|
Name |
Accession |
Description |
Interval |
E-value |
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
6-314 |
1.40e-87 |
|
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: 265.05 E-value: 1.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 6 DLDKQFGFARGHLERLSGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGI 85
Cdd:COG0332 21 DLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFPSTACLVQHKLGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 86 PegNAAAFDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEqPDVAALFGDG-------AAavvltvaa 158
Cdd:COG0332 101 K--NAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTD-RSTCVLFGDGagavvleAS-------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 159 ERDSTIRASVMRTYPSAYEACEIGAGGTRFDFQRQPAEfaaHAVFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVDL 238
Cdd:COG0332 170 EEGPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEG---DHYLRMDGREVFKFAVRNLPEVIREALEKAGLTLDDIDW 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499854147 239 VVPHQASPLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAIE 314
Cdd:COG0332 247 FIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAVLR 322
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
2-314 |
7.65e-84 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 255.92 E-value: 7.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 2 VLSTDLDKQFGFARGHLERLSGVFSRHVCqEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMH 81
Cdd:PRK07204 19 VDSLELDKKLDLPEGWVLKKSGVKTRHFV-DGETSSYMGAEAAKKAVEDAKLTLDDIDCIICASGTIQQAIPCTASLIQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 82 RLGIPEGNAAAFDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWkEQPDVAALFGDGAAAVVLTVAAErD 161
Cdd:PRK07204 98 QLGLQHSGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNW-GQNESCILFGDGAAAVVITKGDH-S 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 162 STIRASVMRTYPSAYEACEIGAGGTRFdfqrQPAEFA----AHAVFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVD 237
Cdd:PRK07204 176 SRILASHMETYSSGAHLSEIRGGGTMI----HPREYSeerkEDFLFDMNGRAIFKLSSKYLMKFIDKLLMDAGYTLADID 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499854147 238 LVVPHQASPLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAIE 314
Cdd:PRK07204 252 LIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSIGGILLE 328
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
6-313 |
3.99e-78 |
|
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: 240.90 E-value: 3.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 6 DLDKQFGFARGHLERLSGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGI 85
Cdd:cd00830 20 ELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLVQARLGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 86 PegNAAAFDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQpDVAALFGDGAAAVVLTVAAErDSTIR 165
Cdd:cd00830 100 K--NAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDR-STAVLFGDGAGAVVLEATEE-DPGIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 166 ASVMRTYPSAYEACEIGAGGTRFDFQRQPAEFAAhavFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQAS 245
Cdd:cd00830 176 DSVLGSDGSGADLLTIPAGGSRSPFEDAEGGDPY---LVMDGREVFKFAVRLMPESIEEALEKAGLTPDDIDWFVPHQAN 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499854147 246 PLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAI 313
Cdd:cd00830 253 LRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
22-310 |
1.18e-52 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 175.44 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 22 SGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPegNAAAFDVNASCLS 101
Cdd:PRK12879 39 TGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQVQARLGIP--NAAAFDINAACAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 102 FLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQpDVAALFGDGAAAVVLTVAAERDSTIrASVMRTYPSAYEACEI 181
Cdd:PRK12879 117 FLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDR-TTCILFGDGAGAVVLEATENEPGFI-DYVLGTDGDGGDILYR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 182 GAGGTRFDfqrqPAEFAAHAVFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQASPLALKHMIQQTGMPGA 261
Cdd:PRK12879 195 TGLGTTMD----RDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPME 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2499854147 262 RVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGG 310
Cdd:PRK12879 271 KTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAA 319
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
22-313 |
8.55e-50 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 167.94 E-value: 8.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 22 SGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIpeGNAAAFDVNASCLS 101
Cdd:PRK09352 38 TGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPDYAFPSTACLVQARLGA--KNAAAFDLSAACSG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 102 FLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQpDVAALFGDGAAAVVLTVAAERDstIRASVMRTYPSAYEACEI 181
Cdd:PRK09352 116 FVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDR-STCVLFGDGAGAVVLGASEEPG--ILSTHLGSDGSYGDLLYL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 182 GAGGTrfdfqRQPAEFAAhavFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQASPLALKHMIQQTGMPGA 261
Cdd:PRK09352 193 PGGGS-----RGPASPGY---LRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGLPME 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2499854147 262 RVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAI 313
Cdd:PRK09352 265 KVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALV 316
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
22-313 |
7.64e-42 |
|
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: 147.14 E-value: 7.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 22 SGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPegNAAAFDVNASCLS 101
Cdd:TIGR00747 37 TGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVATTTPDHAFPSAACMVQAYLGIK--GIPAFDLSAACAG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 102 FLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQpDVAALFGDGAaAVVLTVAAERDSTIRASvmrtypsayeacEI 181
Cdd:TIGR00747 115 FIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDR-GTCVLFGDGA-GAVVLGESEDPGGIIST------------HL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 182 GAGGTRFDFQRQPAEFA---AHAVF-RMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQASPLALKHMIQQTG 257
Cdd:TIGR00747 181 GADGTQGEALYLPAGGRptsGPSPFiTMEGNEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLE 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2499854147 258 MPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAI 313
Cdd:TIGR00747 261 LDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALV 316
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
2-309 |
4.66e-40 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 142.55 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 2 VLSTDLDKQFGFARGHLERLSGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMH 81
Cdd:PRK05963 18 VENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATSTPDHLLPPSAPLLAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 82 RLGIpeGNAAAFDVNASCLSFLTAVDLAAGRIAVgQSRVALVFSAEIASRALPwKEQPDVAALFGDGAAAVVLTVAAERD 161
Cdd:PRK05963 98 RLGL--QNSGAIDLAGACAGFLYALVLADGFVRA-QGKPVLVVAANILSRRIN-MAERASAVLFADAAGAVVLAPSAKAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 162 STIRASVMRTYPSAYEACEIGAGGTRFDFQRQPAefAAHAVFRM-DGKELFRITRRHFPGFVDELLAAAGWSPADVDLVV 240
Cdd:PRK05963 174 SGVLGSQLISDGSHYDLIKIPAGGSARPFAPERD--ASEFLMTMqDGRAVFTEAVRMMSGASQNVLASAAMTPQDIDRFF 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499854147 241 PHQASPLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFG 309
Cdd:PRK05963 252 PHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGG 320
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
2-314 |
5.68e-33 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 124.22 E-value: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 2 VLSTDLDKQ-------FGFARGHLERLSGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGaCGVPYQPL-P 73
Cdd:PRK09258 20 VTSSEIEERlaplyerLRLPPGQLEALTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLIN-TSVCRDYLeP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 74 TTAPLVMHRLGIPeGNAAAFDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASralPWKE-------QPD------ 140
Cdd:PRK09258 99 ATACRVHHNLGLP-KSCANFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGESAR---EIVEatidrllAPEttredf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 141 -------------VAALFGDGAAAvvltvaaERDSTIRASVMRTYPSAYEACEIGAGGTRFDfqrqpaefaAHAVFRmDG 207
Cdd:PRK09258 175 aqsfatltlgsgaAAAVLTRGSLH-------PRGHRLLGGVTRAATEHHELCQGGRDGMRTD---------AVGLLK-EG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 208 KELFRITRRHFpgfvdelLAAAGWSPADVDLVVPHQASPLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWA 287
Cdd:PRK09258 238 VELAVDTWEAF-------LAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAE 310
|
330 340
....*....|....*....|....*..
gi 2499854147 288 EGRITKGMRLLLLGTSAGVSFGGMAIE 314
Cdd:PRK09258 311 EGFLKPGDRVALLGIGSGLNCSMLEVK 337
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
22-310 |
1.58e-32 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 123.69 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 22 SGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPyQPLPTTAPLVMHRLGIPegNAAAFDVNASCLS 101
Cdd:PLN02326 82 TGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSSP-DDLFGSAPQVQAALGCT--NALAFDLTAACSG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 102 FLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQpDVAALFGDGAAAVVLTVAAERDSTIRASVMRTYPSAY----- 176
Cdd:PLN02326 159 FVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDR-GTCILFGDGAGAVVLQACDDDEDGLLGFDMHSDGNGHkhlha 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 177 ---EACEIGAGGTRFDFQRQPAEFAAHAVFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQASPLALKHMI 253
Cdd:PLN02326 238 tfkGEDDDSSGGNTNGVGDFPPKKASYSCIQMNGKEVFKFAVRCVPQVIESALQKAGLTAESIDWLLLHQANQRIIDAVA 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2499854147 254 QQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGG 310
Cdd:PLN02326 318 QRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGFGAGLTWGS 374
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
226-314 |
3.30e-27 |
|
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: 101.81 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 226 LAAAGWSPADVDLVVPHQASPLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAG 305
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
....*....
gi 2499854147 306 VSFGGMAIE 314
Cdd:pfam08541 81 LTWGAALLR 89
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
22-314 |
3.60e-27 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 108.49 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 22 SGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPyQPLPTTAPLVMHRLGipEGNAAAFDVNASCLS 101
Cdd:CHL00203 37 TGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTP-DDLFGSASQLQAEIG--ATRAVAFDITAACSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 102 FLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQPDVAaLFGDGAAAVVLTVAAERdstiraSVMrtypsAYEACEI 181
Cdd:CHL00203 114 FILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCI-LFGDGAGAAIIGASYEN------SIL-----GFKLCTD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 182 GAGGTRFDFQRQPA---EFAAHAVF-------RMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQASPLALKH 251
Cdd:CHL00203 182 GKLNSHLQLMNKPVnnqSFGTTKLPqgqyqsiSMNGKEVYKFAVFQVPAVIIKCLNALNISIDEVDWFILHQANKRILEA 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499854147 252 MIQQTGMPGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAIE 314
Cdd:CHL00203 262 IANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTWGAIVLK 324
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
23-313 |
1.20e-25 |
|
"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: 104.05 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 23 GVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPegNAAAFDVNASCLSF 102
Cdd:cd00827 35 GIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLT--NAEAFDLKQACYGG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 103 LTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQPdvAALFGDGA-----AAVVLTVAAERDSTIRASVMRTYPSAYE 177
Cdd:cd00827 113 TAALQLAANLVESGPWRYALVVASDIASYLLDEGSAL--EPTLGDGAaamlvSRNPGILAAGIVSTHSTSDPGYDFSPYP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 178 ACEIGAGGTRFDFQRQP--AEFAAHAVFRMDGKELFRItrrhfpgfVDELLAAAGwSPADVDLVVPHQASPLALKHMIQQ 255
Cdd:cd00827 191 VMDGGYPKPCKLAYAIRltAEPAGRAVFEAAHKLIAKV--------VRKALDRAG-LSEDIDYFVPHQPNGKKILEAVAK 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2499854147 256 TGMPGARVVNI-----AARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAI 313
Cdd:cd00827 262 KLGGPPEKASQtrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTAEAFVL 324
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
23-314 |
1.33e-16 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 78.89 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 23 GVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIgACGVPYQ--PLPTTAPLVMHRLGIPegNAAAFDVNASCL 100
Cdd:PRK06840 40 GIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVI-YIGSEHKdyPVWSSAPKIQHEIGAK--NAWAFDIMAVCA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 101 SFLTAVDLAAGRIAVGQS-RVALVFSAEIASRALPWkEQPDVAALF--GDGaaavVLTVAAERDST---IRASVMRTYPS 174
Cdd:PRK06840 117 SFPIALKVAKDLLYSDPSiENVLLVGGYRNSDLVDY-DNPRTRFMFnfAAG----GSAALLKKDAGknrILGSAIITDGS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 175 AYEACEIGAGGTRFDFQRQPAEFAAHAvFRMDGKELFR-----ITRRHFPGFVDELLAAAGWSPADVDLVVPHQASPLAL 249
Cdd:PRK06840 192 FSEDVRVPAGGTKQPASPETVENRQHY-LDVIDPESMKerldeVSIPNFLKVIREALRKSGYTPKDIDYLAILHMKRSAH 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499854147 250 KHMIQQTGMPGARVVNIaARFGNQIAASIPTALDIAWAEGRITKGMRLLLLGTSAGVSFGGMAIE 314
Cdd:PRK06840 271 IALLEGLGLTEEQAIYL-DEYGHLGQLDQILSLHLALEQGKLKDGDLVVLVSAGTGYTWAATVIR 334
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
19-147 |
1.62e-14 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 73.37 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 19 ERLSGVFSRHVCQED----------------DDQITL----AVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPL 78
Cdd:PRK07515 58 EKASGIKSRYVMDKEgildpdrmrpripersNDELSIqaemGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIE 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499854147 79 VMHRLGIpEGnaAAFDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQpDVAALFGD 147
Cdd:PRK07515 138 IQQALGI-EG--FAFDMNVACSSATFGIQTAANAIRSGSARRVLVVNPEICSGHLNFRDR-DSHFIFGD 202
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
18-313 |
5.56e-12 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 65.76 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 18 LERLSGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIpEGNAAAFDVNA 97
Cdd:PRK12880 42 MKKVIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVVTQSPDFFMPSTACYLHQLLNL-SSKTIAFDLGQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 98 SCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPwkEQPDVAALFGDGaaavvltvaaerdstIRASVMRTYPSAYE 177
Cdd:PRK12880 121 ACAGYLYGLFVAHSLIQSGLGKILLICGDTLSKFIHP--KNMNLAPIFGDG---------------VSATLIEKTDFNEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 178 ACEIGAGGTRFD--------FQR------------QPAEFAAHAVFRMDGKELFRITRRHFPGFVDELLAAAGWSPADVD 237
Cdd:PRK12880 184 FFELGSDGKYFDkliipkgaMRIpkadifnddslmQTEEFRQLENLYMDGANIFNMALECEPKSFKEILEFSKVDEKDIA 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499854147 238 LVVPHQASPLALKHMIQQTGMPGARVVN-IAARFGNQIAASIPTALdiawAEGRITKGMRLLLLGTSAGVSFGGMAI 313
Cdd:PRK12880 264 FHLFHQSNAYLVDCIKEELKLNDDKVPNfIMEKYANLSACSLPALL----CELDTPKEFKASLSAFGAGLSWGSAVL 336
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
23-129 |
2.69e-11 |
|
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: 63.66 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 23 GVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLVIGA--CGvPYQPLPtTAPLVMHRLGIPEgNAAAFDVNASCL 100
Cdd:COG3425 38 GQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGteSG-PDASKP-IATYVHGALGLPP-NCRAFELKFACY 114
|
90 100
....*....|....*....|....*....
gi 2499854147 101 SFLTAVDLAAGRIAVGQSRVALVFSAEIA 129
Cdd:COG3425 115 AGTAALQAALGWVASGPNKKALVIASDIA 143
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
93-173 |
1.54e-10 |
|
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: 56.37 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 93 FDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKeQPDVAALFGDGAAAVVLTVAAERDSTIRASVMRTY 172
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWT-DRSTAVLFGDGAGAVVLEATDEPGARILDSVLGSD 79
|
.
gi 2499854147 173 P 173
Cdd:pfam08545 80 G 80
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
39-132 |
7.75e-09 |
|
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: 56.33 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 39 LAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPEgNAAAFDVNASCLSFLTAVDLAAGRIAVGQS 118
Cdd:cd00751 25 LGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPE-SVPATTVNRVCGSGLQAVALAAQSIAAGEA 103
|
90
....*....|....
gi 2499854147 119 RVALVFSAEIASRA 132
Cdd:cd00751 104 DVVVAGGVESMSRA 117
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
39-301 |
9.36e-08 |
|
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: 53.00 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 39 LAVAAARLAMQKAAVGPGEIDLVIGACGVPYqPLPTTAPLVMHRLGIPEgnaaafDVNASCLSFL------TAVDLAAGR 112
Cdd:cd00831 88 LAEEAARGALDEAGLRPSDIDHLVVNTSTGN-PTPSLDAMLINRLGLRP------DVKRYNLGGMgcsagaIALDLAKDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 113 IAVGQSRVALVFSAEIASRALPWKEQPD---VAALFGDGAAAV--VLTVAAERDSTIRASVMRTYPSAYEACE------I 181
Cdd:cd00831 161 LEANPGARVLVVSTELCSLWYRGPDHRSmlvGNALFGDGAAAVllSNDPRDRRRERPLFELVRAASTLLPDSEdamgwhL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 182 GAGGTRFDFQRQPAEFAAHAVFRMdgkelfritrrhfpgfVDELLAAA--GWSPADVDLVVPHQASPLALKHMIQQTGMP 259
Cdd:cd00831 241 GEEGLTFVLSRDVPRLVEKNLERV----------------LRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLS 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2499854147 260 GARVV---NIAARFGNQIAASIPTALDIAWAEGRITKGMRLLLLG 301
Cdd:cd00831 305 PEDLEasrMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIA 349
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
39-132 |
1.16e-07 |
|
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: 52.76 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 39 LAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPEgNAAAFDVNASCLSFLTAVDLAAGRIAVGQS 118
Cdd:COG0183 29 LGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPE-SVPAVTVNRVCGSGLQAVALAAQAIAAGDA 107
|
90
....*....|....
gi 2499854147 119 RVALVFSAEIASRA 132
Cdd:COG0183 108 DVVIAGGVESMSRA 121
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
7-242 |
5.58e-07 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 50.52 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 7 LDKQFGFARGHLERLSGVF------SRHVCQEDDDQIT-----------------LAVAAARLAMQKAAVGPGEIDLVIG 63
Cdd:COG3424 25 AAELFGLDERDRRRLRRLFensgieTRHSVLPLEWYLEppsfgernalyieealeLAEEAARRALDKAGLDPEDIDHLVT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 64 ACgvpyqplpTT---AP----LVMHRLGIPE----------GNAAAFdvNAscLSflTAVDLAAGRiavgQSRVALVFSA 126
Cdd:COG3424 105 VS--------CTgfaAPgldaRLINRLGLRPdvrrlpvggmGCAAGA--AG--LR--RAADFLRAD----PDAVVLVVCV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 127 EIASRALpwkeQPD--------VAALFGDGAAAVVLTVAAERDS--TIRASVMRTYPSAYE--ACEIGAGGTRFDFqrqp 194
Cdd:COG3424 167 ELCSLTF----QRDddskdnlvANALFGDGAAAVVVSGDPRPGPgpRILAFRSYLIPDTEDvmGWDVGDTGFRMVL---- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2499854147 195 aefaahavfrmdGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPH 242
Cdd:COG3424 239 ------------SPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVH 274
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
38-311 |
1.37e-06 |
|
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: 48.59 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 38 TLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPEGnaAAFDVNASCLSFLTAVDLAAGRIAVGQ 117
Cdd:cd00327 9 ELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGG--PAYSVNQACATGLTALALAVQQVQNGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 118 SRVALVFSAEIAsralpwkeqpdvaaLFGDGAAAVVLTVAAErdstirASVMRTYPSAyeacEIGAGGTRFDfqrqpaef 197
Cdd:cd00327 87 ADIVLAGGSEEF--------------VFGDGAAAAVVESEEH------ALRRGAHPQA----EIVSTAATFD-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 198 AAHAVFRMDGKELFRItrrhfpgfVDELLAAAGWSPADVDLVVPHQA-----SPLALKHMIQQTGMPGARVVNIAARFGN 272
Cdd:cd00327 135 GASMVPAVSGEGLARA--------ARKALEGAGLTPSDIDYVEAHGTgtpigDAVELALGLDPDGVRSPAVSATLIMTGH 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2499854147 273 QIAASIPTALDIAWAEGRITKGMRLLLLGTSAGV-SFGGM 311
Cdd:cd00327 207 PLGAAGLAILDELLLMLEHEFIPPTPREPRTVLLlGFGLG 246
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
38-283 |
3.96e-06 |
|
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: 47.63 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 38 TLAVAAARLAMQKAAVGP----GEIDLVIGACG-----------------VPYQPLPTTAPLVMHRLGIPEG-NAAAFDV 95
Cdd:cd00825 13 ILGFEAAERAIADAGLSReyqkNPIVGVVVGTGggsprfqvfgadamravGPYVVTKAMFPGASGQIATPLGiHGPAYDV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 96 NASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIASRALPWKEQPDVAALFGDGAAavvltvaaerdstirasvmRTYPSA 175
Cdd:cd00825 93 SAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKAS-------------------RTFDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 176 YEACEIGAGG----------TRFDFQRQPAEFAAHAV-FRMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQA 244
Cdd:cd00825 154 ADGFVFGDGAgalvveelehALARGAHIYAEIVGTAAtIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2499854147 245 S-----PLALKHMIQQTGMPGARVVNIAARFGNQIAASIPTALD 283
Cdd:cd00825 234 GtpigdVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVD 277
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
12-129 |
5.52e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 47.21 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 12 GFARGHLERLSGVFSRHVCQEDDDQITLAVAAARLAMQKAAVGPGEIDLV-IGACGVPYQPLPtTAPLVMHRLGIPEgNA 90
Cdd:PRK04262 27 GDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVyVGSESHPYAVKP-TATIVAEALGATP-DL 104
|
90 100 110
....*....|....*....|....*....|....*....
gi 2499854147 91 AAFDVNASCLSFLTAVDLAAGRIAVGQSRVALVFSAEIA 129
Cdd:PRK04262 105 TAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTA 143
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
33-132 |
7.55e-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: 46.87 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 33 DDDQITLAVAAARLAMQKAAVGPGEIDLVIGACGVPYQPLPTTAPLVMHRLGIPegNAAAFDVNASCLSFLTAVDLAAGR 112
Cdd:cd00829 13 DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL--GKPATRVEAAGASGSAAVRAAAAA 90
|
90 100
....*....|....*....|
gi 2499854147 113 IAVGQSRVALVFSAEIASRA 132
Cdd:cd00829 91 IASGLADVVLVVGAEKMSDV 110
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
39-299 |
1.87e-04 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 42.59 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 39 LAVAAARLAMQKAAVGPGEIDLVigACGV--PYQPLPTTAPLVMHRLGIPEGNAAAFdvNASCLSFLTAVDLAAGRIAVG 116
Cdd:PRK06816 66 MAAEAIRDLLDDAGFSLGDIELL--ACGTsqPDQLMPGHASMVHGELGAPPIEVVSS--AGVCAAGMMALKYAYLSVKAG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 117 QSRVALVFSAEIASRAL-------------PWKEQPDVA--ALF-------GDGAAAVVLTVAAERDS-TIRASVMRTYP 173
Cdd:PRK06816 142 ESRNAVATASELASRWFrasrfeaeeeklaELEENPEIAfeKDFlrwmlsdGAGAVLLENKPRPDGLSlRIDWIDLRSYA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 174 SAYEAC-----EIGAGGTRFDFQR-QPAEFAAHAVF--RMDGKELFRITRRHFPGFVDELLAAAGWSPADVDLVVPHQAS 245
Cdd:PRK06816 222 GELPVCmyagaEKNEDGSLKGWSDyPPEEAEAASALslKQDVRLLNENIVVYTIKPLLELVDKRNLDPDDIDYFLPHYSS 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2499854147 246 P---LALKHMIQQTGM--PGARVVNIAARFGNQIAASIPTALDIAWAEGRITKGMRLLL 299
Cdd:PRK06816 302 EyfrEKIVELLAKAGFmiPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
39-132 |
4.36e-04 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 41.13 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 39 LAVAAARLAMQKAAVGPGEIDLVIgaCGVPYQPLPTTAP--LVMHRLGIPEGnAAAFDVNASCLSFLTAVDLAAGRIAVG 116
Cdd:pfam00108 26 LGAEAIKAALERAGVDPEDVDEVI--VGNVLQAGEGQNParQAALKAGIPDS-APAVTINKVCGSGLKAVYLAAQSIASG 102
|
90
....*....|....*.
gi 2499854147 117 QSRVALVFSAEIASRA 132
Cdd:pfam00108 103 DADVVLAGGVESMSHA 118
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
35-127 |
6.98e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 37.82 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 35 DQITLAVAAARLAMQKAAVGPGEIDLVIGA----CGVP-YQPLPTTAplvmHRLGipEGNAAAFDVNASCLSFLTAVDLA 109
Cdd:PRK06059 22 DFVEYGVVAARAALADAGLDWRDVQLVVGAdtirNGYPgFVAGATFA----QALG--WNGAPVSSSYAACASGSQALQSA 95
|
90
....*....|....*...
gi 2499854147 110 AGRIAVGQSRVALVFSAE 127
Cdd:PRK06059 96 RAQILAGLCDVALVVGAD 113
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
50-130 |
7.03e-03 |
|
FAE1/Type III polyketide synthase-like protein; The members of this family are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region featured in this family contains the active site residues, as well as motifs involved in substrate binding.
Pssm-ID: 429970 Cd Length: 290 Bit Score: 37.61 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499854147 50 KAAVGPGEIDLVIGACGVpYQPLPTTAPLVMHRLGIPEgNAAAFDVNA-SCLSFLTAVDLAAGRIAVGQSRVALVFSAEI 128
Cdd:pfam08392 97 KTGVSPRDIDILVVNCSL-FNPTPSLSAMIVNRYKLRS-DIKSYNLSGmGCSAGLISIDLAKNLLQVHPNTYALVVSTEN 174
|
..
gi 2499854147 129 AS 130
Cdd:pfam08392 175 IT 176
|
|
| |
