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Conserved domains on  [gi|1001822246|emb|CZQ50701|]
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ketosynthase, partial [Serratia sp. 1A-1]

Protein Classification

polyketide synthase( domain architecture ID 10093619)

polyketide synthase assembles complex polyketides via the head-to-tail fusion of acyl and malonyl building blocks; similar to Anser anser anser fatty acid synthase

CATH:  3.10.129.110|3.30.70.3290|3.40.47.10
Gene Ontology:  GO:0006633
SCOP:  4000245

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 4-228 6.81e-120

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


:

Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 347.24  E-value: 6.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSH-RFRHADDIDLYTAAGNAPSVLAGRVSHALGLSGP 82
Cdd:cd00833    83 AMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLElLARDPDEIDAYAATGTSRAFLANRISYFFDLRGP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  83 TLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVL 162
Cdd:cd00833   163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVL 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001822246 163 QRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:cd00833   243 KRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 4-228 6.81e-120

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 347.24  E-value: 6.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSH-RFRHADDIDLYTAAGNAPSVLAGRVSHALGLSGP 82
Cdd:cd00833    83 AMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLElLARDPDEIDAYAATGTSRAFLANRISYFFDLRGP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  83 TLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVL 162
Cdd:cd00833   163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVL 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001822246 163 QRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:cd00833   243 KRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 4-228 1.21e-109

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 343.01  E-value: 1.21e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246    4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSHR-FRHADDIDLYTAAGNAPSVLAGRVSHALGLSGP 82
Cdd:COG3321     87 AMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLlLADPEAIDAYALTGNAKSVLAGRISYKLDLRGP 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   83 TLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVL 162
Cdd:COG3321    167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVL 246

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001822246  163 QRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:COG3321    247 KRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTG 312
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 4-201 1.67e-95

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 280.75  E-value: 1.67e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246    4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYShrfrhaddidlytaagnapsvlagrvshalglsgpt 83
Cdd:smart00825  47 AMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDYS------------------------------------ 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   84 LTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVLQ 163
Cdd:smart00825  91 VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLK 170

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1001822246  164 RLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQ 201
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ 208
mycolic_Pks13 NF040607
polyketide synthase Pks13;
3-228 3.20e-82

polyketide synthase Pks13;


Pssm-ID: 468580 [Multi-domain]  Cd Length: 1671  Bit Score: 267.17  E-value: 3.20e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246    3 DAMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYShrFRHADDIDL---YTAAGNAPSVLAGRVSHALGL 79
Cdd:NF040607   182 ENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDYQ--MLAVADPAEahpYALTGTSSSIIANRVSYFFDF 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   80 SGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAA-ECRAHMLSPSGRCRTFDNNADGFVRGEGCG 158
Cdd:NF040607   260 RGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGfDELGGVLAPDGRIKAFSSDADGMVRSEGGG 339

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  159 VVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:NF040607   340 VVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTG 409
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-168 1.80e-70

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 215.58  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   1 QQDAMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSH---RFRHADDIDLYTAA-GNAPSVLAGRVSHA 76
Cdd:pfam00109  80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAAlllLDEDGGPRRGSPFAvGTMPSVIAGRISYF 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEG 156
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239

                         170
                  ....*....|..
gi 1001822246 157 CGVVVLQRLSDA 168
Cdd:pfam00109 240 VGAVVLKRLSDA 251
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
66-227 3.57e-25

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 101.79  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  66 PSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGR 140
Cdd:PRK07314  138 INMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStrnddPERA 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 141 CRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAG----------SAVNHDGRSAGltvpnqRAqselVQAACR 210
Cdd:PRK07314  218 SRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGygmtgdayhmTAPAPDGEGAA------RA----MKLALK 287

                         170
                  ....*....|....*..
gi 1001822246 211 AARIEPDEVQFIEAHGT 227
Cdd:PRK07314  288 DAGINPEDIDYINAHGT 304
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 63-228 3.46e-24

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 100.47  E-value: 3.46e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   63 GNAPSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCR 142
Cdd:TIGR02813  179 GSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDIQ 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  143 TFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFI 222
Cdd:TIGR02813  259 PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLI 338


                   ....*.
gi 1001822246  223 EAHGTG 228
Cdd:TIGR02813  339 EAHGTG 344
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 4-228 6.81e-120

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 347.24  E-value: 6.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSH-RFRHADDIDLYTAAGNAPSVLAGRVSHALGLSGP 82
Cdd:cd00833    83 AMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLElLARDPDEIDAYAATGTSRAFLANRISYFFDLRGP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  83 TLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVL 162
Cdd:cd00833   163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVL 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001822246 163 QRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:cd00833   243 KRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 4-228 1.21e-109

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 343.01  E-value: 1.21e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246    4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSHR-FRHADDIDLYTAAGNAPSVLAGRVSHALGLSGP 82
Cdd:COG3321     87 AMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLlLADPEAIDAYALTGNAKSVLAGRISYKLDLRGP 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   83 TLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVL 162
Cdd:COG3321    167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVL 246

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001822246  163 QRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:COG3321    247 KRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTG 312
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 4-201 1.67e-95

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 280.75  E-value: 1.67e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246    4 AMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYShrfrhaddidlytaagnapsvlagrvshalglsgpt 83
Cdd:smart00825  47 AMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDYS------------------------------------ 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   84 LTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVLQ 163
Cdd:smart00825  91 VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLK 170

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1001822246  164 RLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQ 201
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ 208
mycolic_Pks13 NF040607
polyketide synthase Pks13;
3-228 3.20e-82

polyketide synthase Pks13;


Pssm-ID: 468580 [Multi-domain]  Cd Length: 1671  Bit Score: 267.17  E-value: 3.20e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246    3 DAMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYShrFRHADDIDL---YTAAGNAPSVLAGRVSHALGL 79
Cdd:NF040607   182 ENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDYQ--MLAVADPAEahpYALTGTSSSIIANRVSYFFDF 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   80 SGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAA-ECRAHMLSPSGRCRTFDNNADGFVRGEGCG 158
Cdd:NF040607   260 RGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGfDELGGVLAPDGRIKAFSSDADGMVRSEGGG 339

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  159 VVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:NF040607   340 VVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTG 409
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-168 1.80e-70

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 215.58  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   1 QQDAMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSH---RFRHADDIDLYTAA-GNAPSVLAGRVSHA 76
Cdd:pfam00109  80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAAlllLDEDGGPRRGSPFAvGTMPSVIAGRISYF 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEG 156
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239

                         170
                  ....*....|..
gi 1001822246 157 CGVVVLQRLSDA 168
Cdd:pfam00109 240 VGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 8-228 1.53e-42

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 146.63  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   8 QQRILLEVAWEAIERASLPASTLTSKATGMFVGVMHQDYSHRFRHADD---IDLYTAAGNAPSVLAGRVSHALGLSGPTL 84
Cdd:cd00825    11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAmraVGPYVVTKAMFPGASGQIATPLGIHGPAY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  85 TVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCRTFDNNADGFVRGEGCGVVVLQR 164
Cdd:cd00825    91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001822246 165 LSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:cd00825   171 LEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTG 234
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 5-228 5.59e-39

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 138.69  E-value: 5.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   5 MDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGV------MHQDYSHRFRH--ADDIDLYTAAGNAPSVLAGRVSHA 76
Cdd:COG0304    68 MDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGSgiggldTLEEAYRALLEkgPRRVSPFFVPMMMPNMAAGHVSIR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGRCRTFDNNADGF 151
Cdd:COG0304   148 FGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddPEKASRPFDKDRDGF 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001822246 152 VRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:COG0304   228 VLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTS 304
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 1-228 9.24e-38

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 135.74  E-value: 9.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   1 QQDAMDPQQRILLEVAWEAIERASLPASTLTSKATGMFVGV------MHQDYSHRFRHADDIDL--YTAAGNAPSVLAGR 72
Cdd:cd00834    64 ELRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGSgigglaTIEEAYRALLEKGPRRVspFFVPMALPNMAAGQ 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  73 VSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGRCRTFDNN 147
Cdd:cd00834   144 VAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALStrnddPEKASRPFDKD 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 148 ADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGT 227
Cdd:cd00834   224 RDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGT 303


                  .
gi 1001822246 228 G 228
Cdd:cd00834   304 S 304
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 5-228 6.31e-29

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 112.15  E-value: 6.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   5 MDPQQRILLEVAWEAIERASL-------PASTLTSKATGMFVGVMHQDYSHRFRHADDIDLYTAAGNAPSVLAGRVS-HA 76
Cdd:cd00828    69 VDRTTLLALVATEEALADAGItdpyevhPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSPNTVAGWVNiLL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNA-VLSPLSTAAECRA---HMLSPSGRCRTFDNNADGFV 152
Cdd:cd00828   149 LSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDpLEEGLSGFANMGAlstAEEEPEEMSRPFDETRDGFV 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001822246 153 RGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPnQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:cd00828   229 EAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTS 303
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
66-227 3.57e-25

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 101.79  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  66 PSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGR 140
Cdd:PRK07314  138 INMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStrnddPERA 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 141 CRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAG----------SAVNHDGRSAGltvpnqRAqselVQAACR 210
Cdd:PRK07314  218 SRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGygmtgdayhmTAPAPDGEGAA------RA----MKLALK 287

                         170
                  ....*....|....*..
gi 1001822246 211 AARIEPDEVQFIEAHGT 227
Cdd:PRK07314  288 DAGINPEDIDYINAHGT 304
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
65-227 1.95e-24

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 99.69  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  65 APSVL----AGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS---- 136
Cdd:PRK06333  144 IPSFLtnmaAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALStrfn 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 137 --PSGRCRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHD------GRSAGLTVpnQRAqselVQAA 208
Cdd:PRK06333  224 daPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADayhmtaGPEDGEGA--RRA----MLIA 297

                         170
                  ....*....|....*....
gi 1001822246 209 CRAARIEPDEVQFIEAHGT 227
Cdd:PRK06333  298 LRQAGIPPEEVQHLNAHAT 316
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 63-228 3.46e-24

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 100.47  E-value: 3.46e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   63 GNAPSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGRCR 142
Cdd:TIGR02813  179 GSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDIQ 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  143 TFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFI 222
Cdd:TIGR02813  259 PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLI 338


                   ....*.
gi 1001822246  223 EAHGTG 228
Cdd:TIGR02813  339 EAHGTG 344
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 69-228 9.36e-24

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 97.79  E-value: 9.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  69 LAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLstaaECRA-----HMLS------P 137
Cdd:PRK07103  146 LVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYW----ECQAlrslgAMGSdrfadeP 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 138 SGRCRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSagLTVPNQRAQSELVQAACRAARIEPD 217
Cdd:PRK07103  222 EAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPE 299

                         170
                  ....*....|.
gi 1001822246 218 EVQFIEAHGTG 228
Cdd:PRK07103  300 DIDYVNPHGTG 310
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 66-227 6.76e-20

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 87.15  E-value: 6.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  66 PSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS------PSG 139
Cdd:PLN02836  160 INMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStkfnscPTE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 140 RCRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEV 219
Cdd:PLN02836  240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQV 319


                  ....*...
gi 1001822246 220 QFIEAHGT 227
Cdd:PLN02836  320 DYVNAHAT 327
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 70-228 1.36e-19

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 86.28  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  70 AGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS------PSGRCRT 143
Cdd:PTZ00050  148 AGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRASRP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 144 FDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACR-AARIEPDEVQFI 222
Cdd:PTZ00050  228 FDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKdGANININDVDYV 307


                  ....*.
gi 1001822246 223 EAHGTG 228
Cdd:PTZ00050  308 NAHATS 313
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 28-227 2.81e-19

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 84.78  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  28 STLTSKATGMFVGVMHQDYSHRFRHADDIDLYTAAGNAPSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAG 107
Cdd:PRK14691   29 ATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 108 ECDIAIVGGVNAVLSPLSTAAECRAHMLS------PSGRCRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAG 181
Cdd:PRK14691  109 EADVALCGGAEAVIDTVSLAGFAAARALSthfnstPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVG 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1001822246 182 SAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGT 227
Cdd:PRK14691  189 YGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHAT 234
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 8-228 1.07e-18

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 81.72  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246   8 QQRILLEVAWEAIERASLPASTLTSKATGMFVGVmhqdyshrfrhaddidlytaaGNAPSVLAGRVSHALGLSGPTLTVD 87
Cdd:cd00327     7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGS---------------------GEFSGAAGQLAYHLGISGGPAYSVN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  88 TACSSSLVAVHLACAALRAGECDIAIVGGVNAvlsplstaaecrahmlspsgrcrtfdnnadgFVRGEGCGVVVLQRLSD 167
Cdd:cd00327    66 QACATGLTALALAVQQVQNGKADIVLAGGSEE-------------------------------FVFGDGAAAAVVESEEH 114

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001822246 168 AQLEGRQIEAVIAGSAVNHDGRSAGlTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:cd00327   115 ALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTG 174
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
70-228 4.11e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 81.99  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  70 AGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECD----IAIVGGVNA-------VLSPLSTAAEcrahmlSPS 138
Cdd:PRK06501  155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDralcIATDGSVSAealirfsLLSALSTQND------PPE 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 139 GRCRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDG----RSAgltvPNQRAQSELVQAACRAARI 214
Cdd:PRK06501  229 KASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhrtRSS----PDGSPAIGAIRAALADAGL 304

                         170
                  ....*....|....
gi 1001822246 215 EPDEVQFIEAHGTG 228
Cdd:PRK06501  305 TPEQIDYINAHGTS 318
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
67-227 1.35e-17

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 80.43  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  67 SVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGRC 141
Cdd:PRK08722  141 NMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALStrndePQKAS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 142 RTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQF 221
Cdd:PRK08722  221 RPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGY 300


                  ....*.
gi 1001822246 222 IEAHGT 227
Cdd:PRK08722  301 VNAHGT 306
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
63-228 1.17e-16

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 77.78  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  63 GNAPSVLAGRVshaLGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGrCR 142
Cdd:PRK05952  122 PHQAAIAAARQ---IGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AY 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 143 TFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFI 222
Cdd:PRK05952  198 PFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYI 277


                  ....*.
gi 1001822246 223 EAHGTG 228
Cdd:PRK05952  278 HAHGTA 283
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
66-228 1.84e-15

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 74.11  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  66 PSVLAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAV-LSPLS--TAAEcrahMLSPsGRCR 142
Cdd:PRK09185  136 LGSLADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLcRLTLNgfNSLE----SLSP-QPCR 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 143 TFDNNADGFVRGEGCGVVVLQRLSDAqlegrqiEAVIAG----------SAVNHDGRSAgltvpnQRAqselVQAACRAA 212
Cdd:PRK09185  211 PFSANRDGINIGEAAAFFLLEREDDA-------AVALLGvgessdahhmSAPHPEGLGA------ILA----MQQALADA 273

                         170
                  ....*....|....*.
gi 1001822246 213 RIEPDEVQFIEAHGTG 228
Cdd:PRK09185  274 GLAPADIGYINLHGTA 289
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 77-227 3.01e-15

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 73.86  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSP--LSTAAECRAhmLS-----PSGRCRTFDNNAD 149
Cdd:PLN02787  278 LGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPigLGGFVACRA--LSqrnddPTKASRPWDMNRD 355

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001822246 150 GFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGT 227
Cdd:PLN02787  356 GFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHAT 433
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 177-228 5.22e-15

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 68.75  E-value: 5.22e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1001822246 177 AVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPDEVQFIEAHGTG 228
Cdd:pfam02801   2 AVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTG 53
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
64-228 8.67e-15

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 72.46  E-value: 8.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  64 NAPSVLAGRVSHAlglSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLS--PLSTAAECRAHMLS----P 137
Cdd:PRK07910  148 NGPAAAVGLERHA---KAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEavPIAGFAQMRIVMSTnnddP 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 138 SGRCRTFDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAQSELVQAACRAARIEPD 217
Cdd:PRK07910  225 AGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPG 304

                         170
                  ....*....|.
gi 1001822246 218 EVQFIEAHGTG 228
Cdd:PRK07910  305 DIDHVNAHATG 315
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 69-227 4.77e-14

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 70.15  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  69 LAGRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGRCRT 143
Cdd:PRK08439  141 LGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALStrnddPKKASRP 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 144 FDNNADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGsaVNHDGRSAGLTVPNQRAQSELVQAACRAAriEPDEVQFIE 223
Cdd:PRK08439  221 FDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRAMKAALEMA--GNPKIDYIN 296


                  ....
gi 1001822246 224 AHGT 227
Cdd:PRK08439  297 AHGT 300
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 71-228 1.77e-11

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 62.76  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  71 GRVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECdIAIVGGVNAVLSPLSTAAECRAHMLSPSGR----CRTFDN 146
Cdd:cd00832   142 GQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTP-LVVSGGVDSALCPWGWVAQLSSGRLSTSDDparaYLPFDA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246 147 NADGFVRGEGCGVVVLQRLSDAQLEGRQIEAVIAGSAVNHDGRSAGLTVPNQRAqseLVQAACRAARIEPDEVQFIEAHG 226
Cdd:cd00832   221 AAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLAR---AIRLALADAGLTPEDVDVVFADA 297


                  ..
gi 1001822246 227 TG 228
Cdd:cd00832   298 AG 299
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 53-119 1.53e-08

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 53.81  E-value: 1.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001822246  53 ADDIDL----YTAAGNAPSVLAGRVSHALGLSG-PTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNA 119
Cdd:cd00829    35 PADIDAvvvgNAAGGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEK 106
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 14-117 1.54e-08

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 53.46  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  14 EVAWEAIERASLPASTLTSkatgMFVGVMhqdyshrfrhaddidlytAAGNAPSVLAGRVSHALGL--SGPTLTVDTACS 91
Cdd:pfam00108  29 EAIKAALERAGVDPEDVDE----VIVGNV------------------LQAGEGQNPARQAALKAGIpdSAPAVTINKVCG 86

                          90       100
                  ....*....|....*....|....*.
gi 1001822246  92 SSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:pfam00108  87 SGLKAVYLAAQSIASGDADVVLAGGV 112
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
 77-117 6.87e-08

acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]


Pssm-ID: 273881 [Multi-domain]  Cd Length: 385  Bit Score: 52.23  E-value: 6.87e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:TIGR01930  70 LPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGV 110
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 77-117 1.25e-07

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 51.33  E-value: 1.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1001822246  77 LGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:cd00751    71 LPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 82-117 1.89e-07

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 50.84  E-value: 1.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1001822246  82 PTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:COG0183    80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGV 115
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
85-188 2.96e-05

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 44.28  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  85 TVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLS-----PSGRCRTFDNNADGFVRGEGCGV 159
Cdd:PRK07967  157 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTkyndtPEKASRAYDANRDGFVIAGGGGV 236

                          90       100
                  ....*....|....*....|....*....
gi 1001822246 160 VVLQRLSDAQLEGRQIEAVIAGSAVNHDG 188
Cdd:PRK07967  237 VVVEELEHALARGAKIYAEIVGYGATSDG 265
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
51-120 8.40e-04

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 39.99  E-value: 8.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001822246  51 RHADDIDLYTA--AGNAPSVLAGRVSHALGLSG-PTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAV 120
Cdd:PRK07851   48 TDIDDLMLGCGlpGGEQGFNMARVVAVLLGYDFlPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETV 120
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
51-128 8.42e-04

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 39.75  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  51 RHADDIDLYTAAGNAPSVlaGRVSH---ALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGVNAV-LSPLST 126
Cdd:PRK06690   42 REIDDVILGNVVGPGGNV--ARLSAleaGLGLHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTsTSPFQN 119


                  ..
gi 1001822246 127 AA 128
Cdd:PRK06690  120 RA 121
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
58-123 1.14e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 39.49  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001822246  58 LYTAAGNAPSVLAGrVSHALGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV-NAVLSP 123
Cdd:PRK05656   57 LTAGAGQNPARQAA-IKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQeNMSLAP 122
PRK05790 PRK05790
putative acyltransferase; Provisional
 67-117 1.27e-03

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 39.37  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1001822246  67 SVLAGrvshaLGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:PRK05790   70 ALKAG-----LPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQ 115
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 53-116 1.60e-03

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: 38.94  E-value: 1.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  53 ADDIDLYTAAGNAPSVL----AGRVSHALGLSG-PTLTVDTACSSSLVAVHLACAALRAGECD-IAIVGG 116
Cdd:COG0332    70 PEDIDLIIVATVTPDYLfpstACLVQHKLGAKNaAAFDINAACSGFVYALSVAAALIRSGQAKnVLVVGA 139
PRK06064 PRK06064
thiolase domain-containing protein;
78-132 1.67e-03

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 38.72  E-value: 1.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1001822246  78 GLSG-PTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV---NAVLSPLSTAAECRA 132
Cdd:PRK06064   72 GLAPiPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVekmTDVPTPDATEAIARA 130
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
 82-117 3.05e-03

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 38.02  E-value: 3.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1001822246  82 PTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:PRK08947   83 PAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGV 118
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
70-131 4.72e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 37.68  E-value: 4.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001822246  70 AGRVSHALGLSGPTL--TVDTACSSSLVAVHLACAALRAGECDIAIVGGV-NAVLSPLSTAAECR 131
Cdd:PRK06366   66 AGQAAYHAGLPFGVTkyTVNVVCASGMLAVESAAREIMLGERDLVIAGGMeNMSNAPFLLPSDLR 130
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
 92-212 5.02e-03

3-oxoacyl-(acyl carrier protein) synthase; Validated


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 37.31  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  92 SSLVAVHLACAALRAGECDIAIVGGVNAVLSPLSTAAECRAHMLSPSGrcrtfdnNADGFVRGEGCGVVVLQRLSDAQLE 171
Cdd:PRK06147  135 SGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQ-------NSNGFIPGEAAAAVLLGRPAGGEAP 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1001822246 172 GRQIEAVIAGSAVNHDGRSAGLTVpnqraQSELVQAACRAA 212
Cdd:PRK06147  208 GLPLLGLGLGREPAPVGESEDLPL-----RGDGLTQAIRAA 243
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
82-127 5.49e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 37.38  E-value: 5.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1001822246  82 PTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV-NAVLSPLSTA 127
Cdd:PRK07801   81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVqNMSQIPISSA 127
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
 67-117 9.59e-03

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 36.47  E-value: 9.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1001822246  67 SVLAGrvshaLGLSGPTLTVDTACSSSLVAVHLACAALRAGECDIAIVGGV 117
Cdd:PRK09050   72 ALLAG-----LPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGV 117
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 53-116 9.90e-03

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 [Multi-domain]  Cd Length: 320  Bit Score: 36.36  E-value: 9.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001822246  53 ADDIDLYTAAGNAPSVL----AGRVSHALGLSG-PTLTVDTACSSSLVAVHLACAALRAGECD-IAIVGG 116
Cdd:cd00830    69 ADDIDLIIVATSTPDYLfpatACLVQARLGAKNaAAFDINAACSGFLYGLSTAAGLIRSGGAKnVLVVGA 138
 
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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