|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-405 |
0e+00 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 823.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEaYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:PRK07967 81 QAIADAGLSEE-QVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVV 240
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 241 EELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDK 320
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVFGDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 321 SPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDR-ELTTVMSNSFGFGGTNATL 399
Cdd:PRK07967 320 SPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNaELTTVMSNSFGFGGTNATL 399
|
....*.
gi 16130258 400 VMRKLK 405
Cdd:PRK07967 400 VFRRYK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-403 |
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: 535.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKdFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYqNNPRVGLIAGSGGGSPRFQVFGADAMRGpRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:COG0304 81 EALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLE-KGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGE-ELCWEMACEFDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGGGGMVV 239
Cdd:COG0304 159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 240 VEELEHALARGAHIYAEIVGYGATSDGADMVA--PSGEGAVRCMKMAMH--GVD-TPIDYLNSHGTSTPVGDVKELAAIR 314
Cdd:COG0304 238 LEELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKdaGLSpEDIDYINAHGTSTPLGDAAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 315 EVFGD--KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVTETT-DRELTTVMSNSFG 391
Cdd:COG0304 318 RVFGDhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDP-ECDLDYVPNEArEAKIDYALSNSFG 396
|
410
....*....|..
gi 16130258 392 FGGTNATLVMRK 403
Cdd:COG0304 397 FGGHNASLVFKR 408
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-401 |
4.93e-169 |
|
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: 478.96 E-value: 4.93e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKL-DTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDfDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYqNNPRVGLIAGSGGGSPRFQVFGADAMRgPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:cd00834 81 EALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALL-EKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMAC-EFDAMGALSTKYNDtPEKASRTYDAHRDGFVIAGGGGMVV 239
Cdd:cd00834 159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLaGFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 240 VEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMH--GVD-TPIDYLNSHGTSTPVGDVKELAAIR 314
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALAdaGLSpEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 315 EVFGD--KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVT-ETTDRELTTVMSNSFG 391
Cdd:cd00834 318 RVFGEhaKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDP-ECDLDYVPnEAREAPIRYALSNSFG 396
|
410
....*....|
gi 16130258 392 FGGTNATLVM 401
Cdd:cd00834 397 FGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-402 |
1.89e-136 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 396.08 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKdFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYqNNPRVGLIAGSG-GGSPRFQVfGADAM--RGPRglkAVGPYVVTKAMASGVSACLATPFKIHGVNY 157
Cdd:TIGR03150 81 EAVEDSGLDIEEE-DAERVGVIIGSGiGGLETIEE-QHIVLleKGPR---RVSPFFIPMSIINMAAGQISIRYGAKGPNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 158 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTkYNDTPEKASRTYDAHRDGFVIAGGGG 236
Cdd:TIGR03150 156 AVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAgFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 237 MVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMH--GVDTP-IDYLNSHGTSTPVGDVKELA 311
Cdd:TIGR03150 235 VLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPApeGEGAARAMRAALKdaGINPEdVDYINAHGTSTPLGDKAETK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 312 AIREVFGD--KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAgLNIVT-ETTDRELTTVMSN 388
Cdd:TIGR03150 315 AIKKVFGDhaYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD-LDYVPnEAREAKIDYALSN 393
|
410
....*....|....
gi 16130258 389 SFGFGGTNATLVMR 402
Cdd:TIGR03150 394 SFGFGGTNASLVFK 407
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
254-362 |
1.60e-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: 131.92 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 254 YAEIVGYGATSDGADMV--APSGEGAVRCMKMAMHGVDTP---IDYLNSHGTSTPVGDVKELAAIREVFGDKSP----AI 324
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALADAGVDpedVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130258 325 SATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIE 362
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
157-401 |
2.11e-24 |
|
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: 102.02 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 157 YSIS--SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCW-EMACEFDAMGALStkyndtPEKASRTYDAHRDGFVIAG 233
Cdd:smart00825 89 YSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNLILSpDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 234 GGGMVVVEELEHALARGAHIYAEIVGYGATSDGAD--MVAPSGEGAVrcmkmamhgvdtpidylnshgtstpvgdvkela 311
Cdd:smart00825 163 GVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPAQL--------------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 312 airevfgdkspAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEEL----DEQAAGLNIVTETTDRELTT--- 384
Cdd:smart00825 210 -----------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPnphiDLEESPLRVPTELTPWPPPGrpr 278
|
250
....*....|....*...
gi 16130258 385 -VMSNSFGFGGTNATLVM 401
Cdd:smart00825 279 rAGVSSFGFGGTNAHVIL 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-405 |
0e+00 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 823.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEaYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:PRK07967 81 QAIADAGLSEE-QVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVV 240
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 241 EELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDK 320
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPIDYINTHGTSTPVGDVKELGAIREVFGDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 321 SPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDR-ELTTVMSNSFGFGGTNATL 399
Cdd:PRK07967 320 SPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNaELTTVMSNSFGFGGTNATL 399
|
....*.
gi 16130258 400 VMRKLK 405
Cdd:PRK07967 400 VFRRYK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-403 |
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: 535.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKdFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYqNNPRVGLIAGSGGGSPRFQVFGADAMRGpRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:COG0304 81 EALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLE-KGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGE-ELCWEMACEFDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGGGGMVV 239
Cdd:COG0304 159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTR-NDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 240 VEELEHALARGAHIYAEIVGYGATSDGADMVA--PSGEGAVRCMKMAMH--GVD-TPIDYLNSHGTSTPVGDVKELAAIR 314
Cdd:COG0304 238 LEELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKdaGLSpEDIDYINAHGTSTPLGDAAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 315 EVFGD--KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVTETT-DRELTTVMSNSFG 391
Cdd:COG0304 318 RVFGDhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDP-ECDLDYVPNEArEAKIDYALSNSFG 396
|
410
....*....|..
gi 16130258 392 FGGTNATLVMRK 403
Cdd:COG0304 397 FGGHNASLVFKR 408
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-401 |
4.93e-169 |
|
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: 478.96 E-value: 4.93e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKL-DTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDfDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYqNNPRVGLIAGSGGGSPRFQVFGADAMRgPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:cd00834 81 EALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALL-EKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMAC-EFDAMGALSTKYNDtPEKASRTYDAHRDGFVIAGGGGMVV 239
Cdd:cd00834 159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLaGFAALRALSTRNDD-PEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 240 VEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMH--GVD-TPIDYLNSHGTSTPVGDVKELAAIR 314
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDpdGEGAARAMRAALAdaGLSpEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 315 EVFGD--KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVT-ETTDRELTTVMSNSFG 391
Cdd:cd00834 318 RVFGEhaKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDP-ECDLDYVPnEAREAPIRYALSNSFG 396
|
410
....*....|
gi 16130258 392 FGGTNATLVM 401
Cdd:cd00834 397 FGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-402 |
1.89e-136 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 396.08 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKdFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYqNNPRVGLIAGSG-GGSPRFQVfGADAM--RGPRglkAVGPYVVTKAMASGVSACLATPFKIHGVNY 157
Cdd:TIGR03150 81 EAVEDSGLDIEEE-DAERVGVIIGSGiGGLETIEE-QHIVLleKGPR---RVSPFFIPMSIINMAAGQISIRYGAKGPNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 158 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTkYNDTPEKASRTYDAHRDGFVIAGGGG 236
Cdd:TIGR03150 156 AVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAgFAAMKALST-RNDDPEKASRPFDKDRDGFVMGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 237 MVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMH--GVDTP-IDYLNSHGTSTPVGDVKELA 311
Cdd:TIGR03150 235 VLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPApeGEGAARAMRAALKdaGINPEdVDYINAHGTSTPLGDKAETK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 312 AIREVFGD--KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAgLNIVT-ETTDRELTTVMSN 388
Cdd:TIGR03150 315 AIKKVFGDhaYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECD-LDYVPnEAREAKIDYALSN 393
|
410
....*....|....
gi 16130258 389 SFGFGGTNATLVMR 402
Cdd:TIGR03150 394 SFGFGGTNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-403 |
4.95e-133 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 387.61 E-value: 4.95e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSM 79
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKdFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 80 EQAIADAGLSPEAyQNNPRVGLIAGSG-GGSPRFQVfGADAM--RGPRglkAVGPYVVTKAMASGVSACLATPFKIHGVN 156
Cdd:PRK07314 81 KQAVEDAGLEITE-ENADRIGVIIGSGiGGLETIEE-QHITLleKGPR---RVSPFFVPMAIINMAAGHVSIRYGAKGPN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 157 YSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGGG 235
Cdd:PRK07314 156 HSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAgFAAARALSTR-NDDPERASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 236 GMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMH--GVdTP--IDYLNSHGTSTPVGDVKE 309
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPApdGEGAARAMKLALKdaGI-NPedIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 310 LAAIREVFGDKSP--AISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAgLNIVT-ETTDRELTTVM 386
Cdd:PRK07314 314 TQAIKRVFGEHAYkvAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD-LDYVPnEARERKIDYAL 392
|
410
....*....|....*..
gi 16130258 387 SNSFGFGGTNATLVMRK 403
Cdd:PRK07314 393 SNSFGFGGTNASLVFKR 409
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
71-401 |
3.01e-126 |
|
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: 367.73 E-value: 3.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 71 ASIYAFLSMEQAIADAGLSPEaYQNNPRVGLIAGSGGGSPRFQVFGADAMRgprglkAVGPYVVTKAMASGVSACLATPF 150
Cdd:cd00825 11 VSILGFEAAERAIADAGLSRE-YQKNPIVGVVVGTGGGSPRFQVFGADAMR------AVGPYVVTKAMFPGASGQIATPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 151 KIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALStkyndTPEKASRTYDAHRDGFV 230
Cdd:cd00825 84 GIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALS-----TPEKASRTFDAAADGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 231 IAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMV--APSGEGAVRCMKMAMHGVDT---PIDYLNSHGTSTPVG 305
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGafAPSAEGLARAAKEALAVAGLtvwDIDYLVAHGTGTPIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 306 DVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqaAGLNIVTETTDRELTTV 385
Cdd:cd00825 239 DVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316
|
330
....*....|....*.
gi 16130258 386 MSNSFGFGGTNATLVM 401
Cdd:cd00825 317 LLNGFGLGGTNATLVL 332
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-406 |
6.88e-111 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 331.58 E-value: 6.88e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK---------LDTTGLIDRKVVRFMSDA 71
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeagFDPDRYLDPKDQRKMDRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 72 SIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSG-GGSPRFqvfgADAMR--GPRGLKAVGPYVVTKAMASGVSACLAT 148
Cdd:PRK06333 83 ILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGvGGFPAI----AEAVRtlDSRGPRRLSPFTIPSFLTNMAAGHVSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 149 PFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTKYNDTPEKASRTYDAHRD 227
Cdd:PRK06333 159 RYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAgFAAARALSTRFNDAPEQASRPFDRDRD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 228 GFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAP--SGEGAVRCMKMAMHGVDTP---IDYLNSHGTST 302
Cdd:PRK06333 239 GFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGpeDGEGARRAMLIALRQAGIPpeeVQHLNAHATST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 303 PVGDVKELAAIREVFG-DKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIV-TETTDR 380
Cdd:PRK06333 319 PVGDLGEVAAIKKVFGhVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVaNKARPM 398
|
410 420
....*....|....*....|....*.
gi 16130258 381 ELTTVMSNSFGFGGTNATLVMRKLKD 406
Cdd:PRK06333 399 DMDYALSNGFGFGGVNASILFRRWEP 424
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-401 |
4.38e-109 |
|
"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: 326.70 E-value: 4.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 3 RAVITGLGIVSSIGNN---QQEVLASLREGRSGITFSQELKDSgMRSHVWGNVKldtTGLIDRKVVR---FMSDASIYAF 76
Cdd:cd00828 2 RVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVARLKSR-FDRGVAGQIP---TGDIPGWDAKrtgIVDRTTLLAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 77 LSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMRgprglKAVGPYVVTKAM--ASGVSACLATPFKI-H 153
Cdd:cd00828 78 VATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDA-----RAVNPYVSPKWMlsPNTVAGWVNILLLSsH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 154 GVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDtPEKASRTYDAHRDGFVIAG 233
Cdd:cd00828 153 GPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEE-PEEMSRPFDETRDGFVEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 234 GGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPS-GEGAVRCMKMAMHGV---DTPIDYLNSHGTSTPVGDVKE 309
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAgGKGIARAIRTALAKAglsLDDLDVISAHGTSTPANDVAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 310 LAAIREVFG--DKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDRELTT--V 385
Cdd:cd00828 312 SRAIAEVAGalGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVraA 391
|
410
....*....|....*.
gi 16130258 386 MSNSFGFGGTNATLVM 401
Cdd:cd00828 392 LVNAFGFGGSNAALVL 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-403 |
3.14e-102 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 309.32 E-value: 3.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 11 IVSSIGNNQQEVLASLREGRSGI--------TFSQELKDSGMRSHVWGNVKLDTTGLIDRKVV--------RFMSDASIY 74
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIrkltefpkFLPDCIPEQKALENLVAAMPCQIAAEVDQSEFdpsdfaptKRESRATHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 75 AFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFqVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHG 154
Cdd:PTZ00050 81 AMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLAD-LTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 155 VNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEelcwemAC-------EFDAMGALSTKYNDTPEKASRTYDAHRD 227
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTE------ASitpvsfaGFSRMRALCTKYNDDPQRASRPFDKDRA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 228 GFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAP--SGEGAVRCMKMAM-HGVDTP---IDYLNSHGTS 301
Cdd:PTZ00050 234 GFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPhpDGRGARRCMENALkDGANINindVDYVNAHATS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 302 TPVGDVKELAAIREVFGD---KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAgLNIVTETT 378
Cdd:PTZ00050 314 TPIGDKIELKAIKKVFGDsgaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD-LNLVQGKT 392
|
410 420
....*....|....*....|....*...
gi 16130258 379 DRELTT---VMSNSFGFGGTNATLVMRK 403
Cdd:PTZ00050 393 AHPLQSidaVLSTSFGFGGVNTALLFTK 420
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-404 |
5.24e-99 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 300.88 E-value: 5.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSM 79
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITdFDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 80 EQAIADAGLSPEAYqNNPRVGLIAGSG-GGSPRFQ---VFGADamRGPRglkAVGPYVVTKAMASGVSACLATPFKIHGV 155
Cdd:PRK08439 81 REAMKDAGFLPEEL-DAERFGVSSASGiGGLPNIEknsIICFE--KGPR---KISPFFIPSALVNMLGGFISIEHGLKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 156 NYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEE-LCWEMACEFDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGG 234
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESaICPVGIGGFAAMKALSTR-NDDPKKASRPFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 235 GGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTP-IDYLNSHGTSTPVGDVKELAAI 313
Cdd:PRK08439 234 AGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAGNPkIDYINAHGTSTPYNDKNETAAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 314 REVFGDKS--PAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQaAGLNIVTETTDR-ELTTVMSNSF 390
Cdd:PRK08439 314 KELFGSKEkvPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPE-CDLDYIPNVARKaELNVVMSNSF 392
|
410
....*....|....
gi 16130258 391 GFGGTNATLVMRKL 404
Cdd:PRK08439 393 GFGGTNGVVIFKKV 406
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-402 |
3.78e-96 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 293.43 E-value: 3.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQEL-KDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLS 78
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWdRYDGLNTRLAAPIDdFELPAHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 79 MEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPR-FQVFGADAMRGP-RGLKAVGpYVvtKAMASGVSACLATPFKIHGVN 156
Cdd:PRK09116 81 SELALEDAGLLGDPILTDGRMGIAYGSSTGSTDpIGAFGTMLLEGSmSGITATT-YV--RMMPHTTAVNVGLFFGLKGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 157 YSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGGGG 236
Cdd:PRK09116 158 IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTR-NDAPELTPRPFDANRDGLVIGEGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 237 MVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTP---IDYLNSHGTSTPVGDVKELAAI 313
Cdd:PRK09116 237 TLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLApedIGYVNAHGTATDRGDIAESQAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 314 REVFGDKSPaISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTdRELTT--VMSNSFG 391
Cdd:PRK09116 317 AAVFGARMP-ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEA-REIDTeyVMSNNFA 394
|
410
....*....|.
gi 16130258 392 FGGTNATLVMR 402
Cdd:PRK09116 395 FGGINTSLIFK 405
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-400 |
5.53e-90 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 278.60 E-value: 5.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGI-TFSQE-LK----DSGMRSHVWGNVKLDTTGLI--------------- 60
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVrALTQDdLKmkseDEETQLYTLDQLPSRVAALVprgtgpgdfdeelwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 61 -DRKVVRFMSdasiYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRfQVFGADAMRGPRGLKAVGPYVVTKAMA 139
Cdd:PLN02836 86 nSRSSSRFIG----YALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSIT-DILEAAQLICEKRLRRLSPFFVPRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 140 SGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTKYNDTPEKA 218
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAgFSRSRALSTKFNSCPTEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 219 SRTYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMHGVD---TPID 293
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHedGRGAVLAMTRALQQSGlhpNQVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 294 YLNSHGTSTPVGDVKELAAIREVFGDKSP----AISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQ-A 368
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFSEHATsgglAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIfD 400
|
410 420 430
....*....|....*....|....*....|..
gi 16130258 369 AGLNIVTETTDRELTTVMSNSFGFGGTNATLV 400
Cdd:PLN02836 401 DGFVPLTASKAMLIRAALSNSFGFGGTNASLL 432
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-404 |
1.82e-76 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 242.99 E-value: 1.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKdFNCEEYMSKKDARKMDLFIQYGIAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAyQNNPRVGLIAGSGGGSPRFQVFGADAM--RGPRglkAVGPYVVTKAMASGVSACLATPFKIHGVNYS 158
Cdd:PRK08722 84 QALDDSGLEVTE-ENAHRIGVAIGSGIGGLGLIEAGHQALveKGPR---KVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 159 ISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGGGGM 237
Cdd:PRK08722 160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAgFGAAKALSTR-NDEPQKASRPWDKDRDGFVLGDGAGM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 238 VVVEELEHALARGAHIYAEIVGYGATSDGADMVAPS--GEGAVRCMKMAMHGVD---TPIDYLNSHGTSTPVGDVKELAA 312
Cdd:PRK08722 239 MVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSedGSGGALAMEAAMRDAGvtgEQIGYVNAHGTSTPAGDVAEIKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 313 IREVFGD---KSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVTETTDR--ELTTVMS 387
Cdd:PRK08722 319 IKRALGEagsKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEE-GLDIDLVPHTARKveSMEYAIC 397
|
410
....*....|....*..
gi 16130258 388 NSFGFGGTNATLVMRKL 404
Cdd:PRK08722 398 NSFGFGGTNGSLIFKKM 414
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-400 |
3.72e-73 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 237.95 E-value: 3.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKsFSTDGWVAPKLSKRMDKFMLYLLTAGK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYQ--NNPRVGLIAGSGGGSprFQVFGaDAMRGPR-GLKAVGPYVVTKAMASGVSACLATPFKIHGVNY 157
Cdd:PLN02787 209 KALADGGITEDVMKelDKTKCGVLIGSAMGG--MKVFN-DAIEALRiSYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNY 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 158 SISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTKyNDTPEKASRTYDAHRDGFVIAGGGG 236
Cdd:PLN02787 286 SISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGgFVACRALSQR-NDDPTKASRPWDMNRDGFVMGEGAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 237 MVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGA--VRCMK--MAMHGVD-TPIDYLNSHGTSTPVGDVKELA 311
Cdd:PLN02787 365 VLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAgvILCIEkaLAQSGVSkEDVNYINAHATSTKAGDLKEYQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 312 AIREVFGDKSP-AISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDR-ELTTVMSNS 389
Cdd:PLN02787 445 ALMRCFGQNPElRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALSNS 524
|
410
....*....|.
gi 16130258 390 FGFGGTNATLV 400
Cdd:PLN02787 525 FGFGGHNSSIL 535
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
5-400 |
6.16e-72 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 231.54 E-value: 6.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 5 VITGLGIVSSIGNNQQEVLASLREGRSGI-----TFSQELkDSGMRshVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSM 79
Cdd:PRK07910 15 VVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEF-DLPVR--IGGHLLEEFDHQLTRVELRRMSYLQRMSTVLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 80 EQAIADAGlSPEAYQNnpRVGLIAGSGGGSPRFQVFGADAMRGpRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSI 159
Cdd:PRK07910 92 RRVWENAG-SPEVDTN--RLMVSIGTGLGSAEELVFAYDDMRA-RGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 160 SSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMA-CEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMV 238
Cdd:PRK07910 168 VSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPiAGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 239 VVEELEHALARGAHIYAEIVGYGATSDGADMVA--PSGEGAVRCMKMAMH--GVD-TPIDYLNSHGTSTPVGDVKELAAI 313
Cdd:PRK07910 248 VIETEEHAKARGANILARIMGASITSDGFHMVApdPNGERAGHAMTRAIElaGLTpGDIDHVNAHATGTSVGDVAEGKAI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 314 REVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQaAGLNIVT-ETTDRELTTVMSNSFGF 392
Cdd:PRK07910 328 NNALGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPE-IDLDVVAgEPRPGNYRYAINNSFGF 406
|
....*...
gi 16130258 393 GGTNATLV 400
Cdd:PRK07910 407 GGHNVALA 414
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
94-406 |
7.80e-69 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 221.14 E-value: 7.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 94 QNNPRVGLIAGSG-GGSPRFqvfgADAMR--GPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCI 170
Cdd:PRK14691 23 EKQERTATIIGAGiGGFPAI----AHAVRtsDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 171 GNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALAR 249
Cdd:PRK14691 99 GDAVRMIRNNEADVALCGGAEAVIDTVSLAgFAAARALSTHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 250 GAHIYAEIVGYGATSDGADMV--APSGEGAVRCMKMAMHGVD-TP--IDYLNSHGTSTPVGDVKELAAIREVFGDKSP-A 323
Cdd:PRK14691 179 GAKPLAEIVGYGTSADAYHMTsgAEDGDGAYRAMKIALRQAGiTPeqVQHLNAHATSTPVGDLGEINAIKHLFGESNAlA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 324 ISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVT-ETTDRELTTVMSNSFGFGGTNATLVMR 402
Cdd:PRK14691 259 ITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAgNAQPHDMTYALSNGFGFAGVNASILLK 338
|
....
gi 16130258 403 KLKD 406
Cdd:PRK14691 339 RWVD 342
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
71-401 |
1.80e-68 |
|
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: 216.93 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 71 ASIYAFLSMEQAIADAGLSpeayqNNPRVGLIAGSGGGSPRFqvfgadamrgprglkavgpyvvtkamaSGVSACLATPF 150
Cdd:cd00327 7 ASELGFEAAEQAIADAGLS-----KGPIVGVIVGTTGGSGEF---------------------------SGAAGQLAYHL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 151 KI-HGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEElcwemacefdamgalstkyndtpekasrtydahrdgF 229
Cdd:cd00327 55 GIsGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------F 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 230 VIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMV-APSGEGAVRCMKMAMHGV---DTPIDYLNSHGTSTPVG 305
Cdd:cd00327 99 VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVpAVSGEGLARAARKALEGAgltPSDIDYVEAHGTGTPIG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 306 DVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPsinieeldeqaaglnivtetTDRELTTV 385
Cdd:cd00327 179 DAVELALGLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP--------------------TPREPRTV 238
|
330
....*....|....*.
gi 16130258 386 MSNSFGFGGTNATLVM 401
Cdd:cd00327 239 LLLGFGLGGTNAAVVL 254
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-403 |
6.50e-67 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 217.98 E-value: 6.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSGItfsQELKDSGMRSHVWGNVKLDTTGL------------IDRKVVRFM 68
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAF---GVMRRPGRQVPDDAGAGLASAFIgaeldslalperLDAKLLRRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 69 SDASIYAFLSMEQAIADAGLSPEayqNNPRVGLIAGSGGGSPRFQVFGADAMRG-PRGLKavgPYVVTKAMASGVSACLA 147
Cdd:PRK07103 78 SLSAQAALAAAREAWRDAALGPV---DPDRIGLVVGGSNLQQREQALVHETYRDrPAFLR---PSYGLSFMDTDLVGLCS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 148 TPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE-FDAMGALST-KYNDTPEKASRTYDAH 225
Cdd:PRK07103 152 EQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQaLRSLGAMGSdRFADEPEAACRPFDQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 226 RDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTP---IDYLNSHGTST 302
Cdd:PRK07103 232 RDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAGLGpedIDYVNPHGTGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 303 PVGDVKELAAIREVfGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEE-LDEQaagLNIVTETTDR- 380
Cdd:PRK07103 312 PLGDETELAALFAS-GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDER---FRWVGSTAESa 387
|
410 420
....*....|....*....|...
gi 16130258 381 ELTTVMSNSFGFGGTNATLVMRK 403
Cdd:PRK07103 388 RIRYALSLSFGFGGINTALVLER 410
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-401 |
1.06e-66 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 217.96 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 5 VITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDttglIDRKVVRFMSDAsiYAFLSMEQAI 83
Cdd:PRK06501 14 AVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDfLP----ESPFGASALSEA--LARLAAEEAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 84 ADAGLS-------------PEAYQNNPRVGLIAGSGGGSPrfqVFGADAMRGPRGLKAvgPYVVTKAMASGVSACLATPF 150
Cdd:PRK06501 88 AQAGIGkgdfpgplflaapPVELEWPARFALAAAVGDNDA---PSYDRLLRAARGGRF--DALHERFQFGSIADRLADRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 151 KIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGE-ELCWEMACEFDAMGALSTKyNDTPEKASRTYDAHRDGF 229
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgSVSAEALIRFSLLSALSTQ-NDPPEKASKPFSKDRDGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 230 VIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMV--APSGEGAVRCMKMAMH--GVD-TPIDYLNSHGTSTPV 304
Cdd:PRK06501 242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTrsSPDGSPAIGAIRAALAdaGLTpEQIDYINAHGTSTPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 305 GDVKELAAIREVFGDKSPAI--SATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVTETT-DRE 381
Cdd:PRK06501 322 NDKMEYLGLSAVFGERLASIpvSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDP-AIPLDVVPNVArDAR 400
|
410 420
....*....|....*....|
gi 16130258 382 LTTVMSNSFGFGGTNATLVM 401
Cdd:PRK06501 401 VTAVLSNSFGFGGQNASLVL 420
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
81-401 |
1.82e-58 |
|
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: 196.24 E-value: 1.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYQNnPRVGLIAGSGGGSPRFQVFgadamrgpRGLKAVGPYVVT---KAMASG-VSAClatpFKIHGVN 156
Cdd:cd00833 97 EALEDAGYSPESLAG-SRTGVFVGASSSDYLELLA--------RDPDEIDAYAATgtsRAFLANrISYF----FDLRGPS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 157 YSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCW-EMACEFDAMGALStkyndtPEKASRTYDAHRDGFVIAGGG 235
Cdd:cd00833 164 LTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSpDMFVGFSKAGMLS------PDGRCRPFDADADGYVRGEGV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 236 GMVVVEELEHALARGAHIYAEIVGYGATSDGAD--MVAPSGEGAVRCMKMAMH--GVDtP--IDYLNSHGTSTPVGDVKE 309
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTkgITAPSGEAQAALIRRAYAraGVD-PsdIDYVEAHGTGTPLGDPIE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 310 LAAIREVFGDKSP-----AISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEE----LDEQAAGLNIVTETTDR 380
Cdd:cd00833 317 VEALAKVFGGSRSadqplLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETpnpkIDFEESPLRVPTEARPW 396
|
330 340
....*....|....*....|....*
gi 16130258 381 ELTTVMS----NSFGFGGTNATLVM 401
Cdd:cd00833 397 PAPAGPRragvSSFGFGGTNAHVIL 421
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-401 |
1.95e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 187.74 E-value: 1.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNNQQEVLASLREGRSgitfsqelkdSGMRSHVWGNVKLDTT--GLIDRKVVRFMSDASIY---- 74
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRA----------SGMRPCDFWLVDLPTWvgEVVGVELPALPAALAAFdcrn 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 75 ------AFLSMEQAIADAglspEAYQNNPRVGLIAG---SGGGSprfqvfGADAMRGPRGLKAVGP--YVVTKAMASGVS 143
Cdd:PRK09185 71 nrlallALQQIEPAVEAA----IARYGADRIGVVLGtstSGILE------GELAYRRRDPAHGALPadYHYAQQELGSLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 144 ACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCwEMACE-FDAMGALStkynDTPekaSRTY 222
Cdd:PRK09185 141 DFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLC-RLTLNgFNSLESLS----PQP---CRPF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 223 DAHRDGFVIAGGGGMVVVE-ELEHALArgahiyaeIVGYGATSDGADMVAP--SGEGAVRCMKMA--MHGVDT-PIDYLN 296
Cdd:PRK09185 213 SANRDGINIGEAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPhpEGLGAILAMQQAlaDAGLAPaDIGYIN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 297 SHGTSTPVGDVKELAAIREVFGDKSPAiSATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTE 376
Cdd:PRK09185 285 LHGTATPLNDAMESRAVAAVFGDGVPC-SSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVEN 363
|
410 420
....*....|....*....|....*
gi 16130258 377 TTDRELTTVMSNSFGFGGTNATLVM 401
Cdd:PRK09185 364 AQALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-403 |
8.28e-51 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 175.24 E-value: 8.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 1 MKRAVITGLGIVSSIGNnQQEVLASLREGRSGITFSQ---ELKDSGMrshvwgnvkldttGLIDRKVvrfmSDASIYAFL 77
Cdd:PRK05952 1 MMKVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQpfpELPPLPL-------------GLIGNQP----SSLEDLTKT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 78 SMEQAIADAGLSPEAyqnnPRVGLIAGS-----------------GGGSPRFQVFGAD---------AMRGPRGLKAVGP 131
Cdd:PRK05952 63 VVTAALKDAGLTPPL----TDCGVVIGSsrgcqgqweklarqmyqGDDSPDEELDLENwldtlphqaAIAAARQIGTQGP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 132 yvVTKAMAsgvsaclatpfkihgvnysissACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMA-CEFDAMGALSTk 210
Cdd:PRK05952 139 --VLAPMA----------------------ACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTlAGFQQMGALAK- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 211 yndtpekaSRTY--DAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEG--AVRCMKMAMH 286
Cdd:PRK05952 194 --------TGAYpfDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGksAIAAIQQCLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 287 GVD-TP--IDYLNSHGTSTPVGDVKELAAIREVFGDKsPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEE 363
Cdd:PRK05952 266 RSGlTPedIDYIHAHGTATRLNDQREANLIQALFPHR-VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE 344
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16130258 364 LDEQaagLNIVTETTDRELTTVMSNSFGFGGTNATLVMRK 403
Cdd:PRK05952 345 PEFD---LNFVRQAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-401 |
4.50e-41 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 155.42 E-value: 4.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYQNNpRVGLIAGSGGGSPrfqvfgadAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS 160
Cdd:COG3321 101 EALEDAGYDPESLAGS-RTGVFVGASSNDY--------ALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGgeelcwemAC---------EFDAMGALStkyndtPEKASRTYDAHRDGFVI 231
Cdd:COG3321 172 TACSSSLVAVHLACQSLRSGECDLALAGG--------VNlmltpesfiLFSKGGMLS------PDGRCRAFDADADGYVR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 232 AGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGAD--MVAPSGEGAVRCMKMAMH--GVDtP--IDYLNSHGTSTPVG 305
Cdd:COG3321 238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALAdaGVD-PatVDYVEAHGTGTPLG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 306 DVKELAAIREVFGDKSP-----AISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEE----LDEQAAGLNIVTE 376
Cdd:COG3321 317 DPIEAAALTAAFGQGRPadqpcAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETpnphIDFENSPFYVNTE 396
|
330 340 350
....*....|....*....|....*....|.
gi 16130258 377 TTDRELTT------VmsNSFGFGGTNATLVM 401
Cdd:COG3321 397 LRPWPAGGgprragV--SSFGFGGTNAHVVL 425
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
254-362 |
1.60e-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: 131.92 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 254 YAEIVGYGATSDGADMV--APSGEGAVRCMKMAMHGVDTP---IDYLNSHGTSTPVGDVKELAAIREVFGDKSP----AI 324
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGltAPNGEGQARAIRRALADAGVDpedVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130258 325 SATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIE 362
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-246 |
1.46e-34 |
|
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: 128.52 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGIT-FSQELKD----SGMRSHVWGNVKLDTTGL------------IDRKV 64
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeIPADRWDpdklYDPPSRIAGKIYTKWGGLddifdfdplffgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 65 VRFMSDASIYAFLSMEQAIADAGLSPEAYqNNPRVGLIAGSGGGSPRfqvfGADAMRGPRGLKAVGPYVVTkAMASGVSA 144
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSL-DGSRTGVFIGSGIGDYA----ALLLLDEDGGPRRGSPFAVG-TMPSVIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 145 CLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGE-ELCWEMACEFDAMGALSTkynDTPEKASRTYD 223
Cdd:pfam00109 155 RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSP---DGPCKAFDPFA 231
|
250 260
....*....|....*....|...
gi 16130258 224 ahrDGFVIAGGGGMVVVEELEHA 246
Cdd:pfam00109 232 ---DGFVRGEGVGAVVLKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-400 |
4.85e-32 |
|
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: 125.17 E-value: 4.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 2 KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVK-LDTTGLIDRKVVRFMSDASIYAFLSME 80
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPdFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 81 QAIADAGLSPEAYQNNpRVGLIAGSGGGSPRFqvfgadamrGPRGLKAV---GPYVVTkAMASGVSACLATPFKI---HG 154
Cdd:cd00832 81 WALADAGVDPAALPPY-DMGVVTASAAGGFEF---------GQRELQKLwskGPRHVS-AYQSFAWFYAVNTGQIsirHG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 155 VNYSISSACATSA---HCIGNAVEQIQLGKQDIVFAGGGEELC-WEMACEFdAMGALSTkyNDTPEKASRTYDAHRDGFV 230
Cdd:cd00832 150 MRGPSGVVVAEQAgglDALAQARRLVRRGTPLVVSGGVDSALCpWGWVAQL-SSGRLST--SDDPARAYLPFDAAAAGYV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 231 IAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMvAPSGEGAVRCMKMAM--HGVdTP--IDYLNSHGTSTPVGD 306
Cdd:cd00832 227 PGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG-SGRPPGLARAIRLALadAGL-TPedVDVVFADAAGVPELD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 307 VKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEqAAGLNIVTETTDR-ELTTV 385
Cdd:cd00832 305 RAEAAALAAVFGPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPP-AYGLDLVTGRPRPaALRTA 383
|
410
....*....|....*
gi 16130258 386 MSNSFGFGGTNATLV 400
Cdd:cd00832 384 LVLARGRGGFNSALV 398
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
80-401 |
1.51e-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: 106.63 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 80 EQAIADAGLsPEAYQNNpRVGLIAGSGGGSPRFQVFGAdAMRGP---RGLKAVGPYVVTKAM------------------ 138
Cdd:TIGR02813 102 KEVLNDAGL-PDGYDRD-KIGITLGVGGGQKQSSSLNA-RLQYPvlkKVFKASGVEDEDSEMlikkfqdqyihweensfp 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 139 ---ASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGgeeLCWE----MACEFDAMGALSTKY 211
Cdd:TIGR02813 179 gslGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDnspfMYMSFSKTPAFTTNE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 212 NDTPekasrtYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDG--ADMVAPSGEGAVRCMKMAMH--G 287
Cdd:TIGR02813 256 DIQP------FDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQAKALKRAYDdaG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 288 VDT-PIDYLNSHGTSTPVGDVKELAAIREVFGDKSP-----AISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINI 361
Cdd:TIGR02813 330 FAPhTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDqkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINV 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16130258 362 EE----LDEQAAGLNIVTET---TDRELTTVMS---NSFGFGGTNATLVM 401
Cdd:TIGR02813 410 DQpnpkLDIENSPFYLNTETrpwMQREDGTPRRagiSSFGFGGTNFHMVL 459
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
157-401 |
2.11e-24 |
|
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: 102.02 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 157 YSIS--SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCW-EMACEFDAMGALStkyndtPEKASRTYDAHRDGFVIAG 233
Cdd:smart00825 89 YSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNLILSpDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 234 GGGMVVVEELEHALARGAHIYAEIVGYGATSDGAD--MVAPSGEGAVrcmkmamhgvdtpidylnshgtstpvgdvkela 311
Cdd:smart00825 163 GVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPAQL--------------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 312 airevfgdkspAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEEL----DEQAAGLNIVTETTDRELTT--- 384
Cdd:smart00825 210 -----------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPnphiDLEESPLRVPTELTPWPPPGrpr 278
|
250
....*....|....*...
gi 16130258 385 -VMSNSFGFGGTNATLVM 401
Cdd:smart00825 279 rAGVSSFGFGGTNAHVIL 296
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
146-191 |
2.22e-04 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 43.05 E-value: 2.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16130258 146 LATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGE 191
Cdd:PRK08963 74 LGTGMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGAD 119
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
162-259 |
9.77e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 41.09 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 162 ACATSAhcIGNAVEQIQLGKQDIVFAGG---GEELCWEMACEFdamGALSTKYNDTPEKASRTYDAhrDGFVIAGGGGMV 238
Cdd:PRK06519 176 SAGVSA--IEIAFARIASGQSDHALVGGaynAERPDMLLLYEL---GGLLLKGGWAPVWSRGGEDG--GGFILGSGGAFL 248
|
90 100
....*....|....*....|.
gi 16130258 239 VVEELEHALARGAHIYAEIVG 259
Cdd:PRK06519 249 VLESREHAEARGARPYARISG 269
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
357-402 |
1.24e-03 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 38.29 E-value: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16130258 357 PSINIEELDEqaAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMR 402
Cdd:pfam16197 1 PNPDIPALLD--GRLKVVTEPTPWPGGIVGVNSFGFGGANAHVILK 44
|
|
| FabG2 |
COG4982 |
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and ... |
161-250 |
5.15e-03 |
|
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and metabolism];
Pssm-ID: 444006 [Multi-domain] Cd Length: 3088 Bit Score: 39.28 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130258 161 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALStkynDTPEKA---------SRTYDAHRDGFVI 231
Cdd:COG4982 2729 AACATAAVSVEEGVDKIRLGKADFVVAGGIDDIGVESITGFGDMNATA----DSEEMLakgiddrffSRANDRRRGGFVE 2804
|
90
....*....|....*....
gi 16130258 232 AGGGGMVVveelehaLARG 250
Cdd:COG4982 2805 AQGGGTIL-------LARG 2816
|
|
| |
