|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
2-373 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 765.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 2 HNVVISGTGLYTPANSISNEELVQSFNAYVQQFNLDNAAAIERGDVEALTESSAAFIEKASGIKSRFVMDKAGILDPQRM 81
Cdd:PRK07515 1 HNVVISGTGLYTPPESISNEELVASFNAYVERFNAENAAAIAAGEVEALQPSSSEFIEKASGIKSRYVMDKEGILDPDRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 82 APRLPERSNDEWSILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQGFGFDMNVACSSATF 161
Cdd:PRK07515 81 RPRIPERSNDELSIQAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGFAFDMNVACSSATF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 162 GIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERADLATSEHQFDVVSTKLLTKFSNNIRNNF 241
Cdd:PRK07515 161 GIQTAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATSAGGFEILGTRLFTQFSNNIRNNF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 242 GFLNRAAEEGIGAPDKLFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKLLGREASVEE 321
Cdd:PRK07515 241 GFLNRADPEGIGARDKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKRFWLHQANINMNQLIGKKVLGRDATPEE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489303248 322 APVILDTYANTSSAGSVIAFHTYQDDLPKGAVAVLSSFGAGYSIGSVILRKR 373
Cdd:PRK07515 321 APVILDEYANTSSAGSIIAFHKHSDDLAAGDLGVICSFGAGYSIGSVIVRKR 372
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
3-370 |
3.10e-91 |
|
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: 276.73 E-value: 3.10e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 3 NVVISGTGLYTPANSISNEELVQSFnayvqqfnldnaaaiergdvealtESSAAFIEKASGIKSRfvmdkagildpqRMA 82
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRL------------------------DTSDEWIRTRTGIRER------------RIA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 83 prlpersnDEWSILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQG-FGFDMNVACSSATF 161
Cdd:cd00830 45 --------DPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLVQARLGAKNaAAFDINAACSGFLY 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 162 GIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERAD----LATSEHQFDVVSTKLLTKFSNNI 237
Cdd:cd00830 117 GLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGAGAVVLEATEedpgILDSVLGSDGSGADLLTIPAGGS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 238 RNNFgflnraaeEGIGAPDKLFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKLLGREa 317
Cdd:cd00830 197 RSPF--------EDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPE- 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489303248 318 svEEAPVILDTYANTSSAGSVIAFHTYQDD--LPKGAVAVLSSFGAGYSIGSVIL 370
Cdd:cd00830 268 --EKVVVNLDRYGNTSAASIPLALDEAIEEgkLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
2-371 |
1.38e-67 |
|
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: 216.13 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 2 HNVVISGTGLYTPANSISNEELvqsfnayvqqfnldnaaaiergdvEALTESSAAFIEKASGIKSRFVMDKagildpqrm 81
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDL------------------------EKRLDTSDEWIEERTGIRERRIAAP--------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 82 aprlpersnDEWSilCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQG-FGFDMNVACSSAT 160
Cdd:COG0332 48 ---------DETT--SDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFPSTACLVQHKLGAKNaAAFDINAACSGFV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 161 FGIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERADLATSehqfdVVSTKLLT--KFSNNIR 238
Cdd:COG0332 117 YALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDGAGAVVLEASEEGPG-----ILGSVLGSdgSGADLLV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 239 NNFGfLNRAAEEGIGAPDKLFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKLlgrEAS 318
Cdd:COG0332 192 VPAG-GSRNPPSPVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRL---GLP 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489303248 319 VEEAPVILDTYANTSSAGSVIAFHTYQDD--LPKGAVAVLSSFGAGYSIGSVILR 371
Cdd:COG0332 268 EEKVVVNIDRYGNTSAASIPLALDEALREgrIKPGDLVLLAGFGAGLTWGAAVLR 322
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
1-371 |
5.89e-50 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 170.25 E-value: 5.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 1 MHNVVISGTGLYTPANSISNEELvqsfnayvqqfnldnaaaiergdvEALTESSAAFIEKASGIKSRfvmdkagildpqR 80
Cdd:PRK09352 1 MMYAKILGTGSYLPERVVTNDDL------------------------EKMVDTSDEWIVTRTGIKER------------R 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 81 MAprlpersnDEWSILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQG-FGFDMNVACSSA 159
Cdd:PRK09352 45 IA--------APDETTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPDYAFPSTACLVQARLGAKNaAAFDLSAACSGF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 160 TFGIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERADlatsehQFDVVSTKLltkFSNNIRN 239
Cdd:PRK09352 117 VYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDGAGAVVLGASE------EPGILSTHL---GSDGSYG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 240 NfgFLNRAA-EEGIGAPDKLFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKLlgrEAS 318
Cdd:PRK09352 188 D--LLYLPGgGSRGPASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKL---GLP 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489303248 319 VEEAPVILDTYANTSSAGSVIAFHTYQDD--LPKGAVAVLSSFGAGYSIGSVILR 371
Cdd:PRK09352 263 MEKVVVTVDKYGNTSAASIPLALDEAVRDgrIKRGDLVLLEGFGGGLTWGAALVR 317
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-372 |
4.33e-49 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 168.12 E-value: 4.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 1 MHNVVISGTGLYTPANSISNEELvqsfnayvqqfnldnaaaiergdvEALTESSAAFIEKASGIKSRfvmdkagildpqR 80
Cdd:PRK12879 2 MSYARITGIGTYVPPRVLTNDDL------------------------ETFIDTSDEWIVQRTGIKER------------R 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 81 MAprlperSNDEWSIlcQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQGFG-FDMNVACSSA 159
Cdd:PRK12879 46 IA------HVEEYTS--DLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQVQARLGIPNAAaFDINAACAGF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 160 TFGIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERAD---------LATSEHQFDVVSTkll 230
Cdd:PRK12879 118 LYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDGAGAVVLEATEnepgfidyvLGTDGDGGDILYR--- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 231 TKFSNNIrnnfgflNRAAEEGIGApdklFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVK 310
Cdd:PRK12879 195 TGLGTTM-------DRDALSGDGY----IVQNGREVFKWAVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCE 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489303248 311 KLlgrEASVEEAPVILDTYANTSSAGSVIAFHTYQDD--LPKGAVAVLSSFGAGYSIGSVILRK 372
Cdd:PRK12879 264 KL---GIPMEKTLVSVEYYGNTSAATIPLALDLALEQgkIKPGDTLLLYGFGAGLTWAALLVKW 324
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
1-370 |
6.67e-35 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 130.73 E-value: 6.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 1 MHNVVISGTGLYTPANSISNEELVQSFNayvqqfnldnaaaiergdveaLTESSaafIEKASGIKSRFVMDkagildpqr 80
Cdd:PRK07204 2 KRYISIKGIGTYLPKRKVDSLELDKKLD---------------------LPEGW---VLKKSGVKTRHFVD--------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 81 maprlpersnDEWSilCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQGFG---FDMNVACS 157
Cdd:PRK07204 49 ----------GETS--SYMGAEAAKKAVEDAKLTLDDIDCIICASGTIQQAIPCTASLIQEQLGLQHSGipcFDINSTCL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 158 SATFGIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERADLATSehqfdVVSTKLLTKFSN-- 235
Cdd:PRK07204 117 SFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGDGAAAVVITKGDHSSR-----ILASHMETYSSGah 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 236 --NIRNNfGFLNRAAEEGIG-APDKLFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKL 312
Cdd:PRK07204 192 lsEIRGG-GTMIHPREYSEErKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKL 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 313 lgrEASVEEAPVILDTYANTSSAGSVIAFHT--YQDDLPKGAVAVLSSFGAGYSIGSVIL 370
Cdd:PRK07204 271 ---GVDEERFVTIFEDHGNMIAASIPVALFEaiKQKKVQRGNKILLLGTSAGLSIGGILL 327
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
282-372 |
1.85e-24 |
|
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: 95.65 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 282 LSENQLNVGDVKRFWLHQANLSMNHLIVKKLlgrEASVEEAPVILDTYANTSSAGSVIAFHTY--QDDLPKGAVAVLSSF 359
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRL---GLPPEKVVVNLDEYGNTSAASIPLALDEAveEGKLKPGDLVLLVGF 77
|
90
....*....|...
gi 489303248 360 GAGYSIGSVILRK 372
Cdd:pfam08541 78 GAGLTWGAALLRW 90
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-370 |
3.87e-24 |
|
"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: 101.36 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 3 NVVISGTGLYTPANSISNEELVQSFNAYVQQFNLdnaaaiergdvealtessaafiekasGIKSRFVmdkagildpqrma 82
Cdd:cd00827 1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTT--------------------------GIGQRHM------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 83 prlperSNDEWSILCqMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQG-FGFDMNVACSSATF 161
Cdd:cd00827 42 ------AGDDEDVPT-MAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLTNaEAFDLKQACYGGTA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 162 GIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDShFIFGDAATAVILERADlatSEHQFDVVSTkLLTKFSNNIRNNF 241
Cdd:cd00827 115 ALQLAANLVESGPWRYALVVASDIASYLLDEGSALE-PTLGDGAAAMLVSRNP---GILAAGIVST-HSTSDPGYDFSPY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 242 GFLNRAAEEGIGAPDKLFVQ---EGRKVFRDVCPMVAELIgkHLSENQLNVGDVKRFWL-HQAN-LSMNHLIVKKLLGRE 316
Cdd:cd00827 190 PVMDGGYPKPCKLAYAIRLTaepAGRAVFEAAHKLIAKVV--RKALDRAGLSEDIDYFVpHQPNgKKILEAVAKKLGGPP 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489303248 317 ASVEEAPVI-LDTYANTSSAGSVIAFHTYQD--DLPKGAVAVLSSFGAGYSIGSVIL 370
Cdd:cd00827 268 EKASQTRWIlLRRVGNMYAASILLGLASLLEsgKLKAGDRVLLFSYGSGFTAEAFVL 324
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
41-371 |
6.48e-24 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 100.79 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 41 AIERGDVEALTESSAAFIEKASGIKSRfvmdkagildpqRMAPrlperSNDEwsiLCQMAVSAAEQALQRAGKTAADIDG 120
Cdd:CHL00203 16 SVENQQFEDIIETSDHWISTRTGIKKR------------HLAP-----SSTS---LTKLAAEAANKALDKAHMDPLEIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 121 VIVACSNLQRAYPAiAIEVQEALG-IQGFGFDMNVACSSATFGIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHF 199
Cdd:CHL00203 76 IILATSTPDDLFGS-ASQLQAEIGaTRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 200 IFGDAATAVILERA--------DLATSEHQFDVVStkLLTKFSNNIRNNFGFLNRAAEEGIGapdklfvQEGRKVFRDVC 271
Cdd:CHL00203 155 LFGDGAGAAIIGASyensilgfKLCTDGKLNSHLQ--LMNKPVNNQSFGTTKLPQGQYQSIS-------MNGKEVYKFAV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 272 PMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKLlgreaSVEEAPVI--LDTYANTSSAGSVIAF-HTYQDD- 347
Cdd:CHL00203 226 FQVPAVIIKCLNALNISIDEVDWFILHQANKRILEAIANRL-----SVPNSKMItnLEKYGNTSAASIPLALdEAIQNNk 300
|
330 340
....*....|....*....|....
gi 489303248 348 LPKGAVAVLSSFGAGYSIGSVILR 371
Cdd:CHL00203 301 IQPGQIIVLSGFGAGLTWGAIVLK 324
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
6-371 |
1.32e-22 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 97.89 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 6 ISGTGLYTPANSISNEELvqsfnayvqqfnldnaaaiergdvEALTESSAAFIEKASGIKSRFVMdkagildpqrmaprl 85
Cdd:PLN02326 50 LVGCGSAVPKLLITNDDL------------------------SKLVDTSDEWIATRTGIRNRRVL--------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 86 perSNDEwsILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAiAIEVQEALGIQG-FGFDMNVACSSATFGIQ 164
Cdd:PLN02326 91 ---SGDE--TLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSSPDDLFGS-APQVQAALGCTNaLAFDLTAACSGFVLGLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 165 NAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILEradlATSEHQ-----FDVVST-----KLLTKFS 234
Cdd:PLN02326 165 TAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAGAVVLQ----ACDDDEdgllgFDMHSDgnghkHLHATFK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 235 NN-------IRNNFGFLN--RAAEEGIGapdklfvQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMN 305
Cdd:PLN02326 241 GEdddssggNTNGVGDFPpkKASYSCIQ-------MNGKEVFKFAVRCVPQVIESALQKAGLTAESIDWLLLHQANQRII 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489303248 306 HLIVKKL-LGREASVEEapviLDTYANTSSAGSVIAFH--TYQDDLPKGAVAVLSSFGAGYSIGSVILR 371
Cdd:PLN02326 314 DAVAQRLgIPPEKVISN----LANYGNTSAASIPLALDeaVRSGKVKKGDVIATAGFGAGLTWGSAIVR 378
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
150-229 |
3.86e-20 |
|
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: 83.72 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 150 FDMNVACSSATFGIQNAANSIQLGQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERADlatsEHQFDVVSTKL 229
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATD----EPGARILDSVL 76
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
6-371 |
1.07e-18 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 85.93 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 6 ISGTGLYTPANSISNEELVQsfnayvqQFNLDnaaaiergdvealtessAAFIEKASGIKSRFVMdkagildpqrmaprl 85
Cdd:PRK05963 6 IAGFGHAVPDRRVENAEIEA-------QLGLE-----------------TGWIERRTGIRCRRWA--------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 86 perSNDEwsILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQGFG-FDMNVACSSATFGIQ 164
Cdd:PRK05963 47 ---APDE--TLSDLAASAGDMALSDAGIERSDIALTLLATSTPDHLLPPSAPLLAHRLGLQNSGaIDLAGACAGFLYALV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 165 NAANSIQLgQARAILMVNPEICTGHLNFRDRDSHFIFGDAATAVIleradLATSEHQFD-VVSTKLLTKFSNN--IRNNF 241
Cdd:PRK05963 122 LADGFVRA-QGKPVLVVAANILSRRINMAERASAVLFADAAGAVV-----LAPSAKANSgVLGSQLISDGSHYdlIKIPA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 242 GFLNRAAEEGIGAPDKLFV-QEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKL-LGREASV 319
Cdd:PRK05963 196 GGSARPFAPERDASEFLMTmQDGRAVFTEAVRMMSGASQNVLASAAMTPQDIDRFFPHQANARIVDKVCETIgIPRAKAA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489303248 320 EEapviLDTYANTSSAGSVIAFHTYQDDLP--KGAVAVLSSFGAGYSIGSVILR 371
Cdd:PRK05963 276 ST----LETYGNSSAATIPLSLSLANLEQPlrEGERLLFAAAGAGMTGGAVVMR 325
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
4-370 |
3.77e-13 |
|
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: 69.95 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 4 VVISGTGLYTPANSISNEELVQsfnAYVQQFNLDNAAAiergDVEALTESSaafieKASGIKSRFVMDKAGI---LDPQR 80
Cdd:cd00831 2 ATILAIGTAVPPHRVPQSELVD---FYRRLFSSDHLPE----LKEKLKRLC-----AKTGIETRYLVLPGGEetyAPRPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 81 MAPRLPERSNDEWSILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAyPAIAIEVqealgIQGFGFDMNVA----- 155
Cdd:cd00831 70 MSPSLDERNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPT-PSLDAML-----INRLGLRPDVKrynlg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 156 ---CSSATFGIQNAANSIQLGQARAILMVNPEICTghLNFRDRD------SHFIFGDAATAVIL--ERADLATSEHQFDV 224
Cdd:cd00831 144 gmgCSAGAIALDLAKDLLEANPGARVLVVSTELCS--LWYRGPDhrsmlvGNALFGDGAAAVLLsnDPRDRRRERPLFEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 225 VSTKlltkfsnnirnnfgflNRAAEEGIGAPDKLFVQEGRKVF--RDVCPMVAELIGKHLSE--NQLNVGDVKR---FWL 297
Cdd:cd00831 222 VRAA----------------STLLPDSEDAMGWHLGEEGLTFVlsRDVPRLVEKNLERVLRKllARLGIGLFKLafdHWC 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 298 -H-------QAnlsmnhliVKKLLG-REASVEEAPVILDTYANTSSAG--SVIAFHTYQDDLPKGAVAVLSSFGAGYSIG 366
Cdd:cd00831 286 vHpggravlDA--------VEKALGlSPEDLEASRMVLRRYGNMSSSSvlYVLAYMEAKGRVKRGDRGLLIAFGPGFTCE 357
|
....
gi 489303248 367 SVIL 370
Cdd:cd00831 358 SAVW 361
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
58-370 |
5.06e-12 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 66.53 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 58 IEKASGIKSRFVMDkagildpqrmaprlpersndEWSILCQMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAI 137
Cdd:PRK12880 42 MKKVIGLNTRYICD--------------------ENTCVSDLGKHAANTLLQGLNIDKNSLDALIVVTQSPDFFMPSTAC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 138 EVQEALGIQG--FGFDMNVACSSATFGIQNAANSIQLGQARaILMVNPEICTGHLNFRDRDSHFIFGDAATAVILERADL 215
Cdd:PRK12880 102 YLHQLLNLSSktIAFDLGQACAGYLYGLFVAHSLIQSGLGK-ILLICGDTLSKFIHPKNMNLAPIFGDGVSATLIEKTDF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 216 ATSEHQ-------FD--VVSTKLLTKFSNNIRNNFGFLNRAAEEGIgapDKLFVqEGRKVFRDVCPMVAELIGKHLSENQ 286
Cdd:PRK12880 181 NEAFFElgsdgkyFDklIIPKGAMRIPKADIFNDDSLMQTEEFRQL---ENLYM-DGANIFNMALECEPKSFKEILEFSK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 287 LNVGDVKRFWLHQANLSMNHLIVKKLlgrEASVEEAP-VILDTYANTSsAGSVIAFhTYQDDLPKGAVAVLSSFGAGYSI 365
Cdd:PRK12880 257 VDEKDIAFHLFHQSNAYLVDCIKEEL---KLNDDKVPnFIMEKYANLS-ACSLPAL-LCELDTPKEFKASLSAFGAGLSW 331
|
....*
gi 489303248 366 GSVIL 370
Cdd:PRK12880 332 GSAVL 336
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
3-371 |
6.71e-12 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 65.80 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 3 NVVISGTGLYTPANSISNEElvqsfnayvqqfnldnaaaiergdvealtessaafIEKASGIKSRFVMDKAGILdpQRMA 82
Cdd:PRK06840 4 NVGIVGTGVYLPKDVMTAEE-----------------------------------IAEKTGIPEEVVIEKFGIY--EKPV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 83 PRlPERSNdewsilCQMAVSAAEQALQRAGKTAADIDGVIVACSNLqRAYP--AIAIEVQEALG-IQGFGFDMNVACSSA 159
Cdd:PRK06840 47 PG-PEDHT------SDMAIAAAKPALKQAGVDPAAIDVVIYIGSEH-KDYPvwSSAPKIQHEIGaKNAWAFDIMAVCASF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 160 TFGIQnaansiqlgQARAILMVNPEICTGHL----------NFRDRDSHFIF--GDAATAVILERadlatSEHQFDVVST 227
Cdd:PRK06840 119 PIALK---------VAKDLLYSDPSIENVLLvggyrnsdlvDYDNPRTRFMFnfAAGGSAALLKK-----DAGKNRILGS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 228 KLLT--KFSNNIRNNFGflnraaeeGIGAPDKLFVQEGRKVFRDVcpMVAELIGKHLSENQL-NVGDVKRFWLHQANLS- 303
Cdd:PRK06840 185 AIITdgSFSEDVRVPAG--------GTKQPASPETVENRQHYLDV--IDPESMKERLDEVSIpNFLKVIREALRKSGYTp 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 304 -----MNHLIVKK-----LLGREASVEEAPVILDTYANTSSAGSVIAFHTYQDD--LPKGAVAVLSSFGAGYSIGSVILR 371
Cdd:PRK06840 255 kdidyLAILHMKRsahiaLLEGLGLTEEQAIYLDEYGHLGQLDQILSLHLALEQgkLKDGDLVVLVSAGTGYTWAATVIR 334
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4-216 |
2.01e-11 |
|
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: 64.73 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 4 VVISGTGLYTP-ANSISneelvqsfnayvqqfnlDNAAAIERGdvealtESSAAFIEK--ASGIKSRF---VMDkagiLD 77
Cdd:COG0304 3 VVITGLGAVSPlGNGVE-----------------EFWEALLAG------RSGIRPITRfdASGLPVRIageVKD----FD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 78 PQRMAPRLPERSNDEWSilcQMAVSAAEQALQRAGKTAADID----GVIVACS-----NLQRAYP--------------- 133
Cdd:COG0304 56 PEEYLDRKELRRMDRFT---QYALAAAREALADAGLDLDEVDpdrtGVIIGSGiggldTLEEAYRallekgprrvspffv 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 134 ------AIAIEVQEALGIQGFGFDMNVACSSATFGIQNAANSIQLGQARAIL------MVNPEICTGHLNFR-------- 193
Cdd:COG0304 133 pmmmpnMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIaggaeaAITPLGLAGFDALGalstrndd 212
|
250 260 270
....*....|....*....|....*....|...
gi 489303248 194 ----------DRDShFIFGDAATAVILERADLA 216
Cdd:COG0304 213 pekasrpfdkDRDG-FVLGEGAGVLVLEELEHA 244
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
99-212 |
1.14e-09 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 59.42 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 99 MAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQGF--GFDMNVACSSATFGIQNAANSIQLGQAR 176
Cdd:COG3425 54 MAANAARRALDRAGIDPSDIGAVYVGTESGPDASKPIATYVHGALGLPPNcrAFELKFACYAGTAALQAALGWVASGPNK 133
|
90 100 110
....*....|....*....|....*....|....*..
gi 489303248 177 AILMvnpeICTGHLNFRDRDS-HFIFGDAATAVILER 212
Cdd:COG3425 134 KALV----IASDIARYGPGSAgEYTQGAGAVAMLVGA 166
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
4-216 |
5.21e-09 |
|
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: 57.55 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 4 VVISGTGLYTP-ANSIsnEELVQSFNAYVQQFnldnaAAIERGDVEALTESSAAFIekasgiksrfvmdkAGILDPQRMA 82
Cdd:cd00834 3 VVITGLGAVTPlGNGV--EEFWEALLAGRSGI-----RPITRFDASGFPSRIAGEV--------------PDFDPEDYLD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 83 PRLPERSNDewsiLCQMAVSAAEQALQRAGKTAADID----GVIVACSN-----------------LQRAYP-------- 133
Cdd:cd00834 62 RKELRRMDR----FAQFALAAAEEALADAGLDPEELDperiGVVIGSGIgglatieeayrallekgPRRVSPffvpmalp 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 134 -AIAIEVQEALGIQGFGFDMNVACSSATFGIQNAANSIQLGQARAIL------MVNPEICTGHLNFR------------- 193
Cdd:cd00834 138 nMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIaggaeaLITPLTLAGFAALRalstrnddpekas 217
|
250 260
....*....|....*....|....*...
gi 489303248 194 -----DRDShFIFGDAATAVILERADLA 216
Cdd:cd00834 218 rpfdkDRDG-FVLGEGAGVLVLESLEHA 244
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
100-222 |
7.20e-09 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 56.81 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 100 AVSAAEQALQRAGKTAADIdGVIVACSnLQRAY--PAIAIEVQEALGIQG--FGFDMNVACSSATFGIQNAANSIQLGQA 175
Cdd:PRK09258 65 AIAAGRKALAEAGIDPSDI-GLLINTS-VCRDYlePATACRVHHNLGLPKscANFDVSNACLGFLNGMLDAANMIELGQI 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489303248 176 RAILMVNPE---------I------CTGHLNFRDRDSHFIFGDAATAVILERADLATSEHQF 222
Cdd:PRK09258 143 DYALVVSGEsareiveatIdrllapETTREDFAQSFATLTLGSGAAAAVLTRGSLHPRGHRL 204
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
99-370 |
8.68e-09 |
|
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: 56.49 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 99 MAVSAAEQALQRAGKTAAD----IDGVIVA---------------------CSNLQRAYPAIAIEVQEALGIQGFGFDMN 153
Cdd:cd00825 14 LGFEAAERAIADAGLSREYqknpIVGVVVGtgggsprfqvfgadamravgpYVVTKAMFPGASGQIATPLGIHGPAYDVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 154 VACSSATFGIQNAANSIQLGQARAILMVNPEI---------------CTGHLNFRDRDSH---FIFGDAATAVILERADL 215
Cdd:cd00825 94 AACAGSLHALSLAADAVQNGKQDIVLAGGSEElaapmdcefdamgalSTPEKASRTFDAAadgFVFGDGAGALVVEELEH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 216 ATSEhqfdvvstklltkfsnnirnnfGFLNRAaeeGIGAPDKLFVQEGRKVFRDVCPMVAELIGKHLSENQLNVGDVKRF 295
Cdd:cd00825 174 ALAR----------------------GAHIYA---EIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 296 WLHQANLSMNHLIVKKlLGREASVEEAPVI---LDTYANTSSAGSV--------------IAFHTYQDDLPKGAV----- 353
Cdd:cd00825 229 VAHGTGTPIGDVKELK-LLRSEFGDKSPAVsatKAMTGNLSSAAVVlavdeavlmlehgfIPPSIHIEELDEAGLnivte 307
|
330 340
....*....|....*....|....*
gi 489303248 354 --------AVLSSFGAGYSIGSVIL 370
Cdd:cd00825 308 ttprelrtALLNGFGLGGTNATLVL 332
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
100-370 |
2.53e-08 |
|
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: 54.37 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 100 AVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQGF-GFDMNVACSSATFGIQNAANSIQLGQARAI 178
Cdd:cd00327 11 GFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGpAYSVNQACATGLTALALAVQQVQNGKADIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 179 LMVNPEICtghlnfrdrdshfIFGDAATAVILER-ADLATSEH--QFDVVSTklltkfsnnirnnfgflnraAEEGIGAp 255
Cdd:cd00327 91 LAGGSEEF-------------VFGDGAAAAVVESeEHALRRGAhpQAEIVST--------------------AATFDGA- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 256 dklfvQEGRKVFRDvcpMVAELIGKHLSENQLNVGDVKRFWLHQANLSMNHLIVKKLLGREASVEEAPV--ILDTYANTS 333
Cdd:cd00327 137 -----SMVPAVSGE---GLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRSPAVsaTLIMTGHPL 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489303248 334 SAGSVIAFHTYQDDLPKGAV---------AVLSSFGAGYSIGSVIL 370
Cdd:cd00327 209 GAAGLAILDELLLMLEHEFIpptpreprtVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
98-214 |
3.10e-08 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 54.96 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 98 QMAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGIQG-FGFDMNVACSSATFGIQNAANSIQLGQAR 176
Cdd:cd00829 18 ELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLAD 97
|
90 100 110
....*....|....*....|....*....|....*...
gi 489303248 177 AILmvnpeiCTGHLNFRDRDSHFIFGDAATAVILERAD 214
Cdd:cd00829 98 VVL------VVGAEKMSDVPTGDEAGGRASDLEWEGPE 129
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
97-216 |
6.28e-06 |
|
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: 46.86 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 97 CQMAVSAAEQALQRAGKTAADID----GVIVACSN--------------LQRAYP--------AIAIEVQEALGIQGfgf 150
Cdd:pfam00109 88 QRLLLEAAWEALEDAGITPDSLDgsrtGVFIGSGIgdyaalllldedggPRRGSPfavgtmpsVIAGRISYFLGLRG--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 151 dMNV----ACSSATFGIQNAANSIQLGQARAIL------MVNPEICTGHLN------------FRDRDSHFIFGDAATAV 208
Cdd:pfam00109 165 -PSVtvdtACSSSLVAIHAAVQSIRSGEADVALaggvnlLLTPLGFAGFSAagmlspdgpckaFDPFADGFVRGEGVGAV 243
|
....*...
gi 489303248 209 ILERADLA 216
Cdd:pfam00109 244 VLKRLSDA 251
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
98-179 |
2.36e-04 |
|
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: 42.85 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 98 QMAVSAAEQALQRAGKTAADIDGVIVACSN--LQRAYPA--------IAIEVQealgiqgfGFDMNVACSSATFGIQNAA 167
Cdd:cd00751 24 DLGAAVIKALLERAGLDPEEVDDVIMGNVLqaGEGQNPArqaallagLPESVP--------ATTVNRVCGSGLQAVALAA 95
|
90
....*....|..
gi 489303248 168 NSIQLGQARAIL 179
Cdd:cd00751 96 QSIAAGEADVVV 107
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
98-179 |
1.08e-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: 40.82 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 98 QMAVSAAEQALQRAGKTAADIDGVIVACSN--LQRAYPA--------IAIEVQealgiqgfGFDMNVACSSATFGIQNAA 167
Cdd:COG0183 28 DLGAAVIKALLERAGLDPEAVDDVILGCVLqaGQGQNPArqaallagLPESVP--------AVTVNRVCGSGLQAVALAA 99
|
90
....*....|..
gi 489303248 168 NSIQLGQARAIL 179
Cdd:COG0183 100 QAIAAGDADVVI 111
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
99-166 |
3.08e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 39.12 E-value: 3.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 99 MAVSAAEQALQRAGKTAADIDGVIVACSNLQRAYPAIAIEVQEALGI--QGFGFDMNVACSSATFGIQNA 166
Cdd:PRK04262 54 IAVEAARNALKRAGIDPKEIGAVYVGSESHPYAVKPTATIVAEALGAtpDLTAADLEFACKAGTAALQAA 123
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
103-175 |
8.74e-03 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 37.83 E-value: 8.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489303248 103 AAEQALQRAGKTAADIDGVIVACSNLQRAYPA-IA--IEVQEALGIQGFGFDMNVACSSATFGIQNAANSIQLGQA 175
Cdd:PRK07108 34 VVQHAVERAKLDPAEVEDVIMGCANPEGATGAnIArqIALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEG 109
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
99-188 |
9.68e-03 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 37.70 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489303248 99 MAVSAAEQALQRAGKTAADIDGviVACSNLQRAYPAIAieVQEALGIQGFGFDMN-VACSSATFGIQNAANSIQLGQARA 177
Cdd:PRK06158 31 LLAQAAHRALADAGLTMADVDG--LFTASPDDALWGLS--VAEYLGIRPRFVDGTmIGGSSFLAHLLPAALALEAGLCDV 106
|
90
....*....|.
gi 489303248 178 ILmvnpeICTG 188
Cdd:PRK06158 107 AL-----ICYG 112
|
|
| |
