|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-213 |
1.23e-122 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 377.68 E-value: 1.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDYQMKALSEVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSLV 80
Cdd:COG3321 100 WEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:COG3321 180 AVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRI 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTG 213
Cdd:COG3321 260 YAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTG 312
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1-216 |
2.38e-116 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 337.61 E-value: 2.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDYQMKALSEVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSLV 80
Cdd:cd00833 96 WEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:cd00833 176 ALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRI 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:cd00833 256 YAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPL 311
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
1-186 |
3.46e-89 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 264.19 E-value: 3.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDYQMkalsevskinaysvlgtahsaivgrlsyilglkgpnvAIDTACSSSLV 80
Cdd:smart00825 60 WEALEDAGIDPESLRGSRTGVFVGVSSSDYSV-------------------------------------TVDTACSSSLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:smart00825 103 ALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPI 182
|
170 180
....*....|....*....|....*.
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQ 186
Cdd:smart00825 183 LAVIRGSAVNQDGRSNGITAPSGPAQ 208
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1-153 |
9.34e-61 |
|
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: 190.54 E-value: 9.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDY-QMKALSE---VSKINAYSVlGTAHSAIVGRLSYILGLKGPNVAIDTACS 76
Cdd:pfam00109 96 WEALEDAGITPDSLDGSRTGVFIGSGIGDYaALLLLDEdggPRRGSPFAV-GTMPSVIAGRISYFLGLRGPSVTVDTACS 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194354520 77 SSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDA 153
Cdd:pfam00109 175 SSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
53-215 |
1.51e-27 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 108.18 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 53 AIVGRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCH 127
Cdd:PRK06501 153 SIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALStqndpPEKASK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 128 TFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYV 207
Cdd:PRK06501 233 PFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYI 312
|
....*...
gi 194354520 208 EAHGTGNP 215
Cdd:PRK06501 313 NAHGTSTP 320
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
45-213 |
2.07e-26 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 106.24 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 45 SVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTG 124
Cdd:TIGR02813 176 SFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 125 KCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASV 204
Cdd:TIGR02813 256 DIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTC 335
|
....*....
gi 194354520 205 DYVEAHGTG 213
Cdd:TIGR02813 336 GLIEAHGTG 344
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-213 |
1.23e-122 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 377.68 E-value: 1.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDYQMKALSEVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSLV 80
Cdd:COG3321 100 WEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:COG3321 180 AVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRI 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTG 213
Cdd:COG3321 260 YAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTG 312
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1-216 |
2.38e-116 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 337.61 E-value: 2.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDYQMKALSEVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSLV 80
Cdd:cd00833 96 WEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:cd00833 176 ALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRI 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:cd00833 256 YAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPL 311
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
1-186 |
3.46e-89 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 264.19 E-value: 3.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDYQMkalsevskinaysvlgtahsaivgrlsyilglkgpnvAIDTACSSSLV 80
Cdd:smart00825 60 WEALEDAGIDPESLRGSRTGVFVGVSSSDYSV-------------------------------------TVDTACSSSLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:smart00825 103 ALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPI 182
|
170 180
....*....|....*....|....*.
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQ 186
Cdd:smart00825 183 LAVIRGSAVNQDGRSNGITAPSGPAQ 208
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1-153 |
9.34e-61 |
|
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: 190.54 E-value: 9.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 1 WEALENAGQTQSSLQNSDTGVYVGICGNDY-QMKALSE---VSKINAYSVlGTAHSAIVGRLSYILGLKGPNVAIDTACS 76
Cdd:pfam00109 96 WEALEDAGITPDSLDGSRTGVFIGSGIGDYaALLLLDEdggPRRGSPFAV-GTMPSVIAGRISYFLGLRGPSVTVDTACS 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194354520 77 SSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDA 153
Cdd:pfam00109 175 SSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
2-216 |
1.08e-47 |
|
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: 159.34 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQSSLQNSDTGVYVGICGNDY--QMKALSEVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSL 79
Cdd:cd00825 21 RAIADAGLSREYQKNPIVGVVVGTGGGSPrfQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 80 VSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDH 159
Cdd:cd00825 101 HALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAH 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194354520 160 VLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:cd00825 181 IYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPI 237
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-216 |
4.26e-46 |
|
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: 157.18 E-value: 4.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQSSLQNSDTGVYVG--ICGNDY---QMKALSE--VSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTA 74
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGsgIGGLDTleeAYRALLEkgPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 75 CSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCHTFSSKADGFVRSEGCGMIVLKR 149
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194354520 150 LSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPL 307
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-216 |
9.96e-43 |
|
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: 148.07 E-value: 9.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQSSLQNSDTGVYVG-----ICGNDYQMKALSEV--SKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTA 74
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGsgiggLATIEEAYRALLEKgpRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 75 CSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCHTFSSKADGFVRSEGCGMIVLKR 149
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALStrnddPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194354520 150 LSDAQRDGDHVLGVIRGSAINQDGNSqgFTAP--BGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYH--ITAPdpDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPL 307
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
53-215 |
1.51e-27 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 108.18 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 53 AIVGRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCH 127
Cdd:PRK06501 153 SIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALStqndpPEKASK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 128 TFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYV 207
Cdd:PRK06501 233 PFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYI 312
|
....*...
gi 194354520 208 EAHGTGNP 215
Cdd:PRK06501 313 NAHGTSTP 320
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-215 |
2.44e-27 |
|
"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: 107.14 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQT-QSSLQNSDTGVYVG--ICGNDYQMKA-LSEVSKINAYSVLGTAHS-----AIVGrlSYILGLKGPNVAID 72
Cdd:cd00828 82 EALADAGITdPYEVHPSEVGVVVGsgMGGLRFLRRGgKLDARAVNPYVSPKWMLSpntvaGWVN--ILLLSSHGPIKTPV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 73 TACSSSLVSVHMAVQALRNNECSQAVAGGVNVvLSPEGSVYFSRLQAISPTGKCH-----TFSSKADGFVRSEGCGMIVL 147
Cdd:cd00828 160 GACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPeemsrPFDETRDGFVEAEGAGVLVL 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194354520 148 KRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPbGPSQQDVIRKALLQADMDPASVDYVEAHGTGNP 215
Cdd:cd00828 239 ERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTP 305
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
45-213 |
2.07e-26 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 106.24 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 45 SVLGTAHSAIVGRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTG 124
Cdd:TIGR02813 176 SFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 125 KCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASV 204
Cdd:TIGR02813 256 DIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTC 335
|
....*....
gi 194354520 205 DYVEAHGTG 213
Cdd:TIGR02813 336 GLIEAHGTG 344
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
2-216 |
6.67e-25 |
|
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: 97.90 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQSSLqnsdTGVYVGICGNDYQMkalsevskinaysvlgtahSAIVGRLSYILGLK-GPNVAIDTACSSSLV 80
Cdd:cd00327 17 QAIADAGLSKGPI----VGVIVGTTGGSGEF-------------------SGAAGQLAYHLGISgGPAYSVNQACATGLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 81 SVHMAVQALRNNECSQAVAGGVNVvlspegsvyfsrlqaisptgkchtfsskadgFVRSEGCGMIVLKRLSDAQRDGDHV 160
Cdd:cd00327 74 ALALAVQQVQNGKADIVLAGGSEE-------------------------------FVFGDGAAAAVVESEEHALRRGAHP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194354520 161 LGVIRGSAINQDGNSQGFtAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:cd00327 123 QAEIVSTAATFDGASMVP-AVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPI 177
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
56-216 |
3.20e-22 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 93.32 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 56 GRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS------PTGKCHTF 129
Cdd:PLN02836 165 GHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStkfnscPTEASRPF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 130 SSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEA 209
Cdd:PLN02836 245 DCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNA 324
|
....*..
gi 194354520 210 HGTGNPI 216
Cdd:PLN02836 325 HATSTPL 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
161-216 |
3.18e-21 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 84.54 E-value: 3.18e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 194354520 161 LGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNPI 216
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPL 56
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
2-216 |
4.50e-21 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 90.14 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAG-QTQSSLQNSDTGVYVGIcgndyQMKALSEV------------SKINAYSVLGTAHSAIVGRLSYILGLKGPN 68
Cdd:PTZ00050 87 EALADAKlDILSEKDQERIGVNIGS-----GIGSLADLtdemktlyekghSRVSPYFIPKILGNMAAGLVAIKHKLKGPS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 69 VAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS------PTGKCHTFSSKADGFVRSEGC 142
Cdd:PTZ00050 162 GSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRASRPFDKDRAGFVMGEGA 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194354520 143 GMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQ-ADMDPASVDYVEAHGTGNPI 216
Cdd:PTZ00050 242 GILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPI 316
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
56-216 |
3.03e-20 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 87.54 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 56 GRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCHTFS 130
Cdd:PRK07314 143 GHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStrnddPERASRPFD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 131 SKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAH 210
Cdd:PRK07314 223 KDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAH 302
|
....*.
gi 194354520 211 GTGNPI 216
Cdd:PRK07314 303 GTSTPA 308
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
56-216 |
7.45e-20 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 86.59 E-value: 7.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 56 GRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS------PTGKCHTF 129
Cdd:PRK06333 154 GHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALStrfndaPEQASRPF 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 130 SSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEA 209
Cdd:PRK06333 234 DRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNA 313
|
....*..
gi 194354520 210 HGTGNPI 216
Cdd:PRK06333 314 HATSTPV 320
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
52-216 |
1.14e-19 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 85.85 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 52 SAIVGRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-------PTG 124
Cdd:PRK07103 144 TDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGsdrfadePEA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 125 KCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQgfTAPBGPSQQDVIRKALLQADMDPASV 204
Cdd:PRK07103 224 ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRG--PDPSLEGEMRVIRAALRRAGLGPEDI 301
|
170
....*....|..
gi 194354520 205 DYVEAHGTGNPI 216
Cdd:PRK07103 302 DYVNPHGTGSPL 313
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-215 |
1.00e-18 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 83.51 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQSSLQNSDTGVYVG--ICGNDY---QMKALSEVS--KINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDTA 74
Cdd:PRK08722 84 QALDDSGLEVTEENAHRIGVAIGsgIGGLGLieaGHQALVEKGprKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 75 CSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCHTFSSKADGFVRSEGCGMIVLKR 149
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALStrndePQKASRPWDKDRDGFVLGDGAGMMVLEE 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194354520 150 LSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNP 215
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTP 309
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
61-213 |
4.92e-18 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 81.25 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 61 ILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAISPTGkCHTFSSKADGFVRSE 140
Cdd:PRK05952 132 QIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGE 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194354520 141 GCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTG 213
Cdd:PRK05952 211 GGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTA 283
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
56-216 |
1.68e-17 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 79.39 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 56 GRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS------PTGKCHTF 129
Cdd:PRK14691 72 GHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSthfnstPEKASRPF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 130 SSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEA 209
Cdd:PRK14691 152 DTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNA 231
|
....*..
gi 194354520 210 HGTGNPI 216
Cdd:PRK14691 232 HATSTPV 238
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
52-216 |
3.67e-15 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 73.23 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 52 SAIV----GRLSYILGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----P 122
Cdd:PRK08439 135 SALVnmlgGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALStrnddP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 123 TGKCHTFSSKADGFVRSEGCGMIVLKRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQqdVIRKALLQADMDPa 202
Cdd:PRK08439 215 KKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLR--AMKAALEMAGNPK- 291
|
170
....*....|....
gi 194354520 203 sVDYVEAHGTGNPI 216
Cdd:PRK08439 292 -IDYINAHGTSTPY 304
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-215 |
3.67e-14 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 70.39 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQ---SSLQNSDTGVYVGICGNDYQ-----MKALS-EVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAID 72
Cdd:PLN02787 209 KALADGGITEdvmKELDKTKCGVLIGSAMGGMKvfndaIEALRiSYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSIS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 73 TACSSSLVSVHMAVQALRNNECSQAVAGGVNVVLSPEGSVYFSRLQAIS-----PTGKCHTFSSKADGFVRSEGCGMIVL 147
Cdd:PLN02787 289 TACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSqrnddPTKASRPWDMNRDGFVMGEGAGVLLL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194354520 148 KRLSDAQRDGDHVLGVIRGSAINQDGNSQGFTAPBGPSQQDVIRKALLQADMDPASVDYVEAHGTGNP 215
Cdd:PLN02787 369 EELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTK 436
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
2-216 |
1.66e-13 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 68.54 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 2 EALENAGQTQSSLQNSDTGVYVGICGND--YQMKALS------EVSKINAYSVLGTAHSAIVGRLSYILGLKGPNVAIDT 73
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGStrNQVEAADamrgprGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 74 ACSSSLVSVHMAVQALRNNECSQAVAGGVNVvLSPEGSVYFSRLQAIS------PTGKCHTFSSKADGFVRSEGCGMIVL 147
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEE-LDWEMSCLFDAMGALStkyndtPEKASRAYDANRDGFVIAGGGGVVVV 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194354520 148 KRLSDAQRDGDHVLGVIRGSAINQDGNSqgFTAPBGPSQQDVIRKALlqADMDpASVDYVEAHGTGNPI 216
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYD--MVAPSGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPV 303
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
62-215 |
1.11e-10 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 60.24 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 62 LGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGVN-VVLSPegsVY-FSRLQAISPtGKCHTFSSKADGFVRS 139
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDsLCRLT---LNgFNSLESLSP-QPCRPFSANRDGINIG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 140 EGCGMIVLKRLSDAQ---------RDGDHVlgvirgSAinqdgnsqgfTAPBGPSQQDVIRKALLQADMDPASVDYVEAH 210
Cdd:PRK09185 223 EAAAFFLLEREDDAAvallgvgesSDAHHM------SA----------PHPEGLGAILAMQQALADAGLAPADIGYINLH 286
|
....*
gi 194354520 211 GTGNP 215
Cdd:PRK09185 287 GTATP 291
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
67-102 |
8.99e-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: 39.21 E-value: 8.99e-04
10 20 30
....*....|....*....|....*....|....*.
gi 194354520 67 PNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGV 102
Cdd:pfam00108 77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGV 112
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
46-102 |
1.30e-03 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 39.13 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 46 VLGTAHSAIVGRLSYI---LGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGV 102
Cdd:TIGR01930 51 VLQAGEQQNIARQAALlagLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGV 110
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| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
46-102 |
6.37e-03 |
|
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: 37.07 E-value: 6.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194354520 46 VLGTAHSAIVGRLSYI---LGLKGPNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGV 102
Cdd:cd00751 52 VLQAGEGQNPARQAALlagLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111
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| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
67-102 |
8.41e-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: 36.58 E-value: 8.41e-03
10 20 30
....*....|....*....|....*....|....*.
gi 194354520 67 PNVAIDTACSSSLVSVHMAVQALRNNECSQAVAGGV 102
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGV 115
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