|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
4-328 |
0e+00 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 512.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 4 KITAAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRIlKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIV 83
Cdd:PRK09352 1 MMYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRI-AAPDETTSDLATEAAKKALEAAGIDPEDIDLIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 84 ATVTPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFG 163
Cdd:PRK09352 80 ATTTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 164 DGAGAVLLEPATDGsGVLDSILRTDGSGRHYLNMKAGGSARPATietvtnkEHFAYQEGKTVFKFAVKGMADVSAELLER 243
Cdd:PRK09352 160 DGAGAVVLGASEEP-GILSTHLGSDGSYGDLLYLPGGGSRGPAS-------PGYLRMEGREVFKFAVRELAKVAREALEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 244 NNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEWEKE--LKKGDNLVLAAFGGGFTW 321
Cdd:PRK09352 232 AGLTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDgrIKRGDLVLLEGFGGGLTW 311
|
....*..
gi 746066411 322 GATWIKW 328
Cdd:PRK09352 312 GAALVRW 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
5-328 |
2.42e-170 |
|
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: 475.75 E-value: 2.42e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 5 ITAAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILkGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVA 84
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIA-APDETTSDLAVEAARKALEAAGIDPEDIDLIIVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 85 TVTPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGD 164
Cdd:COG0332 80 TVTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 165 GAGAVLLEPATDGSGVLDSILRTDGSGRHYLNMKAGGSARPATieTVTNKEHFAYQEGKTVFKFAVKGMADVSAELLERN 244
Cdd:COG0332 160 GAGAVVLEASEEGPGILGSVLGSDGSGADLLVVPAGGSRNPPS--PVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 245 NLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGFTWG 322
Cdd:COG0332 238 GLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEAlrEGRIKPGDLVLLAGFGAGLTWG 317
|
....*.
gi 746066411 323 ATWIKW 328
Cdd:COG0332 318 AAVLRW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
7-323 |
5.67e-159 |
|
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: 446.99 E-value: 5.67e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 7 AAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILkGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATV 86
Cdd:cd00830 2 ARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIA-DPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 87 TPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGDGA 166
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 167 GAVLLEPATDGSGVLDSILRTDGSGRHYLNMKAGGSARPAtiETVTNKEHFAYQEGKTVFKFAVKGMADVSAELLERNNL 246
Cdd:cd00830 161 GAVVLEATEEDPGILDSVLGSDGSGADLLTIPAGGSRSPF--EDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746066411 247 TGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGFTWGA 323
Cdd:cd00830 239 TPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAieEGKLKKGDLVLLLGFGAGLTWGA 317
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
7-328 |
6.80e-153 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 431.98 E-value: 6.80e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 7 AAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILkGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATV 86
Cdd:PRK12879 5 ARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIA-HVEEYTSDLAIKAAERALARAGLDAEDIDLIIVATT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 87 TPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGDGA 166
Cdd:PRK12879 84 TPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 167 GAVLLEPATDGSGVLDSILRTDGSGRHYLNMKAGGSARPATIEtvtNKEHFAYQEGKTVFKFAVKGMADVSAELLERNNL 246
Cdd:PRK12879 164 GAVVLEATENEPGFIDYVLGTDGDGGDILYRTGLGTTMDRDAL---SGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 247 TGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGFTWGAT 324
Cdd:PRK12879 241 TKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLAleQGKIKPGDTLLLYGFGAGLTWAAL 320
|
....
gi 746066411 325 WIKW 328
Cdd:PRK12879 321 LVKW 324
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
6-328 |
1.98e-123 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 357.08 E-value: 1.98e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 6 TAAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRIlKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVAT 85
Cdd:TIGR00747 2 YAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRI-AADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 86 VTPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGDG 165
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 166 AGAVLLEPATDGSGVLDSILRTDGSGRHYLNMKAGGSARPatietvtNKEHFAYQEGKTVFKFAVKGMADVSAELLERNN 245
Cdd:TIGR00747 161 AGAVVLGESEDPGGIISTHLGADGTQGEALYLPAGGRPTS-------GPSPFITMEGNEVFKHAVRKMGDVVEETLEANG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 246 LTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGFTWGA 323
Cdd:TIGR00747 234 LDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELlrTGRIKPGDLLLLVAFGGGLTWGA 313
|
....*
gi 746066411 324 TWIKW 328
Cdd:TIGR00747 314 ALVRF 318
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
7-328 |
1.29e-102 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 306.28 E-value: 1.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 7 AAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILKGEGKATSdMAVPAVLELCKKRGIDPVEIDCMIVATV 86
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTS-LAVEAAKKALEMAGVDPEDVDLVLLCTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 87 TPDMVFpATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGDGA 166
Cdd:PLN02326 127 SPDDLF-GSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 167 GAVLLEPATD-GSGVLDSILRTDGSGRHYLNMK-------AGGSARPATIETVTNKEHFA--YQEGKTVFKFAVKGMADV 236
Cdd:PLN02326 206 GAVVLQACDDdEDGLLGFDMHSDGNGHKHLHATfkgedddSSGGNTNGVGDFPPKKASYSciQMNGKEVFKFAVRCVPQV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 237 SAELLERNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEWEKE--LKKGDNLVLAA 314
Cdd:PLN02326 286 IESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSgkVKKGDVIATAG 365
|
330
....*....|....
gi 746066411 315 FGGGFTWGATWIKW 328
Cdd:PLN02326 366 FGAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
7-328 |
6.07e-86 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 261.80 E-value: 6.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 7 AAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRiLKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATV 86
Cdd:CHL00203 3 VHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRH-LAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 87 TPDMVFpATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGDGA 166
Cdd:CHL00203 82 TPDDLF-GSASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 167 GAVLLEPATDGSgVLDSILRTDGSGRHYLNM--KAGGSARPATIETVTNKEHFAYQEGKTVFKFAVKGMADVSAELLERN 244
Cdd:CHL00203 161 GAAIIGASYENS-ILGFKLCTDGKLNSHLQLmnKPVNNQSFGTTKLPQGQYQSISMNGKEVYKFAVFQVPAVIIKCLNAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 245 NLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWE-W-EKELKKGDNLVLAAFGGGFTWG 322
Cdd:CHL00203 240 NISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEaIqNNKIQPGQIIVLSGFGAGLTWG 319
|
....*.
gi 746066411 323 ATWIKW 328
Cdd:CHL00203 320 AIVLKW 325
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
9-328 |
3.32e-78 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 241.93 E-value: 3.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 9 ITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILKgEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATVTP 88
Cdd:PRK05963 6 IAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAA-PDETLSDLAASAGDMALSDAGIERSDIALTLLATSTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 89 DMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRyKKVVVVGADKMSAIIDYSDRNTCVIFGDGAGA 168
Cdd:PRK05963 85 DHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 169 VLLEP-ATDGSGVLDSILRTDGSGRHYLNMKAGGSARPATIETVTNKEHFAYQEGKTVFKFAVKGMADVSAELLERNNLT 247
Cdd:PRK05963 164 VVLAPsAKANSGVLGSQLISDGSHYDLIKIPAGGSARPFAPERDASEFLMTMQDGRAVFTEAVRMMSGASQNVLASAAMT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 248 GDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCL--WEWEKELKKGDNLVLAAFGGGFTWGATW 325
Cdd:PRK05963 244 PQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLslANLEQPLREGERLLFAAAGAGMTGGAVV 323
|
...
gi 746066411 326 IKW 328
Cdd:PRK05963 324 MRV 326
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
7-322 |
1.37e-58 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 191.59 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 7 AAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILKGEgkATSDMAVPAVLELCKKRGIDPVEIDCMIVATV 86
Cdd:PRK07204 5 ISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVDGE--TSSYMGAEAAKKAVEDAKLTLDDIDCIICASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 87 TPDMVFPATANIVCDKIGAVNAwG---YDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFG 163
Cdd:PRK07204 83 TIQQAIPCTASLIQEQLGLQHS-GipcFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 164 DGAGAVLLEPATDGSGVLDSILRTDGSGRHYLNMKAGGSARPATIETVTNKEHFAYQ-EGKTVFKFAVKGMADVSAELLE 242
Cdd:PRK07204 162 DGAAAVVITKGDHSSRILASHMETYSSGAHLSEIRGGGTMIHPREYSEERKEDFLFDmNGRAIFKLSSKYLMKFIDKLLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 243 RNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGFT 320
Cdd:PRK07204 242 DAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAikQKKVQRGNKILLLGTSAGLS 321
|
..
gi 746066411 321 WG 322
Cdd:PRK07204 322 IG 323
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
9-323 |
8.98e-51 |
|
"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: 171.08 E-value: 8.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 9 ITAVGGYVPEDKLTNFDLEKMVdtNDEWIRTRTGISERRILkGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATVTP 88
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMA-GDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 89 DMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTcVIFGDGAGA 168
Cdd:cd00827 81 IDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALE-PTLGDGAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 169 VLLEP-ATDGSGVLDSILRTDGSGRHYLNMKAGGSARPATiETVTNKEHFAY-QEGKTVFKFAVKGMADVSAELLERNNL 246
Cdd:cd00827 160 MLVSRnPGILAAGIVSTHSTSDPGYDFSPYPVMDGGYPKP-CKLAYAIRLTAePAGRAVFEAAHKLIAKVVRKALDRAGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 247 tGDDIAWLVPHQAN-LRIIDATAERMNLPKEKV----MVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGF 319
Cdd:cd00827 239 -SEDIDYFVPHQPNgKKILEAVAKKLGGPPEKAsqtrWILLRRVGNMYAASILLGLASLleSGKLKAGDRVLLFSYGSGF 317
|
....
gi 746066411 320 TWGA 323
Cdd:cd00827 318 TAEA 321
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
241-328 |
1.36e-41 |
|
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: 139.56 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 241 LERNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGG 318
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAveEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 746066411 319 FTWGATWIKW 328
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
3-328 |
4.66e-40 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 143.61 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 3 NKITAAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRIlKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMI 82
Cdd:PRK06840 1 MEMNVGIVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPV-PGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 83 -VATVTPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIES-GRYKKVVVVGADKMSAIIDYSDRNTCV 160
Cdd:PRK06840 80 yIGSEHKDYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLYSdPSIENVLLVGGYRNSDLVDYDNPRTRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 161 IF--GDGAGAVLLEPATDGSGVLDSILRTDGSGRHYLNMKAGGSARPATIETVTNKEHFAYQEGKTVFKfavKGMADVSA 238
Cdd:PRK06840 160 MFnfAAGGSAALLKKDAGKNRILGSAIITDGSFSEDVRVPAGGTKQPASPETVENRQHYLDVIDPESMK---ERLDEVSI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 239 --------ELLERNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVmVNIQRYGNTTAGTIPLCLWEWEKE--LKKGD 308
Cdd:PRK06840 237 pnflkvirEALRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLTEEQA-IYLDEYGHLGQLDQILSLHLALEQgkLKDGD 315
|
330 340
....*....|....*....|
gi 746066411 309 NLVLAAFGGGFTWGATWIKW 328
Cdd:PRK06840 316 LVVLVSAGTGYTWAATVIRW 335
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
111-189 |
2.70e-36 |
|
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: 125.71 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 111 YDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVIFGDGAGAVLLEPATD-GSGVLDSILRTDG 189
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEpGARILDSVLGSDG 80
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
7-328 |
3.19e-36 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 133.94 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 7 AAITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTR----TGIsERRILKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMI 82
Cdd:PRK12880 8 AKISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGL-NTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 83 VATVTPDMVFPATANIVCDKIG-AVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGaDKMSAIIDYSDRNTCVI 161
Cdd:PRK12880 87 VVTQSPDFFMPSTACYLHQLLNlSSKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 162 FGDGAGAVLLEPATDGSGVLDsiLRTDGSGRHYLNMKAGGSARPAT----------IETVTNKEHFaYQEGKTVFKFAVK 231
Cdd:PRK12880 166 FGDGVSATLIEKTDFNEAFFE--LGSDGKYFDKLIIPKGAMRIPKAdifnddslmqTEEFRQLENL-YMDGANIFNMALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 232 GMADVSAELLERNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNI-QRYGNTTAGTIP--LCLWEWEKELKKgd 308
Cdd:PRK12880 243 CEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPNFImEKYANLSACSLPalLCELDTPKEFKA-- 320
|
330 340
....*....|....*....|
gi 746066411 309 nlVLAAFGGGFTWGATWIKW 328
Cdd:PRK12880 321 --SLSAFGAGLSWGSAVLNF 338
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
59-323 |
6.85e-30 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 116.90 E-value: 6.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 59 MAVPAVLELCKKRGIDPVEIDCMIVATVTPDMVFPATANIVCDKIGAvNAWGYDLSAACSGFLFALTSGAAYIESGRYKK 138
Cdd:PRK07515 98 MGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGI-EGFAFDMNVACSSATFGIQTAANAIRSGSARR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 139 VVVVGADKMSAIIDYSDRNTCVIFGDGAGAVLLEPATDGSG-----VLDSILRTDGSG--RH---YLNmkaggSARPATI 208
Cdd:PRK07515 177 VLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATSaggfeILGTRLFTQFSNniRNnfgFLN-----RADPEGI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 209 eTVTNKeHFaYQEGKTVFKFAVKGMADVSAELLERNNLTGDDIA--WLvpHQANLRIIDATAERMnL-----PKEKVMVn 281
Cdd:PRK07515 252 -GARDK-LF-VQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKKV-LgrdatPEEAPVI- 324
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 746066411 282 IQRYGNT-TAGTIpLCLWEWEKELKKGDNLVLAAFGGGFTWGA 323
Cdd:PRK07515 325 LDEYANTsSAGSI-IAFHKHSDDLAAGDLGVICSFGAGYSIGS 366
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
41-328 |
2.01e-24 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 101.50 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 41 TGISERRiLKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATVTPDMVFPATANIVCDKIG-AVNAWGYDLSAACSG 119
Cdd:PRK09258 47 TGIRERR-WWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGlPKSCANFDVSNACLG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 120 FLFALTSGAAYIESGRYKKVVVVGADKMSAIID------YSDRNTCVIF---------GDGAGAVLLepaTDGSgvldsi 184
Cdd:PRK09258 126 FLNGMLDAANMIELGQIDYALVVSGESAREIVEatidrlLAPETTREDFaqsfatltlGSGAAAAVL---TRGS------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 185 lrtDGSGRHYLNmkaGGSARPATietvtnkEH---------FAYQEGKTVFKFAVKGMADVSAELLERNNLTGDDIAWLV 255
Cdd:PRK09258 197 ---LHPRGHRLL---GGVTRAAT-------EHhelcqggrdGMRTDAVGLLKEGVELAVDTWEAFLAQLGWAVEQVDRVI 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746066411 256 PHQANLRIIDATAERMNLPKEKVMVNIQRYGNTTAGTIP--LCLWEWEKELKKGDNLVLAAFGGGFTWGATWIKW 328
Cdd:PRK09258 264 CHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPitLAMAAEEGFLKPGDRVALLGIGSGLNCSMLEVKW 338
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
106-323 |
7.91e-18 |
|
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: 82.68 E-value: 7.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 106 VNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIID------------------YSDRNTCVIFGDGAG 167
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDcefdamgalstpekasrtFDAAADGFVFGDGAG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 168 AVLLEPATDGSGVLDSILRT-DGSGRHYLNMKAGgsarpatietvtnkehfayqegktVFKFAVKGMADVSAELLERNNL 246
Cdd:cd00825 165 ALVVEELEHALARGAHIYAEiVGTAATIDGAGMG------------------------AFAPSAEGLARAAKEALAVAGL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 247 TGDDIAWLVPHQANLRIIDATAERMNLPKEK-----VMVNIQRYGNTTAGTIPLCLWEWEKELK---------------- 305
Cdd:cd00825 221 TVWDIDYLVAHGTGTPIGDVKELKLLRSEFGdkspaVSATKAMTGNLSSAAVVLAVDEAVLMLEhgfippsihieeldea 300
|
250 260
....*....|....*....|....*....
gi 746066411 306 -----------KGDNLVLAAFGGGFTWGA 323
Cdd:cd00825 301 glnivtettprELRTALLNGFGLGGTNAT 329
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
9-312 |
2.99e-17 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 81.49 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 9 ITAVGGYVPEDKLTNFDLEK---MVDTNDEWIRTR----TGISERR-ILKGEGKAT---SDMAVPAVLELCKKRGIDPVE 77
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEAylgLINGKPSRARRIilrnNGIKTRHyALDPEGRPThsnAQMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 78 IDCMIVATVTPDMVFPATANIVCDKIGA----VNAwgydLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDY 153
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVHGELGAppieVVS----SAGVCAAGMMALKYAYLSVKAGESRNAVATASELASRWFRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 154 S------------DRNTCVIF---------GDGAGAVLLEPATDGSGV---LDSILRTDGSGRHYLNMKAGGSARPAtiE 209
Cdd:PRK06816 161 SrfeaeeeklaelEENPEIAFekdflrwmlSDGAGAVLLENKPRPDGLslrIDWIDLRSYAGELPVCMYAGAEKNED--G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 210 TVTNKEHFAYQEGKTVFKFAVK------------GMADVSAELLERNNLTGDDIAWLVPHQANLRIIDATAERM-----N 272
Cdd:PRK06816 239 SLKGWSDYPPEEAEAASALSLKqdvrllnenivvYTIKPLLELVDKRNLDPDDIDYFLPHYSSEYFREKIVELLakagfM 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 746066411 273 LPKEKVMVNIQRYGNTTAGTIPLCLWEW--EKELKKGDNLVL 312
Cdd:PRK06816 319 IPEEKWFTNLATVGNTGSASIYIMLDELlnSGRLKPGQKILC 360
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
72-323 |
3.06e-17 |
|
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: 79.80 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 72 GIDPVEIDCMIVATVTPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKmsaii 151
Cdd:cd00327 23 GLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 152 dysdrntcVIFGDGAGAVLLEpatdgsgvldsilrtdgSGRHYLnmKAGGSARPATIETVTNkehfayQEGKTV-FKFAV 230
Cdd:cd00327 98 --------FVFGDGAAAAVVE-----------------SEEHAL--RRGAHPQAEIVSTAAT------FDGASMvPAVSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 231 KGMADVSAELLERNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEK-----VMVNIQRYGNTTAGTIPL----CLWEWE 301
Cdd:cd00327 145 EGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvrspaVSATLIMTGHPLGAAGLAildeLLLMLE 224
|
250 260
....*....|....*....|....*..
gi 746066411 302 KELKK-----GDNLVLAAFGGGFTWGA 323
Cdd:cd00327 225 HEFIPptprePRTVLLLGFGLGGTNAA 251
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
6-320 |
5.06e-16 |
|
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: 78.03 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 6 TAAITAVGGYVPEDKLT----------NFDLEKMVDTND--EWIRTRTGISERRILKGEG--------------KATSDM 59
Cdd:cd00831 1 AATILAIGTAVPPHRVPqselvdfyrrLFSSDHLPELKEklKRLCAKTGIETRYLVLPGGeetyaprpemspslDERNDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 60 AVPAVLELC--------KKRGIDPVEIDCMIVATVTpdmvFPAT----ANIVcDKIG------AVNAWGydlsAACSGFL 121
Cdd:cd00831 81 ALEEARELAeeaargalDEAGLRPSDIDHLVVNTST----GNPTpsldAMLI-NRLGlrpdvkRYNLGG----MGCSAGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 122 FALTSGAAYIESGRYKKVVVV----------GADKMSAIIdysdrNTCvIFGDGAGAVLLEPATDGSGVLDSILRTDGSG 191
Cdd:cd00831 152 IALDLAKDLLEANPGARVLVVstelcslwyrGPDHRSMLV-----GNA-LFGDGAAAVLLSNDPRDRRRERPLFELVRAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 192 RHylnmkaggsARPATIETVT---NKEHFAYQEGKTVFKFAVKGMADVSAELLERN---NLTGDDIAWLVpHQANLRIID 265
Cdd:cd00831 226 ST---------LLPDSEDAMGwhlGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgigLFKLAFDHWCV-HPGGRAVLD 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746066411 266 ATAERMNLPKEKV----MVnIQRYGNTTAGTIPLCLWEWEKE--LKKGDNLVLAAFGGGFT 320
Cdd:cd00831 296 AVEKALGLSPEDLeasrMV-LRRYGNMSSSSVLYVLAYMEAKgrVKRGDRGLLIAFGPGFT 355
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
42-150 |
5.86e-13 |
|
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: 68.83 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 42 GISERRILKGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATVTPDMVFPATANIVCDKIGAVNAWGYDLSAACSGFL 121
Cdd:cd00829 2 GVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGS 81
|
90 100
....*....|....*....|....*....
gi 746066411 122 FALTSGAAYIESGRYKKVVVVGADKMSAI 150
Cdd:cd00829 82 AAVRAAAAAIASGLADVVLVVGAEKMSDV 110
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
6-320 |
1.54e-11 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 64.39 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 6 TAAITAVGGYVPE---------------DKLTNFDLEKM--------VDT-----NDEWIRTRTGISER-RILKGEGKat 56
Cdd:COG3424 1 SARILSIATAVPPhrytqeeiaefaaelFGLDERDRRRLrrlfensgIETrhsvlPLEWYLEPPSFGERnALYIEEAL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 57 sDMAVPAVLELCKKRGIDPVEIDCMIVATVT----P--------DMVFPATANIVCdkigaVNAWGydlsaaCSGFLFAL 124
Cdd:COG3424 79 -ELAEEAARRALDKAGLDPEDIDHLVTVSCTgfaaPgldarlinRLGLRPDVRRLP-----VGGMG------CAAGAAGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 125 TSGAAYIESGRYKKVVVV-----------GADKMSAIIDYSdrntcvIFGDGAGAVLLEPATDGSGVLD-----SILRTD 188
Cdd:COG3424 147 RRAADFLRADPDAVVLVVcvelcsltfqrDDDSKDNLVANA------LFGDGAAAVVVSGDPRPGPGPRilafrSYLIPD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 189 GSGRHYLNMKAGG-----SAR-PATIEtvtnkehfayqegktvfkfavKGMADVSAELLERNNLTGDDIAWLVPHQANLR 262
Cdd:COG3424 221 TEDVMGWDVGDTGfrmvlSPEvPDLIA---------------------EHLAPAVEPLLARHGLTIEDIDHWAVHPGGPK 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 746066411 263 IIDATAERMNLPKEK------VMvniQRYGNTTAGTIPLCLWEW--EKELKKGDNLVLAAFGGGFT 320
Cdd:COG3424 280 VLDAVEEALGLPPEAlahsreVL---REYGNMSSATVLFVLERLleEGAPAPGERGLAMAFGPGFT 342
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
9-318 |
1.22e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 61.85 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 9 ITAVGGYVPEDKLTNFDLEKMVDTNDEWIRTRTGISERRILkGEGKATSDMAVPAVLELCKKRGIDPVEIDCMIVATVTP 88
Cdd:PRK04262 5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVP-GPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSESH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 89 DMVFPATANIVCDKIGAV-NAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADKMSA----IIDYSDRN---TCV 160
Cdd:PRK04262 84 PYAVKPTATIVAEALGATpDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAQGapgdALEYTAAAggaAFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 161 IFGDGAGAVLLEPATDGSGVLDSILRtdgSGRHYlnMKAGG--SARPATIETVTNkehfayqegktvfkfAVKGmadvsa 238
Cdd:PRK04262 164 IGKEEVIAEIEATYSYTTDTPDFWRR---EGEPY--PRHGGrfTGEPAYFKHIIS---------------AAKG------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 239 eLLERNNLTGDDIAWLVPHQANLRIIDATAERMNLPKEKVMVNI--QRYGNTTAGTIPLCLWEWEKELKKGDNLVLAAFG 316
Cdd:PRK04262 218 -LMEKLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGLAAVLDVAKPGDRILVVSFG 296
|
..
gi 746066411 317 GG 318
Cdd:PRK04262 297 SG 298
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
9-318 |
8.99e-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: 56.34 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 9 ITAVGGYVPEDKLT--------NFDLEKMVDTndewirtrTGISERRI-LKGEGKATsdMAVPAVLELCKKRGIDPVEID 79
Cdd:COG3425 5 IDAIGFYIPRYRLDleelaearGVDPEKYTKG--------LGQEEKSVpPPDEDAVT--MAANAARRALDRAGIDPSDIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 80 CMIVATVT-PDMVFPaTANIVcdkIGAV----NAWGYDLSAACSGFLFALTSGAAYIESGRYKKVVVVGADK-MSAIIDY 153
Cdd:COG3425 75 AVYVGTESgPDASKP-IATYV---HGALglppNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIaRYGPGSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 154 SDrntcVIFGDGAGAVLLEPAtdgsgvlDSILRTDGSGRHYlnmkaggsarpaTIETV----TNKEHFAYQEGktvfKFA 229
Cdd:COG3425 151 GE----YTQGAGAVAMLVGAD-------PRIAEIEGGSGSY------------TTDVMdfwrPNGSDYPLVDG----RFS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 230 VKG----MADVSAELLERNNLTGDDIAWLVPHQ---------ANLRIIDATAERMNLPKEKVMVNI---QRYGNTTAGTI 293
Cdd:COG3425 204 EPAyldhLEEAVKDYKEKTGLKPDDFDYFVFHQpfgkmpkkaAKKLGRKAGREIQEDFEEQVEPSLiysRRIGNTYTGSL 283
|
330 340
....*....|....*....|....*...
gi 746066411 294 PLCL---WEwEKELKKGDNLVLAAFGGG 318
Cdd:COG3425 284 YLGLaslLD-NAKDLPGDRIGLFSYGSG 310
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
96-270 |
9.41e-05 |
|
"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: 43.97 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 96 ANIVCDKIgavnAWGYDLS--------AACSGFLFALTSGAAYIESGRYKKVVVVGADKMSAIIDYSDRNTCVI------ 161
Cdd:cd00828 137 PNTVAGWV----NILLLSShgpiktpvGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALstaeee 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 162 --------FGDGAGAVLLEpatdGSGVLdsILRTDgsgRHYLNMKAGGSARPATIETVTNKEHfAYQEGktvfkfAVKGM 233
Cdd:cd00828 213 peemsrpfDETRDGFVEAE----GAGVL--VLERA---ELALARGAPIYGRVAGTASTTDGAG-RSVPA------GGKGI 276
|
170 180 190
....*....|....*....|....*....|....*..
gi 746066411 234 ADVSAELLERNNLTGDDIAWLVPHQANLRIIDATAER 270
Cdd:cd00828 277 ARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
58-148 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 58 DMAVPAVLELCKKRGIDPVEIDCMIVATVTPDmvfPATANIvcdkigAVNAW----------GYDLSAACSGFLFALTSG 127
Cdd:cd00751 24 DLGAAVIKALLERAGLDPEEVDDVIMGNVLQA---GEGQNP------ARQAAllaglpesvpATTVNRVCGSGLQAVALA 94
|
90 100
....*....|....*....|.
gi 746066411 128 AAYIESGRYKKVVVVGADKMS 148
Cdd:cd00751 95 AQSIAAGEADVVVAGGVESMS 115
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
58-148 |
3.30e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 42.19 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 58 DMAVPAVLELCKKRGIDPVEIDCMIVATVTPDMVF--PATANIVCDKIGAVNAWGYDLSAAC-SGFLfALTSGAAYIESG 134
Cdd:PRK06064 24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVsqEHIAALIADYAGLAPIPATRVEAACaSGGA-ALRQAYLAVASG 102
|
90
....*....|....
gi 746066411 135 RYKKVVVVGADKMS 148
Cdd:PRK06064 103 EADVVLAAGVEKMT 116
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
58-148 |
9.56e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 37.35 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746066411 58 DMAVPAVLELCKKRGIDPVEIDCMIVATVTPDMVFPATANIVCDKIGA-VNAWGYDLSAACSGFLFALTSGAAYIESGRY 136
Cdd:COG0183 28 DLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLpESVPAVTVNRVCGSGLQAVALAAQAIAAGDA 107
|
90
....*....|..
gi 746066411 137 KKVVVVGADKMS 148
Cdd:COG0183 108 DVVIAGGVESMS 119
|
|
| |
