|
Name |
Accession |
Description |
Interval |
E-value |
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
36-394 |
2.99e-89 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 272.37 E-value: 2.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPERTRDVADAERDLHRRNPKVAPRlpmvsrlTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDL 115
Cdd:COG0332 3 VRILGTGSYLPERVVTNDDLEKRLDTSDEWIEER-------TGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 116 LIFASATQDMIEPATSHITAAKLG-VRAPVMDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvpDRRT 194
Cdd:COG0332 76 IIVATVTPDYLFPSTACLVQHKLGaKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWT--DRST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 195 YamsaagYTMSDAGAAVLVEatgagsgtggadafeddlaaelarlvePTDRPSGILASAFTAESQHWDVGMLPSGGTVNP 274
Cdd:COG0332 154 C------VLFGDGAGAVVLE---------------------------ASEEGPGILGSVLGSDGSGADLLVVPAGGSRNP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 275 R---DPERSYFEIDGSRLREAFLALGPGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADHGN 351
Cdd:COG0332 201 PspvDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGN 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2267659504 352 IASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVRW 394
Cdd:COG0332 281 TSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAVLRW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
36-392 |
9.64e-74 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 232.43 E-value: 9.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPERTRDVADAERDLHrrnpkvAPRLPMVSRlTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDL 115
Cdd:cd00830 2 ARILGIGSYLPERVVTNDELEKRLD------TSDEWIRTR-TGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 116 LIFASATQDMIEPATSHITAAKLGVR-APVMDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvpDRRT 194
Cdd:cd00830 75 IIVATSTPDYLFPATACLVQARLGAKnAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWT--DRST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 195 YAMSAAGytmsdAGAAVLveatgagsgtggadafeddlaaelarlvEPTDRPSGILASAFTAESQHWDVGMLPSGGTVNP 274
Cdd:cd00830 153 AVLFGDG-----AGAVVL----------------------------EATEEDPGILDSVLGSDGSGADLLTIPAGGSRSP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 275 RDPERS---YFEIDGSRLREAFLALGPGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADHGN 351
Cdd:cd00830 200 FEDAEGgdpYLVMDGREVFKFAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGN 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2267659504 352 IASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVV 392
Cdd:cd00830 280 TSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
36-394 |
1.60e-53 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 179.88 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPERTRDVADAERdlhrrnpkvaprlpMV--------SRlTGVRRVHVADDDQQASDLAVAASRTVLDRAG 107
Cdd:PRK09352 4 AKILGTGSYLPERVVTNDDLEK--------------MVdtsdewivTR-TGIKERRIAAPDETTSDLATEAAKKALEAAG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 108 LRPQDVDLLIFASATQDMIEPATSHITAAKLGVR-APVMDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVR 186
Cdd:PRK09352 69 IDPEDIDLIIVATTTPDYAFPSTACLVQARLGAKnAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 187 WDvpDRRTYAMSAAGytmsdAGAAVLveatgagsgtggadafeddlaaelarlvEPTDRPsGILASAFTAESQHWDVGML 266
Cdd:PRK09352 149 WT--DRSTCVLFGDG-----AGAVVL----------------------------GASEEP-GILSTHLGSDGSYGDLLYL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 267 PSGGTVNPrdPERSYFEIDGsrlREAF-LALG--PGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTI 343
Cdd:PRK09352 193 PGGGSRGP--ASPGYLRMEG---REVFkFAVRelAKVAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVV 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2267659504 344 VTVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVRW 394
Cdd:PRK09352 268 VTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRW 318
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
36-394 |
2.51e-48 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 166.58 E-value: 2.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPERTRDVADAERDLHRRNPKVAPRlpmvsrlTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDL 115
Cdd:PRK12879 5 ARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQR-------TGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 116 LIFASATQDMIEPATSHITAAKLGVR-APVMDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvpDRRT 194
Cdd:PRK12879 78 IIVATTTPDYLFPSTASQVQARLGIPnAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYT--DRTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 195 YAMSAAGytmsdAGAAVlveatgagsgtggadafeddlaaelarlVEPTDRPSGILASAFTAESQHWDVGMLPSGGTVNP 274
Cdd:PRK12879 156 CILFGDG-----AGAVV----------------------------LEATENEPGFIDYVLGTDGDGGDILYRTGLGTTMD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 275 RDPE--RSYFEIDGsrlREAF---LALGPGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADH 349
Cdd:PRK12879 203 RDALsgDGYIVQNG---REVFkwaVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYY 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2267659504 350 GNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVRW 394
Cdd:PRK12879 280 GNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLVKW 324
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
69-394 |
3.05e-36 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 135.01 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 69 RLPM--VSRLTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAKLGV--RAPV 144
Cdd:PRK09258 37 RLPPgqLEALTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGLpkSCAN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 145 MDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGV-----RWDVPD--RRTYAMSAAGYTMSDAGAAVLveatg 217
Cdd:PRK09258 117 FDVSNACLGFLNGMLDAANMIELGQIDYALVVSGESAREIVeatidRLLAPEttREDFAQSFATLTLGSGAAAAV----- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 218 agsgtggadafeddlaaeLARLVEPTDRPSgILASAFTAESQHWDvgmLPSGGtvnprdpeRSYFEIDGSRLREAFLALG 297
Cdd:PRK09258 192 ------------------LTRGSLHPRGHR-LLGGVTRAATEHHE---LCQGG--------RDGMRTDAVGLLKEGVELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 298 PGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADHGNIASATLPLQLATALESGRLRRGDVVL 377
Cdd:PRK09258 242 VDTWEAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVA 321
|
330
....*....|....*..
gi 2267659504 378 LLGLAGGISMGAMVVRW 394
Cdd:PRK09258 322 LLGIGSGLNCSMLEVKW 338
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
34-394 |
1.33e-34 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 130.34 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 34 PVARIVDVAVHLPERTRDVADAERDLHRRNPKVAPRLPMVSRltgvrrvHVADDdQQASDLAVAASRTVLDRAGLRPQDV 113
Cdd:PRK07204 3 RYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTR-------HFVDG-ETSSYMGAEAAKKAVEDAKLTLDDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 114 DLLIFASATQDMIEPATSHITAAKLGVRA---PVMDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvp 190
Cdd:PRK07204 75 DCIICASGTIQQAIPCTASLIQEQLGLQHsgiPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWG-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 191 DRRTYAMsaagytMSDAGAAVLVEAtgagsgtggadafeddlaaelarlvepTDRPSGILASAFTAESQHWDVGMLPSGG 270
Cdd:PRK07204 153 QNESCIL------FGDGAAAVVITK---------------------------GDHSSRILASHMETYSSGAHLSEIRGGG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 271 T-VNPRDP-----ERSYFEIDGSRLREAFLALGPGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIV 344
Cdd:PRK07204 200 TmIHPREYseerkEDFLFDMNGRAIFKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVT 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2267659504 345 TVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVRW 394
Cdd:PRK07204 280 IFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSIGGILLEY 329
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
36-392 |
1.50e-33 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 127.55 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPERTRDVADAERdlhrrnpkvAPRLPMVSRLTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDL 115
Cdd:cd00827 2 VGIEAIGAYLPRYRVDNEELAE---------GLGVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 116 LIFASATQDMIEPATSHITAAKLG-VRAPVMDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGemptrgvrwDVPDRRT 194
Cdd:cd00827 73 LIVATESPIDKGKSAATYLAELLGlTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVAS---------DIASYLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 195 YAMSAAGYTMSDAGAAVLVEatgagsgtggadafeddlaaelarlVEPTDRPSGILASAFTAE-SQHWDVGMLPSGGTVN 273
Cdd:cd00827 144 DEGSALEPTLGDGAAAMLVS-------------------------RNPGILAAGIVSTHSTSDpGYDFSPYPVMDGGYPK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 274 PRDPERSYF---EIDGSRLREAFLALGPGPVGQALDQAGVTmDDVALVAVHQV-AVGYLEDVHRALGVPADRTIVT---- 345
Cdd:cd00827 199 PCKLAYAIRltaEPAGRAVFEAAHKLIAKVVRKALDRAGLS-EDIDYFVPHQPnGKKILEAVAKKLGGPPEKASQTrwil 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2267659504 346 VADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVV 392
Cdd:cd00827 278 LRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTAEAFVL 324
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
37-394 |
2.01e-30 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 119.05 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 37 RIVDVAVHLPERTRDVADAERDLhrrnpkvAPRLPMVSRLTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDLL 116
Cdd:PRK05963 5 RIAGFGHAVPDRRVENAEIEAQL-------GLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 117 IFASATQDMIEPATSHITAAKLGV-RAPVMDVKNACNSVLNGIEVAEALIGTGRyRRVLVACGEMPTRgvRWDVPDRRTY 195
Cdd:PRK05963 78 LLATSTPDHLLPPSAPLLAHRLGLqNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSR--RINMAERASA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 196 AMSAagytmsDAGAAVLVEatgagsgtggadafeddlaaelarlvePTDRP-SGILASAFTAESQHWDVGMLPSGGTVNP 274
Cdd:PRK05963 155 VLFA------DAAGAVVLA---------------------------PSAKAnSGVLGSQLISDGSHYDLIKIPAGGSARP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 275 ----RDPERSYFEI-DGSRLREAFLALGPGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADH 349
Cdd:PRK05963 202 fapeRDASEFLMTMqDGRAVFTEAVRMMSGASQNVLASAAMTPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETY 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2267659504 350 GNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVRW 394
Cdd:PRK05963 282 GNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVMRV 326
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
77-394 |
9.75e-28 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 112.52 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 77 TGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAkLGVRAPV-MDVKNACNSVL 155
Cdd:PLN02326 82 TGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSSPDDLFGSAPQVQAA-LGCTNALaFDLTAACSGFV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 156 NGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvpDRRTYAMsaagytMSDAGAAVLVEATGagsgtggadafeDDLAAE 235
Cdd:PLN02326 161 LGLVTAARFIRGGGYKNVLVIGADALSRYVDWT--DRGTCIL------FGDGAGAVVLQACD------------DDEDGL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 236 LARLVEPTDRPSGILASAFTAESQHWDVGMLPSGGTVNPRDPERSYFEIDGsrlREAF---LALGPGPVGQALDQAGVTM 312
Cdd:PLN02326 221 LGFDMHSDGNGHKHLHATFKGEDDDSSGGNTNGVGDFPPKKASYSCIQMNG---KEVFkfaVRCVPQVIESALQKAGLTA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 313 DDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVV 392
Cdd:PLN02326 298 ESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGFGAGLTWGSAIV 377
|
..
gi 2267659504 393 RW 394
Cdd:PLN02326 378 RW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
73-394 |
2.80e-27 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 110.42 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 73 VSRLTGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAKLGVRAPVMDVKNACN 152
Cdd:CHL00203 33 ISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDLFGSASQLQAEIGATRAVAFDITAACS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 153 SVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvpDRRTYAMSAAGytmsdAGAAVLVEATGAGSGTggadaFEDDL 232
Cdd:CHL00203 113 GFILALVTATQFIQNGSYKNILVVGADTLSKWIDWS--DRKTCILFGDG-----AGAAIIGASYENSILG-----FKLCT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 233 AAELARLVEPTDRPSgilasaftaESQHWDVGMLPSGgtvnprdpERSYFEIDGSRLREAFLALGPGPVGQALDQAGVTM 312
Cdd:CHL00203 181 DGKLNSHLQLMNKPV---------NNQSFGTTKLPQG--------QYQSISMNGKEVYKFAVFQVPAVIIKCLNALNISI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 313 DDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVV 392
Cdd:CHL00203 244 DEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWGAIVL 323
|
..
gi 2267659504 393 RW 394
Cdd:CHL00203 324 KW 325
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
305-394 |
1.40e-25 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 99.11 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 305 LDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVPADRTIVTVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGG 384
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 2267659504 385 ISMGAMVVRW 394
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
33-394 |
5.49e-21 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 92.76 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 33 RPVARIVDVAVHLPERtrdVADAERDLHRRNpkvAPRLPMVSRLtGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQD 112
Cdd:PRK06840 2 EMNVGIVGTGVYLPKD---VMTAEEIAEKTG---IPEEVVIEKF-GIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 113 VDLLI-FASATQDMIEPATSHITAAKLGV-RAPVMDVKNACNSVLNGIEVAEALIGT-GRYRRVLVACGEMPTRGVRWDV 189
Cdd:PRK06840 75 IDVVIyIGSEHKDYPVWSSAPKIQHEIGAkNAWAFDIMAVCASFPIALKVAKDLLYSdPSIENVLLVGGYRNSDLVDYDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 190 PdrRTYAMsaagYTMSDAGAAVLveatgagsgtggadafeddLAAELARLVeptdrpsgILASAF-TAESQHWDVGMlPS 268
Cdd:PRK06840 155 P--RTRFM----FNFAAGGSAAL-------------------LKKDAGKNR--------ILGSAIiTDGSFSEDVRV-PA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 269 GGTVNPRDPE---RSYFEID-------GSRLREAFLALGPGPVGQALDQAGVTMDDVALVAVHQVAVGYLEDVHRALGVP 338
Cdd:PRK06840 201 GGTKQPASPEtveNRQHYLDvidpesmKERLDEVSIPNFLKVIREALRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLT 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2267659504 339 ADRTIVtVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVRW 394
Cdd:PRK06840 281 EEQAIY-LDEYGHLGQLDQILSLHLALEQGKLKDGDLVVLVSAGTGYTWAATVIRW 335
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
36-394 |
4.02e-12 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 66.70 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPE---RTRDVADAERDLHRRNPKVAPRLPMVSRLTGVRRVH-VADDD----------------QQASDLA 95
Cdd:COG3424 2 ARILSIATAVPPhryTQEEIAEFAAELFGLDERDRRRLRRLFENSGIETRHsVLPLEwyleppsfgernalyiEEALELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 96 VAASRTVLDRAGLRPQDVDLLIFASATQDMIePATSHITAAKLG-----VRAPV--MdvknACNSVLNGIEVAEALIGTG 168
Cdd:COG3424 82 EEAARRALDKAGLDPEDIDHLVTVSCTGFAA-PGLDARLINRLGlrpdvRRLPVggM----GCAAGAAGLRRAADFLRAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 169 RYRRVLVACGEMPTRGVRWDVPDRRTyAMSAAGYtmSDAGAAVLVEAtgagsgtggadafeDDLAAELARLVEptdrpsg 248
Cdd:COG3424 157 PDAVVLVVCVELCSLTFQRDDDSKDN-LVANALF--GDGAAAVVVSG--------------DPRPGPGPRILA------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 249 iLASAFTAESQH---WDVGmlpSGGtvnprdpersyFEIDGSR-----LREAFlalgPGPVGQALDQAGVTMDDVALVAV 320
Cdd:COG3424 213 -FRSYLIPDTEDvmgWDVG---DTG-----------FRMVLSPevpdlIAEHL----APAVEPLLARHGLTIEDIDHWAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 321 H----QVavgyLEDVHRALGVPADRTIVT---VADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMVVR 393
Cdd:COG3424 274 HpggpKV----LDAVEEALGLPPEALAHSrevLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLR 349
|
.
gi 2267659504 394 W 394
Cdd:COG3424 350 W 350
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
145-214 |
2.05e-09 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 53.67 E-value: 2.05e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 145 MDVKNACNSVLNGIEVAEALIGTGRYRRVLVACGEMPTRGVRWDvpDRRTyamsaaGYTMSDAGAAVLVE 214
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWT--DRST------AVLFGDGAGAVVLE 62
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
36-179 |
2.31e-09 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 58.44 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 36 ARIVDVAVHLPERTRDVADAERDLHRRNPKVAPRLPMVSrltGVRRVHVADDDQQASDLAVAASRTVLDRAGLRPQDVDL 115
Cdd:PRK12880 8 AKISGICVSVPEHKICIDDELESVFSNDIKTLKRMKKVI---GLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267659504 116 LIFASATQDMIEPATSHITAAKLGVRAPVM--DVKNACNSVLNGIEVAEALIGTGrYRRVLVACGE 179
Cdd:PRK12880 85 LIVVTQSPDFFMPSTACYLHQLLNLSSKTIafDLGQACAGYLYGLFVAHSLIQSG-LGKILLICGD 149
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
91-391 |
8.58e-09 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 56.85 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 91 ASDLAVAASRTVLDRAGLRPQDVDLLIFASATqDMIEPATSHITAAKLGVRApvmDVK------NACNSVLNGIEVAEAL 164
Cdd:cd00831 85 ARELAEEAARGALDEAGLRPSDIDHLVVNTST-GNPTPSLDAMLINRLGLRP---DVKrynlggMGCSAGAIALDLAKDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 165 IGTGRYRRVLVACGEMPTRGVRWdvPDRRTYAMSAAGYtmSDAGAAVLVeATGAGSGTGGADAFEDDLAAelarlveptd 244
Cdd:cd00831 161 LEANPGARVLVVSTELCSLWYRG--PDHRSMLVGNALF--GDGAAAVLL-SNDPRDRRRERPLFELVRAA---------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 245 rpSGILASafTAESQHWDVGmlPSGGTVNprdpersyFEIDGSRLREAFLALGPGPVGQALdQAGVTMDDVALVAVHQ-- 322
Cdd:cd00831 226 --STLLPD--SEDAMGWHLG--EEGLTFV--------LSRDVPRLVEKNLERVLRKLLARL-GIGLFKLAFDHWCVHPgg 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2267659504 323 VAVgyLEDVHRALGVPADRTIV---TVADHGNIASATLPLQLATALESGRLRRGDVVLLLGLAGGISMGAMV 391
Cdd:cd00831 291 RAV--LDAVEKALGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFTCESAV 360
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
95-214 |
1.15e-08 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 56.43 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 95 AVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATS-HITAAkLGVRAPVMDVKNACNSVLNGIEVAEALIGTGRYRRV 173
Cdd:PRK07515 99 GVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAiEIQQA-LGIEGFAFDMNVACSSATFGIQTAANAIRSGSARRV 177
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2267659504 174 LVACGEMPTRGVRWDvpDRRTYamsaagYTMSDAGAAVLVE 214
Cdd:PRK07515 178 LVVNPEICSGHLNFR--DRDSH------FIFGDVATAVIVE 210
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
93-198 |
1.22e-06 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 49.95 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 93 DLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAKLGVR-APVMDVKNACNSVLNGIEVAEALIGTGRYR 171
Cdd:cd00829 18 ELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLgKPATRVEAAGASGSAAVRAAAAAIASGLAD 97
|
90 100
....*....|....*....|....*..
gi 2267659504 172 RVLVACGEMPTRGVRWDVPDRRTYAMS 198
Cdd:cd00829 98 VVLVVGAEKMSDVPTGDEAGGRASDLE 124
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
92-392 |
2.56e-05 |
|
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: 45.70 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 92 SDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAKLGVRAPVMDVKNACNSVLNGIEVAEALIGTGRYR 171
Cdd:cd00825 37 IVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 172 RVLVACGEMPTR--------GVRWDVPDR--RTYAMSAAGYTMSDAGAAVLVEatgagsgtggadafEDDLAAELARLVE 241
Cdd:cd00825 117 IVLAGGSEELAApmdcefdaMGALSTPEKasRTFDAAADGFVFGDGAGALVVE--------------ELEHALARGAHIY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 242 PTDRPSGILASAFTAESQHWDVGMLPSGgtvnprdpersyfeidgsrlreaflalgpgpVGQALDQAGVTMDDVALVAVH 321
Cdd:cd00825 183 AEIVGTAATIDGAGMGAFAPSAEGLARA-------------------------------AKEALAVAGLTVWDIDYLVAH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 322 QVAVGYLEDVHRALGVPADR-----TIVTVADHGNIASATLPLQLATALESGRL-------------------------R 371
Cdd:cd00825 232 GTGTPIGDVKELKLLRSEFGdkspaVSATKAMTGNLSSAAVVLAVDEAVLMLEHgfippsihieeldeaglnivtettpR 311
|
330 340
....*....|....*....|.
gi 2267659504 372 RGDVVLLLGLAGGISMGAMVV 392
Cdd:cd00825 312 ELRTALLNGFGLGGTNATLVL 332
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
91-178 |
4.95e-05 |
|
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: 45.16 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 91 ASDLAVAASRTVLDRAGLRPQDVDLLIFASATQdmiEPATSHIT-----AAKLGVRAPVMDVKNACNSVLNGIEVAEALI 165
Cdd:cd00751 22 ADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQ---AGEGQNPArqaalLAGLPESVPATTVNRVCGSGLQAVALAAQSI 98
|
90
....*....|...
gi 2267659504 166 GTGRYrRVLVACG 178
Cdd:cd00751 99 AAGEA-DVVVAGG 110
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
84-175 |
5.06e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 41.82 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 84 VADDDQQASDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAKLGVrAPVM---DVKNACNSVLNGIEV 160
Cdd:PRK04262 44 VPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESHPYAVKPTATIVAEALGA-TPDLtaaDLEFACKAGTAALQA 122
|
90
....*....|....*
gi 2267659504 161 AEALIGTGRYRRVLV 175
Cdd:PRK04262 123 AMGLVKSGMIKYALA 137
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
91-392 |
3.05e-03 |
|
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: 38.96 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 91 ASDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITAAKLGVR-APVMDVKNACNSVLNGIEVAEALIGTGR 169
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 170 YRRVLVACGEMPTRGvrwdvpdrrtyamsaagytmsDAGAAVLVEatgagsgtggadafeddlaaELARLVEPTDRPSGI 249
Cdd:cd00327 87 ADIVLAGGSEEFVFG---------------------DGAAAAVVE--------------------SEEHALRRGAHPQAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 250 LASAFTAesqhwdvgmlpsggtvnprdpersyfeIDGSRLREAFLALGPGP-VGQALDQAGVTMDDVALVAVHQVAVGYL 328
Cdd:cd00327 126 IVSTAAT---------------------------FDGASMVPAVSGEGLARaARKALEGAGLTPSDIDYVEAHGTGTPIG 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267659504 329 EDVHRALGVPAD-----RTIVTVADHGNIASATLPLQLATAL-------ESGRLRRGDVVLLLGLAGGISMGAMVV 392
Cdd:cd00327 179 DAVELALGLDPDgvrspAVSATLIMTGHPLGAAGLAILDELLlmlehefIPPTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
91-178 |
6.13e-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: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 91 ASDLAVAASRTVLDRAGLRPQDVDLLIFASATQDMIEPATSHITA--AKLGVRAPVMDVKNACNSVLNGIEVAEALIGTG 168
Cdd:COG0183 26 ADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAAllAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAG 105
|
90
....*....|
gi 2267659504 169 RYrRVLVACG 178
Cdd:COG0183 106 DA-DVVIAGG 114
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
88-178 |
9.98e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 37.82 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267659504 88 DQQASDLAVAASRTVLDRAGLRPQDVDLLIFA---SATQDMIEPATSHItAAKLGVRAPVMDVKNACNSVLNGIEVAEAL 164
Cdd:PRK05790 23 DVSAVELGAIVIKAALERAGVPPEQVDEVIMGqvlQAGAGQNPARQAAL-KAGLPVEVPALTINKVCGSGLKAVALAAQA 101
|
90
....*....|....
gi 2267659504 165 IGTGRYrRVLVACG 178
Cdd:PRK05790 102 IRAGDA-DIVVAGG 114
|
|
| |
