|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-410 |
0e+00 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 828.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKLgsaELAELVDRRAMRFLSQGGAWNHV 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKL---DPTGLIDRKVMRFMGDASAYAYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 81 AMKQALADSGLEEkDYAQNERTGIIMGSGGPSTRTLIEAAEITIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNY 160
Cdd:PRK07967 78 AMEQAIADAGLSE-EQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 161 SISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNLFDAMGAMSSKYNDTPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:PRK07967 157 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEGAIRCMRQALATVKGDVDYVNTHGTSTPVGDSKEIGAIREVF 320
Cdd:PRK07967 237 VVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 321 GSKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDDAKIDIALSNSFGFGGTN 400
Cdd:PRK07967 317 GDKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTN 396
|
410
....*....|
gi 502310494 401 ATLVFQRYNG 410
Cdd:PRK07967 397 ATLVFRRYKG 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-408 |
0e+00 |
|
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: 536.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKlgSAELAELVDRRAMRFLSQGGAWNHVA 81
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK--DFDPEEYLDRKELRRMDRFTQYALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 82 MKQALADSGLEEKDYAqNERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYS 161
Cdd:COG0304 79 AREALADAGLDLDEVD-PDRTGVIIGSGIGGLDTLEEAYR-ALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 162 ISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHE-DLDWTMSNLFDAMGAMSSKyNDTPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:COG0304 157 VSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVA--PSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:COG0304 236 LVLEELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKDAGlspEDIDYINAHGTSTPLGDAAETKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKIPH--IQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIdDAKIDIALSNS 393
Cdd:COG0304 316 IKRVFGDHAYKvpVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAR-EAKIDYALSNS 394
|
410
....*....|....*
gi 502310494 394 FGFGGTNATLVFQRY 408
Cdd:COG0304 395 FGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-405 |
4.87e-168 |
|
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: 476.65 E-value: 4.87e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKLGSAElaELVDRRAMRFLSQGGAWNHVA 81
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPE--DYLDRKELRRMDRFAQFALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 82 MKQALADSGLEEKDYAQnERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYS 161
Cdd:cd00834 79 AEEALADAGLDPEELDP-ERIGVVIGSGIGGLATIEEAYR-ALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 162 ISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHE-DLDWTMSNLFDAMGAMSSKYNDtPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:cd00834 157 VSTACASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTLAGFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPS--GEGAIRCMRQAL--ATVK-GDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:cd00834 236 LVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALadAGLSpEDIDYINAHGTSTPLNDAAESKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKI--PHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEgVPIVRKRIDDAKIDIALSNS 393
Cdd:cd00834 316 IKRVFGEHAkkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-LDYVPNEAREAPIRYALSNS 394
|
410
....*....|..
gi 502310494 394 FGFGGTNATLVF 405
Cdd:cd00834 395 FGFGGHNASLVF 406
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
257-365 |
6.47e-37 |
|
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: 130.38 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 257 YAEIVGYGATSDGYDMV--APSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGDSKEIGAIREVFGSKIP----HI 327
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALADAGvdpEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 502310494 328 QSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHIT 365
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
80-408 |
4.98e-25 |
|
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: 108.17 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 80 VAMKQALADSGLEEkDYAQnERTGIIMGSGG--------------PSTRTLIEAA-------EITIKNNSPKRIG--PFA 136
Cdd:TIGR02813 99 VVAKEVLNDAGLPD-GYDR-DKIGITLGVGGgqkqssslnarlqyPVLKKVFKASgvededsEMLIKKFQDQYIHweENS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 137 VPKAMSSTASATLATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGG-HEDLDWTMSNLFDAMGAMsskyn 215
Cdd:TIGR02813 177 FPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGvCTDNSPFMYMSFSKTPAF----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 216 dTPDSASRAYDVNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGY--DMVAPSGEGAIRCMRQALATVKG 293
Cdd:TIGR02813 252 -TTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAKALKRAYDDAGF 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 294 D---VDYVNTHGTSTPVGDSKEIGAIREVFG---SKIPHIQ--STKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHIT 365
Cdd:TIGR02813 331 AphtCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIAlgSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVD 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502310494 366 ELDP--EFEGVPIV--------RKRIDDAKIDIALSnSFGFGGTNATLVFQRY 408
Cdd:TIGR02813 411 QPNPklDIENSPFYlntetrpwMQREDGTPRRAGIS-SFGFGGTNFHMVLEEY 462
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
160-404 |
6.07e-21 |
|
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: 92.01 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 160 YSIS--SACSTSAHCIGNAAEMIQWGKQDVMFAGG-HEDLDWTMSNLFDAMGAMSskyndtPDSASRAYDVNRDGFVIAG 236
Cdd:smart00825 89 YSVTvdTACSSSLVALHLACQSLRSGECDMALAGGvNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 237 GAGVLVLEELERAKARGAKIYAEIVGYGATSDGYD--MVAPSGEGaircmrQALatvkgdvdyvnthgtstpvgdskeIG 314
Cdd:smart00825 163 GVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA------QLL------------------------IG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 315 airevfgskiphiqSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFE----GVPIVRKRIDDAKID--- 387
Cdd:smart00825 213 --------------SVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDleesPLRVPTELTPWPPPGrpr 278
|
250
....*....|....*..
gi 502310494 388 IALSNSFGFGGTNATLV 404
Cdd:smart00825 279 RAGVSSFGFGGTNAHVI 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-410 |
0e+00 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 828.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKLgsaELAELVDRRAMRFLSQGGAWNHV 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKL---DPTGLIDRKVMRFMGDASAYAYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 81 AMKQALADSGLEEkDYAQNERTGIIMGSGGPSTRTLIEAAEITIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNY 160
Cdd:PRK07967 78 AMEQAIADAGLSE-EQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 161 SISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNLFDAMGAMSSKYNDTPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:PRK07967 157 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEGAIRCMRQALATVKGDVDYVNTHGTSTPVGDSKEIGAIREVF 320
Cdd:PRK07967 237 VVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 321 GSKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDDAKIDIALSNSFGFGGTN 400
Cdd:PRK07967 317 GDKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGGTN 396
|
410
....*....|
gi 502310494 401 ATLVFQRYNG 410
Cdd:PRK07967 397 ATLVFRRYKG 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-408 |
0e+00 |
|
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: 536.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKlgSAELAELVDRRAMRFLSQGGAWNHVA 81
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK--DFDPEEYLDRKELRRMDRFTQYALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 82 MKQALADSGLEEKDYAqNERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYS 161
Cdd:COG0304 79 AREALADAGLDLDEVD-PDRTGVIIGSGIGGLDTLEEAYR-ALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 162 ISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHE-DLDWTMSNLFDAMGAMSSKyNDTPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:COG0304 157 VSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVA--PSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:COG0304 236 LVLEELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKDAGlspEDIDYINAHGTSTPLGDAAETKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKIPH--IQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIdDAKIDIALSNS 393
Cdd:COG0304 316 IKRVFGDHAYKvpVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAR-EAKIDYALSNS 394
|
410
....*....|....*
gi 502310494 394 FGFGGTNATLVFQRY 408
Cdd:COG0304 395 FGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-405 |
4.87e-168 |
|
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: 476.65 E-value: 4.87e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKLGSAElaELVDRRAMRFLSQGGAWNHVA 81
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPE--DYLDRKELRRMDRFAQFALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 82 MKQALADSGLEEKDYAQnERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYS 161
Cdd:cd00834 79 AEEALADAGLDPEELDP-ERIGVVIGSGIGGLATIEEAYR-ALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 162 ISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHE-DLDWTMSNLFDAMGAMSSKYNDtPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:cd00834 157 VSTACASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTLAGFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPS--GEGAIRCMRQAL--ATVK-GDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:cd00834 236 LVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALadAGLSpEDIDYINAHGTSTPLNDAAESKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKI--PHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEgVPIVRKRIDDAKIDIALSNS 393
Cdd:cd00834 316 IKRVFGEHAkkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-LDYVPNEAREAPIRYALSNS 394
|
410
....*....|..
gi 502310494 394 FGFGGTNATLVF 405
Cdd:cd00834 395 FGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-408 |
1.73e-138 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 401.86 E-value: 1.73e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGIS-----FSSDFAEH------GFKCQVWGSPKlgsaelaelvDRRAMR 69
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGpithfDTSDLAVKiagevkDFNPDDYMSRK----------EARRMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 70 FLSQGGAwnhVAMKQALADSGLEEKDyAQNERTGIIMGSG--GPSTrtlIEAAEITIKNNSPKRIGPFAVPKAMSSTASA 147
Cdd:PRK07314 71 RFIQYGI---AAAKQAVEDAGLEITE-ENADRIGVIIGSGigGLET---IEEQHITLLEKGPRRVSPFFVPMAIINMAAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 148 TLATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDldwTMSNL----FDAMGAMSSKyNDTPDSASR 223
Cdd:PRK07314 144 HVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA---AITPLgiagFAAARALSTR-NDDPERASR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 224 AYDVNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPS--GEGAIRCMRQALATVK---GDVDYV 298
Cdd:PRK07314 220 PFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPApdGEGAARAMKLALKDAGinpEDIDYI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 299 NTHGTSTPVGDSKEIGAIREVFG---SKIPhIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEgVP 375
Cdd:PRK07314 300 NAHGTSTPAGDKAETQAIKRVFGehaYKVA-VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD-LD 377
|
410 420 430
....*....|....*....|....*....|...
gi 502310494 376 IVRKRIDDAKIDIALSNSFGFGGTNATLVFQRY 408
Cdd:PRK07314 378 YVPNEARERKIDYALSNSFGFGGTNASLVFKRY 410
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-410 |
5.63e-114 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 339.67 E-value: 5.63e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGS-PKLGSAELAEL--------VDRRAM-RF 70
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQvPDLAEDAEAGFdpdryldpKDQRKMdRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 71 LsqggAWNHVAMKQALADSGLEEKDYAQNERTGIIMGSGGPSTRTLIEAAEITIKNnSPKRIGPFAVPKAMSSTASATLA 150
Cdd:PRK06333 83 I----LFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSR-GPRRLSPFTIPSFLTNMAAGHVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 151 TWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMS-NLFDAMGAMSSKYNDTPDSASRAYDVNR 229
Cdd:PRK06333 158 IRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSlAGFAAARALSTRFNDAPEQASRPFDRDR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 230 DGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAP--SGEGAIRCMRQALATV---KGDVDYVNTHGTS 304
Cdd:PRK06333 238 DGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGpeDGEGARRAMLIALRQAgipPEEVQHLNAHATS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 305 TPVGDSKEIGAIREVFGS-KIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDD 383
Cdd:PRK06333 318 TPVGDLGEVAAIKKVFGHvSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANKARP 397
|
410 420
....*....|....*....|....*..
gi 502310494 384 AKIDIALSNSFGFGGTNATLVFQRYNG 410
Cdd:PRK06333 398 MDMDYALSNGFGFGGVNASILFRRWEP 424
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-408 |
1.49e-111 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 333.58 E-value: 1.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 11 VVSSIGNDAAEVTESLRQAKSGI-----------SFSSDFAEH-----GFKCQVwGSPKLGSAELAELV--DRRAMRFLS 72
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIrkltefpkflpDCIPEQKALenlvaAMPCQI-AAEVDQSEFDPSDFapTKRESRATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 73 QGGAwnhvAMKQALADSGLEEKDYAQNERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATW 152
Cdd:PTZ00050 80 FAMA----AAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMK-TLYEKGHSRVSPYFIPKILGNMAAGLVAIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 153 FKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNL-FDAMGAMSSKYNDTPDSASRAYDVNRDG 231
Cdd:PTZ00050 155 HKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAgFSRMRALCTKYNDDPQRASRPFDKDRAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 232 FVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAP--SGEGAIRCMRQALATV----KGDVDYVNTHGTST 305
Cdd:PTZ00050 235 FVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPhpDGRGARRCMENALKDGaninINDVDYVNAHATST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 306 PVGDSKEIGAIREVFG---SKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRID 382
Cdd:PTZ00050 315 PIGDKIELKAIKKVFGdsgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAH 394
|
410 420
....*....|....*....|....*..
gi 502310494 383 DAK-IDIALSNSFGFGGTNATLVFQRY 408
Cdd:PTZ00050 395 PLQsIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-405 |
2.23e-101 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 307.87 E-value: 2.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGI-----------SFSSDFAEHGFK---CQVWGSPKLGSA-----ELAEL 62
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVraltqddlkmkSEDEETQLYTLDqlpSRVAALVPRGTGpgdfdEELWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 63 VDRRAMRFLsqggAWNHVAMKQALADSGLEEKDYAQNERTGIIMGSGGPSTRTLIEAAEITIKNNSpKRIGPFAVPKAMS 142
Cdd:PLN02836 86 NSRSSSRFI----GYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRL-RRLSPFFVPRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 143 STASATLATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHED-LDWTMSNLFDAMGAMSSKYNDTPDSA 221
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESsIDALSIAGFSRSRALSTKFNSCPTEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 222 SRAYDVNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPS--GEGAIRCMRQALATV---KGDVD 296
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHedGRGAVLAMTRALQQSglhPNQVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 297 YVNTHGTSTPVGDSKEIGAIREVFGSKIPH----IQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFE 372
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFSEHATSgglaFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD 400
|
410 420 430
....*....|....*....|....*....|....*
gi 502310494 373 G--VPIVRKRidDAKIDIALSNSFGFGGTNATLVF 405
Cdd:PLN02836 401 DgfVPLTASK--AMLIRAALSNSFGFGGTNASLLF 433
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-408 |
2.43e-100 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 304.35 E-value: 2.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKlgSAELAELVD----RRAMRFLSQGGA 76
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT--DFDPTEVMDpkevKKADRFIQLGLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 77 wnhvAMKQALADSGLEEKDYaQNERTGIIMGSG--GPSTrtlIEAAEITIKNNSPKRIGPFAVPKAMSSTASATLATWFK 154
Cdd:PRK08439 79 ----AAREAMKDAGFLPEEL-DAERFGVSSASGigGLPN---IEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 155 IHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDldwTMSNL----FDAMGAMSSKyNDTPDSASRAYDVNRD 230
Cdd:PRK08439 151 LKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAES---AICPVgiggFAAMKALSTR-NDDPKKASRPFDKDRD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 231 GFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEGAIRCMRQALATVKGD-VDYVNTHGTSTPVGD 309
Cdd:PRK08439 227 GFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAGNPkIDYINAHGTSTPYND 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 310 SKEIGAIREVFGSK--IPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPE--FEGVP-IVRKriddA 384
Cdd:PRK08439 307 KNETAALKELFGSKekVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPEcdLDYIPnVARK----A 382
|
410 420
....*....|....*....|....
gi 502310494 385 KIDIALSNSFGFGGTNATLVFQRY 408
Cdd:PRK08439 383 ELNVVMSNSFGFGGTNGVVIFKKV 406
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-405 |
2.24e-91 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 281.11 E-value: 2.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEH-GFKCQVwGSPkLGSAELAELVDRRAMRFLSQGGAWNH 79
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYdGLNTRL-AAP-IDDFELPAHYTRKKIRSMGRVSLMAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 80 VAMKQALADSGLEEKDYAQNERTGIIMGSGGPSTRTLIEAAEItIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVN 159
Cdd:PRK09116 79 RASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTM-LLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 160 YSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNLFDAMGAMSSKyNDTPDSASRAYDVNRDGFVIAGGAG 239
Cdd:PRK09116 158 IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGEGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 240 VLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGDSKEIGAI 316
Cdd:PRK09116 237 TLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGlapEDIGYVNAHGTATDRGDIAESQAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 317 REVFGSKIPhIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDDAKIDIALSNSFGF 396
Cdd:PRK09116 317 AAVFGARMP-ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAF 395
|
....*....
gi 502310494 397 GGTNATLVF 405
Cdd:PRK09116 396 GGINTSLIF 404
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-409 |
6.86e-85 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 268.77 E-value: 6.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPKLGSAE--LAELVDRRAMRFLsqggAWNH 79
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDgwVAPKLSKRMDKFM----LYLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 80 VAMKQALADSGLEEK--DYAQNERTGIIMGSGGPSTRTL---IEAAEItiknnSPKRIGPFAVPKAMSSTASATLATWFK 154
Cdd:PLN02787 205 TAGKKALADGGITEDvmKELDKTKCGVLIGSAMGGMKVFndaIEALRI-----SYRKMNPFCVPFATTNMGSAMLAMDLG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 155 IHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMS-NLFDAMGAMSSKyNDTPDSASRAYDVNRDGFV 233
Cdd:PLN02787 280 WMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGlGGFVACRALSQR-NDDPTKASRPWDMNRDGFV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 234 IAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEGA--IRCMRQALA---TVKGDVDYVNTHGTSTPVG 308
Cdd:PLN02787 359 MGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAgvILCIEKALAqsgVSKEDVNYINAHATSTKAG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 309 DSKEIGAIREVFGSKIP-HIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDDAKID 387
Cdd:PLN02787 439 DLKEYQALMRCFGQNPElRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIK 518
|
410 420
....*....|....*....|..
gi 502310494 388 IALSNSFGFGGTNATLVFQRYN 409
Cdd:PLN02787 519 VALSNSFGFGGHNSSILFAPYK 540
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
81-404 |
6.38e-81 |
|
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: 252.17 E-value: 6.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 81 AMKQALADSGLEeKDYAQNERTGIIMGSGGPSTRTLIEAAEitiknnSPKRIGPFAVPKAMSSTASATLATWFKIHGVNY 160
Cdd:cd00825 18 AAERAIADAGLS-REYQKNPIVGVVVGTGGGSPRFQVFGAD------AMRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 161 SISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNLFDAMGAMSskyndTPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:cd00825 91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALS-----TPEKASRTFDAAADGFVFGDGAGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMV--APSGEGAIRCMRQALA---TVKGDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:cd00825 166 LVVEELEHALARGAHIYAEIVGTAATIDGAGMGafAPSAEGLARAAKEALAvagLTVWDIDYLVAHGTGTPIGDVKELKL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIvrkRIDDAKIDIALSNSFG 395
Cdd:cd00825 246 LRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVT---ETTPRELRTALLNGFG 322
|
....*....
gi 502310494 396 FGGTNATLV 404
Cdd:cd00825 323 LGGTNATLV 331
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-407 |
1.88e-80 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 253.39 E-value: 1.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSPK-LGSAELAELVDRRAMRFLSQGGAwnhV 80
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKdFNCEEYMSKKDARKMDLFIQYGI---A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 81 AMKQALADSGLEEKDyAQNERTGIIMGSGgPSTRTLIEAAEITIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNY 160
Cdd:PRK08722 81 AGIQALDDSGLEVTE-ENAHRIGVAIGSG-IGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 161 SISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMS-NLFDAMGAMSSKyNDTPDSASRAYDVNRDGFVIAGGAG 239
Cdd:PRK08722 159 AISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGmAGFGAAKALSTR-NDEPQKASRPWDKDRDGFVLGDGAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 240 VLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPS--GEGAIRCMRQAL--ATVKGD-VDYVNTHGTSTPVGDSKEIG 314
Cdd:PRK08722 238 MMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSedGSGGALAMEAAMrdAGVTGEqIGYVNAHGTSTPAGDVAEIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 315 AIREVFG---SKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITelDPEfEG-----VPIVRKRIDDakI 386
Cdd:PRK08722 318 GIKRALGeagSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLD--DPE-EGldidlVPHTARKVES--M 392
|
410 420
....*....|....*....|.
gi 502310494 387 DIALSNSFGFGGTNATLVFQR 407
Cdd:PRK08722 393 EYAICNSFGFGGTNGSLIFKK 413
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-404 |
4.19e-79 |
|
"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: 249.66 E-value: 4.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEV---TESLRQAKSGISFSSDFAEHgFKCQVWGSPKLGSAElAELVDRraMRFLSQGGAWN 78
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSR-FDRGVAGQIPTGDIP-GWDAKR--TGIVDRTTLLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 79 HVAMKQALADSGLEEKDYAQNERTGIIMGSGGPSTRtlieAAEITIKNNSpKRIGPFAVPKAM--SSTASATLATWFKI- 155
Cdd:cd00828 77 LVATEEALADAGITDPYEVHPSEVGVVVGSGMGGLR----FLRRGGKLDA-RAVNPYVSPKWMlsPNTVAGWVNILLLSs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 156 HGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNLFDAMGAMSSKYNDtPDSASRAYDVNRDGFVIA 235
Cdd:cd00828 152 HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEE-PEEMSRPFDETRDGFVEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 236 GGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPS-GEGAIRCMRQALATV---KGDVDYVNTHGTSTPVGDSK 311
Cdd:cd00828 231 EGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAgGKGIARAIRTALAKAglsLDDLDVISAHGTSTPANDVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 312 EIGAIREVFG--SKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDD-AKIDI 388
Cdd:cd00828 311 ESRAIAEVAGalGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLnLKVRA 390
|
410
....*....|....*.
gi 502310494 389 ALSNSFGFGGTNATLV 404
Cdd:cd00828 391 ALVNAFGFGGSNAALV 406
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-407 |
1.84e-76 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 243.01 E-value: 1.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGSP------KLGSAELAELVDRRAMRFLSQG 74
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAGAGLAsafigaELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 75 GAWNHVAMKQALADSGLeekDYAQNERTGIIMGSGGPSTRTLIEAAEITIKNnsPKRIGPFAVPKAMSSTASATLATWFK 154
Cdd:PRK07103 81 AQAALAAAREAWRDAAL---GPVDPDRIGLVVGGSNLQQREQALVHETYRDR--PAFLRPSYGLSFMDTDLVGLCSEQFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 155 IHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFA-GGHEDLDWTMSNLFDAMGAM-SSKYNDTPDSASRAYDVNRDGF 232
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAvGALMDLSYWECQALRSLGAMgSDRFADEPEAACRPFDQDRDGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 233 VIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGD 309
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAGlgpEDIDYVNPHGTGSPLGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 310 SKEIGAIrevFGSKIPH--IQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITE-LDPEFEgvpIVRKRIDDAKI 386
Cdd:PRK07103 316 ETELAAL---FASGLAHawINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERFR---WVGSTAESARI 389
|
410 420
....*....|....*....|.
gi 502310494 387 DIALSNSFGFGGTNATLVFQR 407
Cdd:PRK07103 390 RYALSLSFGFGGINTALVLER 410
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4-408 |
8.63e-71 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 228.46 E-value: 8.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 4 VVVTGLGVVSSIGNDAAEVTESLRQAKSGI-SFSSDF-AEHGFKCQVWGSPKLGSAELAELVDRRAMRFLSQGGAwnhVA 81
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIrTLDDPFvEEFDLPVRIGGHLLEEFDHQLTRVELRRMSYLQRMST---VL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 82 MKQALADSGLEEKDyaqNERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYS 161
Cdd:PRK07910 91 GRRVWENAGSPEVD---TNRLMVSIGTGLGSAEELVFAYD-DMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 162 ISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHED-LDWTMSNLFDAMGAMSSKYNDTPDSASRAYDVNRDGFVIAGGAGV 240
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETrIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 241 LVLEELERAKARGAKIYAEIVGYGATSDGYDMVA--PSGEGAIRCMRQALATV---KGDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVApdPNGERAGHAMTRAIELAgltPGDIDHVNAHATGTSVGDVAEGKA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEgVPIVRKRIDDAKIDIALSNSFG 395
Cdd:PRK07910 327 INNALGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEID-LDVVAGEPRPGNYRYAINNSFG 405
|
410
....*....|...
gi 502310494 396 FGGTNATLVFQRY 408
Cdd:PRK07910 406 FGGHNVALAFGRY 418
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
98-408 |
9.76e-68 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 218.44 E-value: 9.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 98 QNERTGIIMGSGGPSTRTLIEAAEiTIKNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYSISSACSTSAHCIGNAA 177
Cdd:PRK14691 24 KQERTATIIGAGIGGFPAIAHAVR-TSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 178 EMIQWGKQDVMFAGGHEDLDWTMSNL-FDAMGAMSSKYNDTPDSASRAYDVNRDGFVIAGGAGVLVLEELERAKARGAKI 256
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAgFAAARALSTHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 257 YAEIVGYGATSDGYDMV--APSGEGAIRCMRQAL---ATVKGDVDYVNTHGTSTPVGDSKEIGAIREVFG-SKIPHIQST 330
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTsgAEDGDGAYRAMKIALrqaGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGeSNALAITST 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502310494 331 KSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRIDDAKIDIALSNSFGFGGTNATLVFQRY 408
Cdd:PRK14691 263 KSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-408 |
4.16e-64 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 211.41 E-value: 4.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 4 VVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGS------PKLGSAELAElvdrramrflsqggAW 77
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTvdflpeSPFGASALSE--------------AL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 78 NHVAMKQALADSGLEEKDY-------------------AQNERTGiimGSGGPSTRTLIEAAeitiknnspkRIGPFAV- 137
Cdd:PRK06501 79 ARLAAEEALAQAGIGKGDFpgplflaappvelewparfALAAAVG---DNDAPSYDRLLRAA----------RGGRFDAl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 138 -PKAMSSTASATLATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGhEDLDWTMSNL--FDAMGAMSSKy 214
Cdd:PRK06501 146 hERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIA-TDGSVSAEALirFSLLSALSTQ- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 215 NDTPDSASRAYDVNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMV--APSGEGAIRCMRQALA--- 289
Cdd:PRK06501 224 NDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTrsSPDGSPAIGAIRAALAdag 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 290 TVKGDVDYVNTHGTSTPVGDSKEIGAIREVFGSKIPHI--QSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITEL 367
Cdd:PRK06501 304 LTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIpvSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNP 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 502310494 368 DP--EFEGVPIVRKridDAKIDIALSNSFGFGGTNATLVFQRY 408
Cdd:PRK06501 384 DPaiPLDVVPNVAR---DARVTAVLSNSFGFGGQNASLVLTAE 423
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-407 |
7.13e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 199.30 E-value: 7.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCqVWGS------PKLGSAeLAElVDRRAMRFLSQG 74
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRASGMRPCDFWLVDLPT-WVGEvvgvelPALPAA-LAA-FDCRNNRLALLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 75 GAWNHVAMKQALADSGleekdyaqNERTGIIMG---SGgpstrtlIEAAEITIK---NNSPKRIGPFAVPKAMSSTASAT 148
Cdd:PRK09185 78 LQQIEPAVEAAIARYG--------ADRIGVVLGtstSG-------ILEGELAYRrrdPAHGALPADYHYAQQELGSLADF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 149 LATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDLDWTMSNLFDAMGAMSskyndtpDSASRAYDVN 228
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLS-------PQPCRPFSAN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 229 RDGFVIAGGAGVLVLEELERAKARgakiyaeIVGYGATSDGYDMVAP--SGEGAIRCMRQALATVK---GDVDYVNTHGT 303
Cdd:PRK09185 216 RDGINIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPhpEGLGAILAMQQALADAGlapADIGYINLHGT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 304 STPVGDSKEIGAIREVFGSKIPhIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFEGVPIVRKRiDD 383
Cdd:PRK09185 289 ATPLNDAMESRAVAAVFGDGVP-CSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENA-QA 366
|
410 420
....*....|....*....|....
gi 502310494 384 AKIDIALSNSFGFGGTNATLVFQR 407
Cdd:PRK09185 367 LAIRYVLSNSFAFGGNNCSLIFGR 390
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
84-404 |
3.83e-57 |
|
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: 193.16 E-value: 3.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 84 QALADSGLEEKDYAqNERTGIIMGSGGPSTRTLIeaaeitikNNSPKRIGPFAVPKAMSSTASATLATWFKIHGVNYSIS 163
Cdd:cd00833 97 EALEDAGYSPESLA-GSRTGVFVGASSSDYLELL--------ARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 164 SACSTSAHCIGNAAEMIQWGKQDVMFAGG-HEDLDWTMSNLFDAMGAMSskyndtPDSASRAYDVNRDGFVIAGGAGVLV 242
Cdd:cd00833 168 TACSSSLVALHLACQSLRSGECDLALVGGvNLILSPDMFVGFSKAGMLS------PDGRCRPFDADADGYVRGEGVGVVV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 243 LEELERAKARGAKIYAEIVGYGATSDGYD--MVAPSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGDSKEIGAIR 317
Cdd:cd00833 242 LKRLSDALRDGDRIYAVIRGSAVNQDGRTkgITAPSGEAQAALIRRAYARAGvdpSDIDYVEAHGTGTPLGDPIEVEALA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 318 EVFGSKIPH-----IQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPE--FEGVP--IVRKRID---DAK 385
Cdd:cd00833 322 KVFGGSRSAdqpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKidFEESPlrVPTEARPwpaPAG 401
|
330
....*....|....*....
gi 502310494 386 IDIALSNSFGFGGTNATLV 404
Cdd:cd00833 402 PRRAGVSSFGFGGTNAHVI 420
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-407 |
2.01e-51 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 176.78 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 1 MRRVVVTGLGVVSSIGnDAAEVTESLRQAKSGISFSSDFAEhgfkcqvwgspkLGSAELAELVDR-RAMRFLSQggawnh 79
Cdd:PRK05952 1 MMKVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPFPE------------LPPLPLGLIGNQpSSLEDLTK------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 80 VAMKQALADSGLEekdyAQNERTGIIMGSggpsTRTLIEAAEITIKNNSPKRIGPFAVPK---------AMSSTASATLA 150
Cdd:PRK05952 62 TVVTAALKDAGLT----PPLTDCGVVIGS----SRGCQGQWEKLARQMYQGDDSPDEELDlenwldtlpHQAAIAAARQI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 151 twfKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHED--LDWTMSNlFDAMGAMSskyndtpdsASRAY--D 226
Cdd:PRK05952 134 ---GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEApiTPLTLAG-FQQMGALA---------KTGAYpfD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 227 VNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYDMVAPSGEG--AIRCMRQALA---TVKGDVDYVNTH 301
Cdd:PRK05952 201 RQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGksAIAAIQQCLArsgLTPEDIDYIHAH 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 302 GTSTPVGDSKEIGAIREVFGSKIPhIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITEldPEFEgVPIVRKRi 381
Cdd:PRK05952 281 GTATRLNDQREANLIQALFPHRVA-VSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFD-LNFVRQA- 355
|
410 420
....*....|....*....|....*.
gi 502310494 382 DDAKIDIALSNSFGFGGTNATLVFQR 407
Cdd:PRK05952 356 QQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
81-404 |
9.12e-45 |
|
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: 155.68 E-value: 9.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 81 AMKQALADSGLEekdyaQNERTGIIMGSGGPSTRtlieaaeitiknnspkrigpfavpkamSSTASATLATWFKI-HGVN 159
Cdd:cd00327 14 AAEQAIADAGLS-----KGPIVGVIVGTTGGSGE---------------------------FSGAAGQLAYHLGIsGGPA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 160 YSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEDldwtmsnlfdamgamsskyndtpdsasraydvnrdgFVIAGGAG 239
Cdd:cd00327 62 YSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDGAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 240 VLVLEELERAKARGAKIYAEIVGYGATSDGYDMV-APSGEGAIRCMRQALATV---KGDVDYVNTHGTSTPVGDSKEIGA 315
Cdd:cd00327 106 AAVVESEEHALRRGAHPQAEIVSTAATFDGASMVpAVSGEGLARAARKALEGAgltPSDIDYVEAHGTGTPIGDAVELAL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 316 IREVFGSKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESahiteldpefegvpivrkridDAKIDIALSNSFG 395
Cdd:cd00327 186 GLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------------PREPRTVLLLGFG 244
|
....*....
gi 502310494 396 FGGTNATLV 404
Cdd:cd00327 245 LGGTNAAVV 253
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
76-401 |
9.26e-38 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 145.79 E-value: 9.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 76 AWnhvamkQALADSGLEEKDYAqNERTGIIMGSGGPSTRTLIEAAeitiknnsPKRIGPFAVPKAMSSTASATLATWFKI 155
Cdd:COG3321 99 AW------EALEDAGYDPESLA-GSRTGVFVGASSNDYALLLLAD--------PEAIDAYALTGNAKSVLAGRISYKLDL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 156 HGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGG-HEDLDWTMSNLFDAMGAMSskyndtPDSASRAYDVNRDGFVI 234
Cdd:COG3321 164 RGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGvNLMLTPESFILFSKGGMLS------PDGRCRAFDADADGYVR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 235 AGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGYD--MVAPSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGD 309
Cdd:COG3321 238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADAGvdpATVDYVEAHGTGTPLGD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 310 SKEIGAIREVFGSKIP-----HIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPE--FEGVP--IVRKR 380
Cdd:COG3321 318 PIEAAALTAAFGQGRPadqpcAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHidFENSPfyVNTEL 397
|
330 340
....*....|....*....|....
gi 502310494 381 ID---DAKIDIALSNSFGFGGTNA 401
Cdd:COG3321 398 RPwpaGGGPRRAGVSSFGFGGTNA 421
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
257-365 |
6.47e-37 |
|
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: 130.38 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 257 YAEIVGYGATSDGYDMV--APSGEGAIRCMRQALATVK---GDVDYVNTHGTSTPVGDSKEIGAIREVFGSKIP----HI 327
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALADAGvdpEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 502310494 328 QSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHIT 365
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-249 |
2.20e-31 |
|
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: 120.05 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGIS-FSSD----FAEHGFKCQV-------WGSPKL----------GSAEL 59
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeIPADrwdpDKLYDPPSRIagkiytkWGGLDDifdfdplffgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 60 AELVDRRAMRFLsqggawnhVAMKQALADSGLEEKDYAqNERTGIIMGSGGPSTRTLIEAAEitikNNSPKRIGPFAVPk 139
Cdd:pfam00109 81 AERMDPQQRLLL--------EAAWEALEDAGITPDSLD-GSRTGVFIGSGIGDYAALLLLDE----DGGPRRGSPFAVG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 140 AMSSTASATLATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHE-DLDWTMSNLFDAMGAMSskyndtP 218
Cdd:pfam00109 147 TMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLS------P 220
|
250 260 270
....*....|....*....|....*....|.
gi 502310494 219 DSASRAYDVNRDGFVIAGGAGVLVLEELERA 249
Cdd:pfam00109 221 DGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-404 |
4.00e-27 |
|
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: 111.68 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 2 RRVVVTGLGVVSSIGNDAAEVTESLRQAKSGISFSSDFAEHGFKCQVWGspklgsaELAELVDRRAM--RFLSQGGAWNH 79
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAG-------EVPDFDAAEHLpgRLLPQTDRMTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 80 ---VAMKQALADSGLEEKDYAQNERtGIIM--GSGGpstrtlIEAAEITIKN---NSPKRIGPFavpkamSSTAsatlat 151
Cdd:cd00832 74 lalAAADWALADAGVDPAALPPYDM-GVVTasAAGG------FEFGQRELQKlwsKGPRHVSAY------QSFA------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 152 WFkiHGVN---YSISSACStsAHC-------------IGNAAEMIQWGKqDVMFAGGHED--LDWTMSNLFdAMGAMSSk 213
Cdd:cd00832 135 WF--YAVNtgqISIRHGMR--GPSgvvvaeqaggldaLAQARRLVRRGT-PLVVSGGVDSalCPWGWVAQL-SSGRLST- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 214 yNDTPDSASRAYDVNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGyDMVAPSGEGAIRCMRQALA---T 290
Cdd:cd00832 208 -SDDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDP-PPGSGRPPGLARAIRLALAdagL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 291 VKGDVDYVNTHGTSTPVGDSKEIGAIREVFGSKIPHIQSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPE 370
Cdd:cd00832 286 TPEDVDVVFADAAGVPELDRAEAAALAAVFGPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPA 365
|
410 420 430
....*....|....*....|....*....|....
gi 502310494 371 FeGVPIVRKRIDDAKIDIALSNSFGFGGTNATLV 404
Cdd:cd00832 366 Y-GLDLVTGRPRPAALRTALVLARGRGGFNSALV 398
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
80-408 |
4.98e-25 |
|
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: 108.17 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 80 VAMKQALADSGLEEkDYAQnERTGIIMGSGG--------------PSTRTLIEAA-------EITIKNNSPKRIG--PFA 136
Cdd:TIGR02813 99 VVAKEVLNDAGLPD-GYDR-DKIGITLGVGGgqkqssslnarlqyPVLKKVFKASgvededsEMLIKKFQDQYIHweENS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 137 VPKAMSSTASATLATWFKIHGVNYSISSACSTSAHCIGNAAEMIQWGKQDVMFAGG-HEDLDWTMSNLFDAMGAMsskyn 215
Cdd:TIGR02813 177 FPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGvCTDNSPFMYMSFSKTPAF----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 216 dTPDSASRAYDVNRDGFVIAGGAGVLVLEELERAKARGAKIYAEIVGYGATSDGY--DMVAPSGEGAIRCMRQALATVKG 293
Cdd:TIGR02813 252 -TTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAKALKRAYDDAGF 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 294 D---VDYVNTHGTSTPVGDSKEIGAIREVFG---SKIPHIQ--STKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHIT 365
Cdd:TIGR02813 331 AphtCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIAlgSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVD 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502310494 366 ELDP--EFEGVPIV--------RKRIDDAKIDIALSnSFGFGGTNATLVFQRY 408
Cdd:TIGR02813 411 QPNPklDIENSPFYlntetrpwMQREDGTPRRAGIS-SFGFGGTNFHMVLEEY 462
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
160-404 |
6.07e-21 |
|
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: 92.01 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 160 YSIS--SACSTSAHCIGNAAEMIQWGKQDVMFAGG-HEDLDWTMSNLFDAMGAMSskyndtPDSASRAYDVNRDGFVIAG 236
Cdd:smart00825 89 YSVTvdTACSSSLVALHLACQSLRSGECDMALAGGvNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 237 GAGVLVLEELERAKARGAKIYAEIVGYGATSDGYD--MVAPSGEGaircmrQALatvkgdvdyvnthgtstpvgdskeIG 314
Cdd:smart00825 163 GVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA------QLL------------------------IG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 315 airevfgskiphiqSTKSLTGHSLGAAGVQESIYSLLMMQQGFIGESAHITELDPEFE----GVPIVRKRIDDAKID--- 387
Cdd:smart00825 213 --------------SVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDleesPLRVPTELTPWPPPGrpr 278
|
250
....*....|....*..
gi 502310494 388 IALSNSFGFGGTNATLV 404
Cdd:smart00825 279 RAGVSSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
231-262 |
1.80e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 40.32 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|..
gi 502310494 231 GFVIAGGAGVLVLEELERAKARGAKIYAEIVG 262
Cdd:PRK06519 238 GFILGSGGAFLVLESREHAEARGARPYARISG 269
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
229-298 |
5.56e-03 |
|
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: 38.51 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502310494 229 RDGFVIAG-------GAGVLVLEELERAKARGAKIYAEIVGYGATSdgydmVAPS--GEGAIRCMRQALA----TVkGDV 295
Cdd:COG0183 236 KDGTVTAGnasgindGAAALLLMSEEAAKELGLKPLARIVAYAVAG-----VDPEimGIGPVPATRKALAraglTL-DDI 309
|
...
gi 502310494 296 DYV 298
Cdd:COG0183 310 DLI 312
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
160-202 |
7.68e-03 |
|
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: 38.23 E-value: 7.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 502310494 160 YSISSACSTSAHCIGNAAEMIQWGKQDVMFAGGHEdldwTMSN 202
Cdd:cd00751 78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVE----SMSR 116
|
|
| |
