved domains on  [gi|564337997|ref|XP_006233064|]
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hydroxymethylglutaryl-CoA synthase, mitochondrial isoform X1 [Rattus norvegicus]

Protein Classification

hydroxymethylglutaryl-CoA synthase family protein( domain architecture ID 11493194)

hydroxymethylglutaryl-CoA (HMG-CoA) synthase family protein such as HMG-CoA synthase that condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase

Graphical summary

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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 ...
50-506 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: 887.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997   50 WPKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEV 129
Cdd:TIGR01833   1 WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNIDYDQIGRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  130 GTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTG 209
Cdd:TIGR01833  81 GTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRYALVVAGDIAVYAKGNARPTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  210 GAGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQNQWKQAGNNQP 289
Cdd:TIGR01833 161 GAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSIQCYLSALDRCYKSYCKKIEKQWGKSGSDRK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  290 FTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTK 369
Cdd:TIGR01833 241 FTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPSSTDTSLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKTK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  370 ASLYLSTNNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEKLVSSVSDLPKRL 449
Cdd:TIGR01833 321 PSLLVPTQVGNMYTASLYGCLASLLSSKSAQELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNRL 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564337997  450 DSRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARR 506
Cdd:TIGR01833 401 DSRHCVAPEEFEETMELREQAHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK 457
 
Name Accession Description Interval E-value
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
50-506 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: 887.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997   50 WPKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEV 129
Cdd:TIGR01833   1 WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNIDYDQIGRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  130 GTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTG 209
Cdd:TIGR01833  81 GTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRYALVVAGDIAVYAKGNARPTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  210 GAGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQNQWKQAGNNQP 289
Cdd:TIGR01833 161 GAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSIQCYLSALDRCYKSYCKKIEKQWGKSGSDRK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  290 FTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTK 369
Cdd:TIGR01833 241 FTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPSSTDTSLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKTK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  370 ASLYLSTNNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEKLVSSVSDLPKRL 449
Cdd:TIGR01833 321 PSLLVPTQVGNMYTASLYGCLASLLSSKSAQELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNRL 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564337997  450 DSRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARR 506
Cdd:TIGR01833 401 DSRHCVAPEEFEETMELREQAHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK 457
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
51-508 0e+00

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 612.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  51 PKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVG 130
Cdd:PLN02577   2 PKNVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKYNIDPKQIGRLEVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 131 TETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTGG 210
Cdd:PLN02577  82 SETVIDKSKSIKTFLMQLFEESGNTDIEGVDSTNACYGGTAALLNCVNWVESSSWDGRYGLVVAADSAVYAEGPARPTGG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 211 AGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQnqwKQAGnnQPF 290
Cdd:PLN02577 162 AGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLASEYPVVDGKLSQTCYLMALDSCYKRFCEKYE---KLEG--KQF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 291 TLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTKA 370
Cdd:PLN02577 237 SISDADYFVFHAPYNKLVQKSFARLVYNDFQRNASSVDEDAKEKLAPFAGLSSDESYQNRDLEKVSQQVAKPLYDAKVQP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 371 SLYLSTNNGNMYTSSLYGCLASLLsHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEklVSSVSDLPKRLD 450
Cdd:PLN02577 317 TTLIPKQVGNMYTASLYAALASLV-HNKHSELAGKRILMFSYGSGLTATMFSLRLHEGQHPFSLSN--IAKVMDVSEKLK 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564337997 451 SRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARRPV 508
Cdd:PLN02577 394 SRHEVSPEKFVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYRRFYDRKAL 451
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
224-506 1.35e-162

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 461.94  E-value: 1.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  224 LVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQNQWKQAGnnQPFTLDDVQYMIFHTP 303
Cdd:pfam08540   1 IVFDRGLRGSHMEHAYDFYKPDLTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRITKDGD--KIFGLNDFDYMIFHSP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  304 FCKMVQKSLARLMFNDFLSS-SSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTKASLYLSTNNGNMY 382
Cdd:pfam08540  79 TCKLVQKSLARLLYNDFLSNpSSDKFNGVDEKLTAFGGLTLDESYTDKDLEKAFMKLSKPFFKKKVQPSLLVPTNNGNMY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  383 TSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEklVSSVSDLPKRLDSRRRMSPEEFTE 462
Cdd:pfam08540 159 TASLYAALASLLSHVSADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILD--IASVLDLGKRLDSRICVTPEEFTE 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 564337997  463 IMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARR 506
Cdd:pfam08540 237 AMELREQAHLKKNFKPQGSIDSLFPGTYYLTNVDDKFRRSYARK 280
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
54-504 7.01e-93

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442651 [Multi-domain]  Cd Length: 382  Bit Score: 287.85  E-value: 7.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  54 VGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTET 133
Cdd:COG3425    3 VGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTES 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 134 IIDKSKAVKTVLMELFQDSGNTDieGIDTTNACYGGTASLFNAANWMESSywDGRYALVVCGDIAVYPSGNA-RPTGGAG 212
Cdd:COG3425   83 GPDASKPIATYVHGALGLPPNCR--AFELKFACYAGTAALQAALGWVASG--PNKKALVIASDIARYGPGSAgEYTQGAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 213 AVAMLIGPKaPLVLE-QGLRGTHMENAYDFYKPNlASEYPLVDGKLSIQCYLRALDRCYAAYRRKiqnqwkqAGNnqpfT 291
Cdd:COG3425  159 AVAMLVGAD-PRIAEiEGGSGSYTTDVMDFWRPN-GSDYPLVDGRFSEPAYLDHLEEAVKDYKEK-------TGL----K 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 292 LDDVQYMIFHTPFCKMVQKSLARLMFNDflssssdkqnnlykgleafkglkleetytnkdvdkalLKASLDMFNKKTKAS 371
Cdd:COG3425  226 PDDFDYFVFHQPFGKMPKKAAKKLGRKA-------------------------------------GREIQEDFEEQVEPS 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 372 LYLSTNNGNMYTSSLYGCLASLLSHhsAQELAGSRIGAFSYGSGLAASFFSFRVSKDAspgsplEKLVSSVsDLPKRLDS 451
Cdd:COG3425  269 LIYSRRIGNTYTGSLYLGLASLLDN--AKDLPGDRIGLFSYGSGAGSEFFSGTVTPGI------EERLRRP-GVEEQLAN 339
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564337997 452 RRRMSPEEFTEIMNQREqfyhkvnfsPPGDTSNLFPGTWYLERVdEMHRRKYA 504
Cdd:COG3425  340 RRYLSYAEYEKLRGKIL---------PEDAEDVTLPGEFVLTGI-KDHERIYE 382
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
53-423 5.69e-88

"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 [Multi-domain]  Cd Length: 324  Bit Score: 273.15  E-value: 5.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  53 DVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCsvQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTE 132
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGD--DEDVPTMAVEAARRALERAGIDPDDIGLLIVATE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 133 TIIDKSKAVKTVLMELFqdsGNTDIEGIDTTNACYGGTASLFNAANWMESSYWdgRYALVVCGDIAVYP---SGNARPTG 209
Cdd:cd00827   79 SPIDKGKSAATYLAELL---GLTNAEAFDLKQACYGGTAALQLAANLVESGPW--RYALVVASDIASYLldeGSALEPTL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 210 GAGAVAMLIGPKAPlVLEQGLRGTHMENAYDFYKpnlaSEYPLVDGKLSIQCYLRALDRCYAAYRRKIqnqwkqagnnqp 289
Cdd:cd00827  154 GDGAAAMLVSRNPG-ILAAGIVSTHSTSDPGYDF----SPYPVMDGGYPKPCKLAYAIRLTAEPAGRA------------ 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 290 ftlddvQYMIFHTPFCKMVQKSLARLMfndflsssSDKQNNLYKGLEAFKGLKLEETYtnKDVDKALLKASLDMFnkktk 369
Cdd:cd00827  217 ------VFEAAHKLIAKVVRKALDRAG--------LSEDIDYFVPHQPNGKKILEAVA--KKLGGPPEKASQTRW----- 275
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564337997 370 aslYLSTNNGNMYTSSLYGCLASLLshHSAQELAGSRIGAFSYGSGLAASFFSF 423
Cdd:cd00827  276 ---ILLRRVGNMYAASILLGLASLL--ESGKLKAGDRVLLFSYGSGFTAEAFVL 324
 
Name Accession Description Interval E-value
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
50-506 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: 887.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997   50 WPKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEV 129
Cdd:TIGR01833   1 WPKDVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYNIDYDQIGRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  130 GTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTG 209
Cdd:TIGR01833  81 GTETIIDKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWDGRYALVVAGDIAVYAKGNARPTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  210 GAGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQNQWKQAGNNQP 289
Cdd:TIGR01833 161 GAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDLASEYPVVDGKLSIQCYLSALDRCYKSYCKKIEKQWGKSGSDRK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  290 FTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTK 369
Cdd:TIGR01833 241 FTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPSSTDTSLYEGLEALSGLKLEDTYTDRDLEKAFMKASKELFDKKTK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  370 ASLYLSTNNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEKLVSSVSDLPKRL 449
Cdd:TIGR01833 321 PSLLVPTQVGNMYTASLYGCLASLLSSKSAQELAGKRVGMFSYGSGLAASMFSLRVSQDASPGSALDKLIASLSDLKNRL 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564337997  450 DSRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARR 506
Cdd:TIGR01833 401 DSRHCVAPEEFEETMELREQAHHKKNFTPQGSIDSLFPGTWYLERVDSKHRRSYARK 457
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
51-508 0e+00

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 612.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  51 PKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVG 130
Cdd:PLN02577   2 PKNVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKYNIDPKQIGRLEVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 131 TETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTGG 210
Cdd:PLN02577  82 SETVIDKSKSIKTFLMQLFEESGNTDIEGVDSTNACYGGTAALLNCVNWVESSSWDGRYGLVVAADSAVYAEGPARPTGG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 211 AGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQnqwKQAGnnQPF 290
Cdd:PLN02577 162 AGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLASEYPVVDGKLSQTCYLMALDSCYKRFCEKYE---KLEG--KQF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 291 TLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTKA 370
Cdd:PLN02577 237 SISDADYFVFHAPYNKLVQKSFARLVYNDFQRNASSVDEDAKEKLAPFAGLSSDESYQNRDLEKVSQQVAKPLYDAKVQP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 371 SLYLSTNNGNMYTSSLYGCLASLLsHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEklVSSVSDLPKRLD 450
Cdd:PLN02577 317 TTLIPKQVGNMYTASLYAALASLV-HNKHSELAGKRILMFSYGSGLTATMFSLRLHEGQHPFSLSN--IAKVMDVSEKLK 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564337997 451 SRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARRPV 508
Cdd:PLN02577 394 SRHEVSPEKFVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYRRFYDRKAL 451
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
224-506 1.35e-162

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 461.94  E-value: 1.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  224 LVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQNQWKQAGnnQPFTLDDVQYMIFHTP 303
Cdd:pfam08540   1 IVFDRGLRGSHMEHAYDFYKPDLTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRITKDGD--KIFGLNDFDYMIFHSP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  304 FCKMVQKSLARLMFNDFLSS-SSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTKASLYLSTNNGNMY 382
Cdd:pfam08540  79 TCKLVQKSLARLLYNDFLSNpSSDKFNGVDEKLTAFGGLTLDESYTDKDLEKAFMKLSKPFFKKKVQPSLLVPTNNGNMY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  383 TSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEklVSSVSDLPKRLDSRRRMSPEEFTE 462
Cdd:pfam08540 159 TASLYAALASLLSHVSADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILD--IASVLDLGKRLDSRICVTPEEFTE 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 564337997  463 IMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARR 506
Cdd:pfam08540 237 AMELREQAHLKKNFKPQGSIDSLFPGTYYLTNVDDKFRRSYARK 280
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
51-223 3.91e-126

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 365.02  E-value: 3.91e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997   51 PKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVG 130
Cdd:pfam01154   1 PKDVGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMERYNLPWDKIGRLEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  131 TETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTGG 210
Cdd:pfam01154  81 TETIIDKSKSVKSVLMQLFQESGNTDIEGIDTTNACYGGTAALFNAANWIESSSWDGRYALVVCGDIAIYPSGNARPTGG 160
                         170
                  ....*....|...
gi 564337997  211 AGAVAMLIGPKAP 223
Cdd:pfam01154 161 AGAVAMLIGPKAP 173
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
54-504 7.01e-93

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442651 [Multi-domain]  Cd Length: 382  Bit Score: 287.85  E-value: 7.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  54 VGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTET 133
Cdd:COG3425    3 VGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTES 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 134 IIDKSKAVKTVLMELFQDSGNTDieGIDTTNACYGGTASLFNAANWMESSywDGRYALVVCGDIAVYPSGNA-RPTGGAG 212
Cdd:COG3425   83 GPDASKPIATYVHGALGLPPNCR--AFELKFACYAGTAALQAALGWVASG--PNKKALVIASDIARYGPGSAgEYTQGAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 213 AVAMLIGPKaPLVLE-QGLRGTHMENAYDFYKPNlASEYPLVDGKLSIQCYLRALDRCYAAYRRKiqnqwkqAGNnqpfT 291
Cdd:COG3425  159 AVAMLVGAD-PRIAEiEGGSGSYTTDVMDFWRPN-GSDYPLVDGRFSEPAYLDHLEEAVKDYKEK-------TGL----K 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 292 LDDVQYMIFHTPFCKMVQKSLARLMFNDflssssdkqnnlykgleafkglkleetytnkdvdkalLKASLDMFNKKTKAS 371
Cdd:COG3425  226 PDDFDYFVFHQPFGKMPKKAAKKLGRKA-------------------------------------GREIQEDFEEQVEPS 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 372 LYLSTNNGNMYTSSLYGCLASLLSHhsAQELAGSRIGAFSYGSGLAASFFSFRVSKDAspgsplEKLVSSVsDLPKRLDS 451
Cdd:COG3425  269 LIYSRRIGNTYTGSLYLGLASLLDN--AKDLPGDRIGLFSYGSGAGSEFFSGTVTPGI------EERLRRP-GVEEQLAN 339
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564337997 452 RRRMSPEEFTEIMNQREqfyhkvnfsPPGDTSNLFPGTWYLERVdEMHRRKYA 504
Cdd:COG3425  340 RRYLSYAEYEKLRGKIL---------PEDAEDVTLPGEFVLTGI-KDHERIYE 382
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
53-423 5.69e-88

"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 [Multi-domain]  Cd Length: 324  Bit Score: 273.15  E-value: 5.69e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  53 DVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCsvQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTE 132
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGD--DEDVPTMAVEAARRALERAGIDPDDIGLLIVATE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 133 TIIDKSKAVKTVLMELFqdsGNTDIEGIDTTNACYGGTASLFNAANWMESSYWdgRYALVVCGDIAVYP---SGNARPTG 209
Cdd:cd00827   79 SPIDKGKSAATYLAELL---GLTNAEAFDLKQACYGGTAALQLAANLVESGPW--RYALVVASDIASYLldeGSALEPTL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 210 GAGAVAMLIGPKAPlVLEQGLRGTHMENAYDFYKpnlaSEYPLVDGKLSIQCYLRALDRCYAAYRRKIqnqwkqagnnqp 289
Cdd:cd00827  154 GDGAAAMLVSRNPG-ILAAGIVSTHSTSDPGYDF----SPYPVMDGGYPKPCKLAYAIRLTAEPAGRA------------ 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 290 ftlddvQYMIFHTPFCKMVQKSLARLMfndflsssSDKQNNLYKGLEAFKGLKLEETYtnKDVDKALLKASLDMFnkktk 369
Cdd:cd00827  217 ------VFEAAHKLIAKVVRKALDRAG--------LSEDIDYFVPHQPNGKKILEAVA--KKLGGPPEKASQTRW----- 275
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564337997 370 aslYLSTNNGNMYTSSLYGCLASLLshHSAQELAGSRIGAFSYGSGLAASFFSF 423
Cdd:cd00827  276 ---ILLRRVGNMYAASILLGLASLL--ESGKLKAGDRVLLFSYGSGFTAEAFVL 324
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
54-427 1.33e-55

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: 190.34  E-value: 1.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997   54 VGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLpwDAVGRLEVGTET 133
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDK--QKIDMVIFGTES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  134 IIDKSKAVKTVLMELFQDSGNTdiEGIDTTNACYGGTASLFNAANWMESSywDGRYALVVCGDIAVYpsGN---ARPTGG 210
Cdd:TIGR01835  79 GIDQSKAAAVYVHGLLGLQPFC--RSFELKQACYGATAALQMAKGHVALS--PDRKVLVIASDIAKY--GLespGEPTQG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  211 AGAVAMLIGpKAPLVLEQGL-RGTHMENAYDFYKPNlASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQnqwkqagnnqp 289
Cdd:TIGR01835 153 AGAVAMLVS-ADPKLLAINEdSVLYTDDIMDFWRPN-YSTTALVDGQYSNEQYLNAFENAWNDYAKRTG----------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  290 FTLDDVQYMIFHTPFCKMVQKSLARLMfndflssssDKQNnlykgleafkglkleetytnKDVDKALLKASLDmfnkktk 369
Cdd:TIGR01835 220 LSLADFAAFCFHVPFTKMGLKALRHIL---------KKNY--------------------EDEDESVQNAYLE------- 263
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564337997  370 aSLYLSTNNGNMYTSSLYGCLASLLSHhSAQELAGSRIGAFSYGSGLAASFFSFRVSK 427
Cdd:TIGR01835 264 -SIIYNREVGNLYTGSLYLGLASLLEN-AFEDTTGDKIGLFSYGSGAVAEFFSGTLVA 319
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
54-301 4.78e-07

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 51.65  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997  54 VGILALEVYFPAQYVDQTDLEKFNNVEAGKYtvglgQTRMG-----FCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLE 128
Cdd:COG0332    3 VRILGTGSYLPERVVTNDDLEKRLDTSDEWI-----EERTGirerrIAAPDETTSDLAVEAARKALEAAGIDPEDIDLII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 129 VGTETIiDK---SKAVKtVLMELfqdsGNTDIEGIDTTNACYGGTASLFNAANWMESSywDGRYALVVCGDIAV----YP 201
Cdd:COG0332   78 VATVTP-DYlfpSTACL-VQHKL----GAKNAAAFDINAACSGFVYALSVAAALIRSG--QAKNVLVVGAETLSrivdWT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337997 202 SGNARPTGGAGAVAMLIGPKAPlvlEQGLRGTHMENAYDFYK----PNLASEYPLVDGKLSIQcYLR---------ALDR 268
Cdd:COG0332  150 DRSTCVLFGDGAGAVVLEASEE---GPGILGSVLGSDGSGADllvvPAGGSRNPPSPVDEGDH-YLRmdgrevfkfAVRN 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564337997 269 CYAAYRRKIQnqwkQAGnnqpFTLDDVQYMIFH 301
Cdd:COG0332  226 LPEVIREALE----KAG----LTLDDIDWFIPH 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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