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Conserved domains on  [gi|447009051|ref|WP_001086307|]
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MULTISPECIES: ketoacyl-ACP synthase III [Bacillus cereus group]

Protein Classification

ketoacyl-ACP synthase III( domain architecture ID 11486248)

beta-ketoacyl-[acyl-carrier-protein] synthase 3 initiates the elongation in type II fatty acid synthase by specifically using acetyl-CoA over acyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 1-325 0e+00

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


:

Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 555.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   1 MNSKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIV 80
Cdd:PRK12879   1 MMSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  81 ATTTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFG 160
Cdd:PRK12879  81 ATTTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 161 DGAGAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMNDTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANM 240
Cdd:PRK12879 161 DGAGAVVLEATENEPGFIDYVLGTDGDGGDILYRTGLGTTMDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 241 QIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDTLLLYGFGGGLTHLGL 320
Cdd:PRK12879 241 TKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAAL 320


                 ....*
gi 447009051 321 IVEWD 325
Cdd:PRK12879 321 LVKWG 325
 
Name Accession Description Interval E-value
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 1-325 0e+00

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 555.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   1 MNSKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIV 80
Cdd:PRK12879   1 MMSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  81 ATTTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFG 160
Cdd:PRK12879  81 ATTTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 161 DGAGAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMNDTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANM 240
Cdd:PRK12879 161 DGAGAVVLEATENEPGFIDYVLGTDGDGGDILYRTGLGTTMDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 241 QIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDTLLLYGFGGGLTHLGL 320
Cdd:PRK12879 241 TKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAAL 320


                 ....*
gi 447009051 321 IVEWD 325
Cdd:PRK12879 321 LVKWG 325
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 4-305 1.32e-143

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: 408.08  E-value: 1.32e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   4 KSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATT 83
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  84 TADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGA 163
Cdd:cd00830   81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 164 GAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMN-DTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANMQI 242
Cdd:cd00830  161 GAVVLEATEEDPGILDSVLGSDGSGADLLTIPAGGSRSPfEDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447009051 243 DDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:cd00830  241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDL 303
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 3-305 1.28e-142

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: 405.65  E-value: 1.28e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   3 SKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVAT 82
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  83 TTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDG 162
Cdd:COG0332   81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 163 AGAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMNDTPLQTNE-KIVQNGREVYKWATRTVPAGIKELLHTANMQ 241
Cdd:COG0332  161 AGAVVLEASEEGPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDhYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447009051 242 IDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:COG0332  241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDL 304
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
 4-304 7.06e-116

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: 337.43  E-value: 7.06e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051    4 KSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATT 83
Cdd:TIGR00747   2 YAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVATT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   84 TADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGA 163
Cdd:TIGR00747  82 TPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  164 GAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTtmndTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANMQID 243
Cdd:TIGR00747 162 GAVVLGESEDPGGIISTHLGADGTQGEALYLPAGGR----PTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPE 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447009051  244 DIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGD 304
Cdd:TIGR00747 238 DIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGD 298
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
 108-186 7.03e-38

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: 129.56  E-value: 7.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  108 FDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGAGAILLERDENK-PSFIAYHMGTNG 186
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPgARILDSVLGSDG 80
 
Name Accession Description Interval E-value
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 1-325 0e+00

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 555.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   1 MNSKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIV 80
Cdd:PRK12879   1 MMSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  81 ATTTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFG 160
Cdd:PRK12879  81 ATTTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 161 DGAGAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMNDTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANM 240
Cdd:PRK12879 161 DGAGAVVLEATENEPGFIDYVLGTDGDGGDILYRTGLGTTMDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 241 QIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDTLLLYGFGGGLTHLGL 320
Cdd:PRK12879 241 TKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAAL 320


                 ....*
gi 447009051 321 IVEWD 325
Cdd:PRK12879 321 LVKWG 325
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
4-305 2.13e-144

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 409.85  E-value: 2.13e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   4 KSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATT 83
Cdd:PRK09352   3 YAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVATT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  84 TADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGA 163
Cdd:PRK09352  83 TPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 164 GAILLERDENkPSFIAYHMGTNGHGDIHLYRTNLSTTMNDTPlqtnEKIVQNGREVYKWATRTVPAGIKELLHTANMQID 243
Cdd:PRK09352 163 GAVVLGASEE-PGILSTHLGSDGSYGDLLYLPGGGSRGPASP----GYLRMEGREVFKFAVRELAKVAREALEAAGLTPE 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447009051 244 DIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:PRK09352 238 DIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDL 299
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 4-305 1.32e-143

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: 408.08  E-value: 1.32e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   4 KSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATT 83
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  84 TADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGA 163
Cdd:cd00830   81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 164 GAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMN-DTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANMQI 242
Cdd:cd00830  161 GAVVLEATEEDPGILDSVLGSDGSGADLLTIPAGGSRSPfEDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447009051 243 DDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:cd00830  241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDL 303
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 3-305 1.28e-142

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: 405.65  E-value: 1.28e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   3 SKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVAT 82
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  83 TTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDG 162
Cdd:COG0332   81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 163 AGAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTTMNDTPLQTNE-KIVQNGREVYKWATRTVPAGIKELLHTANMQ 241
Cdd:COG0332  161 AGAVVLEASEEGPGILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDhYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447009051 242 IDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:COG0332  241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDL 304
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
 4-304 7.06e-116

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: 337.43  E-value: 7.06e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051    4 KSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATT 83
Cdd:TIGR00747   2 YAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVATT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   84 TADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGA 163
Cdd:TIGR00747  82 TPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  164 GAILLERDENKPSFIAYHMGTNGHGDIHLYRTNLSTtmndTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANMQID 243
Cdd:TIGR00747 162 GAVVLGESEDPGGIISTHLGADGTQGEALYLPAGGR----PTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPE 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447009051  244 DIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGD 304
Cdd:TIGR00747 238 DIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGD 298
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
 3-324 2.10e-92

3-oxoacyl-[acyl-carrier-protein] synthase III


Pssm-ID: 215185  Cd Length: 379  Bit Score: 280.08  E-value: 2.10e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   3 SKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVAT 82
Cdd:PLN02326  46 SGSKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  83 TTADYVFPSvACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDG 162
Cdd:PLN02326 126 SSPDDLFGS-APQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDG 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 163 AGAILLER-DENKPSFIAYHMGTNGHGDIHLYRT-----NLSTTMNDTPLQ-------TNEKIVQNGREVYKWATRTVPA 229
Cdd:PLN02326 205 AGAVVLQAcDDDEDGLLGFDMHSDGNGHKHLHATfkgedDDSSGGNTNGVGdfppkkaSYSCIQMNGKEVFKFAVRCVPQ 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 230 GIKELLHTANMQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDTLLLY 309
Cdd:PLN02326 285 VIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATA 364

                        330
                 ....*....|....*
gi 447009051 310 GFGGGLTHLGLIVEW 324
Cdd:PLN02326 365 GFGAGLTWGSAIVRW 379
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
 7-304 7.16e-74

3-oxoacyl-acyl-carrier-protein synthase 3; Provisional


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 230.60  E-value: 7.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   7 ITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATTTAD 86
Cdd:CHL00203   5 ILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  87 YVFPSvACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGAGAI 166
Cdd:CHL00203  85 DLFGS-ASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDGAGAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 167 LLErDENKPSFIAYHMGTNGHGDIHLYRTNlsTTMNDTPLQTNE-------KIVQNGREVYKWATRTVPAGIKELLHTAN 239
Cdd:CHL00203 164 IIG-ASYENSILGFKLCTDGKLNSHLQLMN--KPVNNQSFGTTKlpqgqyqSISMNGKEVYKFAVFQVPAVIIKCLNALN 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447009051 240 MQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGD 304
Cdd:CHL00203 241 ISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQ 305
PRK05963 PRK05963
beta-ketoacyl-ACP synthase III;
3-305 1.88e-59

beta-ketoacyl-ACP synthase III;


Pssm-ID: 180328 [Multi-domain]  Cd Length: 326  Bit Score: 193.78  E-value: 1.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   3 SKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVAT 82
Cdd:PRK05963   2 CSSRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  83 TTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSgSHKKVLVVATETLSKVTDYTDRTTCILFGDG 162
Cdd:PRK05963  82 STPDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRA-QGKPVLVVAANILSRRINMAERASAVLFADA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 163 AGAILL---ERDenKPSFIAYHMGTNGHG-DIHLYRTNLSTTMNDTPLQTNEK--IVQNGREVYKWATRTVPAGIKELLH 236
Cdd:PRK05963 161 AGAVVLapsAKA--NSGVLGSQLISDGSHyDLIKIPAGGSARPFAPERDASEFlmTMQDGRAVFTEAVRMMSGASQNVLA 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447009051 237 TANMQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:PRK05963 239 SAAMTPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGER 307
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
1-304 1.06e-52

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 176.18  E-value: 1.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   1 MNSKSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASeDEYASNLAIKAVENLCTTYKKNLEDVDCIIV 80
Cdd:PRK07204   1 MKRYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVD-GETSSYMGAEAAKKAVEDAKLTLDDIDCIIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  81 ATTTADYVFPSVACQIQQYLNIPHT--MAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCIL 158
Cdd:PRK07204  80 ASGTIQQAIPCTASLIQEQLGLQHSgiPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCIL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 159 FGDGAGAILLERDENKPSFIAYHMGTNGHGDiHLYRTNLSTTM--NDTPLQTNEKIV---QNGREVYKWATRTVPAGIKE 233
Cdd:PRK07204 160 FGDGAAAVVITKGDHSSRILASHMETYSSGA-HLSEIRGGGTMihPREYSEERKEDFlfdMNGRAIFKLSSKYLMKFIDK 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447009051 234 LLHTANMQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGD 304
Cdd:PRK07204 239 LLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGN 309
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 6-305 3.55e-48

"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: 164.14  E-value: 3.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   6 RITAIGTHVPEQILSNHDLEKMIdtNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCIIVATTTA 85
Cdd:cd00827    3 GIEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  86 DYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCIlFGDGAGA 165
Cdd:cd00827   81 IDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALEPT-LGDGAAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 166 ILLERDENKPS--FIAYHMGTNGH------GDIHLYRTNLSTTMNDTPLQTNekivQNGREVYKWATRTVPAGIKELLHT 237
Cdd:cd00827  160 MLVSRNPGILAagIVSTHSTSDPGydfspyPVMDGGYPKPCKLAYAIRLTAE----PAGRAVFEAAHKLIAKVVRKALDR 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447009051 238 ANMQiDDIDWLIPHSANLRMIES----ICEKSQIPIQKTLTSV-EYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:cd00827  236 AGLS-EDIDYFVPHQPNGKKILEavakKLGGPPEKASQTRWILlRRVGNMYAASILLGLASLLESGKLKAGDR 307
PRK12880 PRK12880
beta-ketoacyl-ACP synthase III;
4-291 2.77e-42

beta-ketoacyl-ACP synthase III;


Pssm-ID: 171793  Cd Length: 353  Bit Score: 149.73  E-value: 2.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   4 KSRITAIGTHVPEQILSNHDLEKMIDTNDEWIVQR----TGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCII 79
Cdd:PRK12880   7 KAKISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  80 VATTTADYVFPSVACQIQQYLNI-PHTMAFDLNATCAGFTYGLHVGNSLITSGShKKVLVVATETLSKVTDYTDRTTCIL 158
Cdd:PRK12880  87 VVTQSPDFFMPSTACYLHQLLNLsSKTIAFDLGQACAGYLYGLFVAHSLIQSGL-GKILLICGDTLSKFIHPKNMNLAPI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 159 FGDGAGAILLERDENKPSFiaYHMGTNGHGDIHLYRTNLSTTMNDTPLQTNEKIVQ------------NGREVYKWATRT 226
Cdd:PRK12880 166 FGDGVSATLIEKTDFNEAF--FELGSDGKYFDKLIIPKGAMRIPKADIFNDDSLMQteefrqlenlymDGANIFNMALEC 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447009051 227 VPAGIKELLHTANMQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSV-EYMGNTSSVSIPLAL 291
Cdd:PRK12880 244 EPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPNFImEKYANLSACSLPALL 309
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
 108-186 7.03e-38

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: 129.56  E-value: 7.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  108 FDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGAGAILLERDENK-PSFIAYHMGTNG 186
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPgARILDSVLGSDG 80
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 4-305 9.24e-31

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 236037  Cd Length: 372  Bit Score: 119.21  E-value: 9.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   4 KSRITAIGTHVPEQILSNHDL------------------------EKMIDTNDEWIVQRTGMKER--------------- 44
Cdd:PRK07515   2 NVVISGTGLYTPPESISNEELvasfnayverfnaenaaaiaagevEALQPSSSEFIEKASGIKSRyvmdkegildpdrmr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  45 -RIA--SEDEYA--SNLAIKAVENLCTTYKKNLEDVDCIIVATTTADYVFPSVACQIQQYLNIpHTMAFDLNATCAGFTY 119
Cdd:PRK07515  82 pRIPerSNDELSiqAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGI-EGFAFDMNVACSSATF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 120 GLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGAGAILLERDENKPSfiayhmgtNGHGDI---HLY--- 193
Cdd:PRK07515 161 GIQTAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATS--------AGGFEIlgtRLFtqf 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 194 ----RTN---LSTTMNDTPLQTNEKIVQNGREVYKWATRTVPAGIKELLHTANMQIDDID--WLipHSANLRMIESICEK 264
Cdd:PRK07515 233 snniRNNfgfLNRADPEGIGARDKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKK 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447009051 265 --------SQIPIqktltsV--EYmGNTSSVSIPLALDLARKEgkLNNGDT 305
Cdd:PRK07515 311 vlgrdatpEEAPV------IldEY-ANTSSAGSIIAFHKHSDD--LAAGDL 352
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
 235-305 1.86e-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: 102.96  E-value: 1.86e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447009051  235 LHTANMQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDL 71
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 89-299 9.21e-23

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: 96.55  E-value: 9.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  89 FPSVACQIQQYLNIpHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTD------------------Y 150
Cdd:cd00825   72 FPGASGQIATPLGI-HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDcefdamgalstpekasrtF 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 151 TDRTTCILFGDGAGAILLERDEnkpsfiayHMGTNGHgdiHLYRTNLSTTMNDTPlqtnekivqNGREVYKWATRTVPAG 230
Cdd:cd00825  151 DAAADGFVFGDGAGALVVEELE--------HALARGA---HIYAEIVGTAATIDG---------AGMGAFAPSAEGLARA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447009051 231 IKELLHTANMQIDDIDWLIPHSANLRMIESICEKS--------QIPIQKTLTSveyMGNTSSVSIPLALDLARKEGK 299
Cdd:cd00825  211 AKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLlrsefgdkSPAVSATKAM---TGNLSSAAVVLAVDEAVLMLE 284
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 78-299 8.72e-21

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: 89.81  E-value: 8.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  78 IIVATTTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETlskvtdytdrttcI 157
Cdd:cd00327   32 VIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE-------------F 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 158 LFGDGAGAILLERDEnkpsfiayHMGTNGhgdIHLYRTNLSTTMNDTPLQTNEKIVQNGREvykwatrtvpAGIKELLHT 237
Cdd:cd00327   99 VFGDGAAAAVVESEE--------HALRRG---AHPQAEIVSTAATFDGASMVPAVSGEGLA----------RAARKALEG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 238 ANMQIDDIDWLIPHSANLRMIESICEKS--------QIPIQKTLTSveyMGNTSSVSIPLALDLARKEGK 299
Cdd:cd00327  158 AGLTPSDIDYVEAHGTGTPIGDAVELALgldpdgvrSPAVSATLIM---TGHPLGAAGLAILDELLLMLE 224
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
7-304 1.58e-20

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 90.45  E-value: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   7 ITAIGTHVPEQILSNHDLEKMIDTNDEWIVQRTGMKERRIASEDEYASNLAIKAVENLCTTYKKNLEDVDCII-VATTTA 85
Cdd:PRK06840   7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVIyIGSEHK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  86 DYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITS-GSHKKVLVVATETLSKVTDYTDRTTCILF--GDG 162
Cdd:PRK06840  87 DYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLYSdPSIENVLLVGGYRNSDLVDYDNPRTRFMFnfAAG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 163 AGAILLERDENKPSFIAYHMGTNGH----------GDIH-LYRTNLSTTMN--------DTPLQTNEKIVQNGREVykwa 223
Cdd:PRK06840 167 GSAALLKKDAGKNRILGSAIITDGSfsedvrvpagGTKQpASPETVENRQHyldvidpeSMKERLDEVSIPNFLKV---- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 224 trtvpagIKELLHTANMQIDDIDWLIPHSANLRMIESICEKSQIPIQKTLTSVEYmGNTSSVSIPLALDLARKEGKLNNG 303
Cdd:PRK06840 243 -------IREALRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLTEEQAIYLDEY-GHLGQLDQILSLHLALEQGKLKDG 314


                 .
gi 447009051 304 D 304
Cdd:PRK06840 315 D 315
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 3-304 1.89e-18

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 181732  Cd Length: 338  Bit Score: 84.55  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   3 SKSRITAIGTHVPEQILSNHDLEKMI-DTND-----EWIVQR-TGMKERRIASEDEYASNLAIKAVEnlcttykKNLE-- 73
Cdd:PRK09258   4 SNVAILSLAYELAPVVVTSSEIEERLaPLYErlrlpPGQLEAlTGIRERRWWPEGTQLSDGAIAAGR-------KALAea 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  74 -----DVDCIIVATTTADYVFPSVACQIQQYLNIP-HTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKV 147
Cdd:PRK09258  77 gidpsDIGLLINTSVCRDYLEPATACRVHHNLGLPkSCANFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGESAREI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 148 TDYT------DRTTCILF---------GDGAGAILLERDENKPSfiaYHM--------GTNGH----GDIHLYRTNLSTT 200
Cdd:PRK09258 157 VEATidrllaPETTREDFaqsfatltlGSGAAAAVLTRGSLHPR---GHRllggvtraATEHHelcqGGRDGMRTDAVGL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 201 MNdtplqtnekivqNGREVykwATRTvpagIKELLHTANMQIDDIDWLIPH---SANLRMiesICEKSQIPIQKTLTSVE 277
Cdd:PRK09258 234 LK------------EGVEL---AVDT----WEAFLAQLGWAVEQVDRVICHqvgAAHTRA---ILKALGIDPEKVFTTFP 291

                        330       340
                 ....*....|....*....|....*..
gi 447009051 278 YMGNTSSVSIPLALDLARKEGKLNNGD 304
Cdd:PRK09258 292 TLGNMGPASLPITLAMAAEEGFLKPGD 318
BH0617 COG3424
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ...
 5-305 3.72e-14

Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442650 [Multi-domain]  Cd Length: 351  Bit Score: 72.10  E-value: 3.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   5 SRITAIGTHVPEQILSNHD------------------LEKM-----IDT-----NDEWIVQRTGMKERRIASEDEyASNL 56
Cdd:COG3424    2 ARILSIATAVPPHRYTQEEiaefaaelfglderdrrrLRRLfensgIETrhsvlPLEWYLEPPSFGERNALYIEE-ALEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  57 AIKAVENLCTTYKKNLEDVDCIIVATTTAdYVFPSVACQIQQYLNI-PHTMAFDLNAT-CAGFTYGLHVGNSLITSGSHK 134
Cdd:COG3424   81 AEEAARRALDKAGLDPEDIDHLVTVSCTG-FAAPGLDARLINRLGLrPDVRRLPVGGMgCAAGAAGLRRAADFLRADPDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 135 KVLVVATE--TLSKVTDYTDRTTCI---LFGDGAGAILL---ERDENKPSFIAYHMGT--NGHGDIHLyrtnlstTMNDT 204
Cdd:COG3424  160 VVLVVCVElcSLTFQRDDDSKDNLVanaLFGDGAAAVVVsgdPRPGPGPRILAFRSYLipDTEDVMGW-------DVGDT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 205 PLQtnekiVQNGREVYKWATRTVPAGIKELLHTANMQIDDIDWLIPHSANLRMIESICEKSQIPIQK------TLTsvEY 278
Cdd:COG3424  233 GFR-----MVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEAlahsreVLR--EY 305

                        330       340
                 ....*....|....*....|....*..
gi 447009051 279 mGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:COG3424  306 -GNMSSATVLFVLERLLEEGAPAPGER 331
PRK06816 PRK06816
StlD/DarB family beta-ketosynthase;
7-305 8.23e-14

StlD/DarB family beta-ketosynthase;


Pssm-ID: 235866  Cd Length: 378  Bit Score: 71.48  E-value: 8.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   7 ITAIGTHVPEQILSNHDLEK---MIDTNDE----WIVQRTGMKERRIASEDEYA---SN--LAIKAVENLCTTYKKNLED 74
Cdd:PRK06816   5 ITSTGAFLPGEPVSNDEMEAylgLINGKPSrarrIILRNNGIKTRHYALDPEGRpthSNaqMAAEAIRDLLDDAGFSLGD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  75 VDCIIVATTTADYVFPSVACQIQQYLNIPhtmAFDLNAT----CAGFTYGLHVGNSlITSGSHKKVLVVATETLSKV--- 147
Cdd:PRK06816  85 IELLACGTSQPDQLMPGHASMVHGELGAP---PIEVVSSagvcAAGMMALKYAYLS-VKAGESRNAVATASELASRWfra 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 148 ---------TDYTDRTTCILF---------GDGAGAILLErdeNKP---------------SFiAYHMGT--------NG 186
Cdd:PRK06816 161 srfeaeeekLAELEENPEIAFekdflrwmlSDGAGAVLLE---NKPrpdglslridwidlrSY-AGELPVcmyagaekNE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 187 HGDIHLYRtnlsttmnDTPLQT----------------NEKIVQNGREVYKwatrtvpagikELLHTANMQIDDIDWLIP 250
Cdd:PRK06816 237 DGSLKGWS--------DYPPEEaeaasalslkqdvrllNENIVVYTIKPLL-----------ELVDKRNLDPDDIDYFLP 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 251 H--SANLRM-IESICEKSQ--IPIQKTLTSVEYMGNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:PRK06816 298 HysSEYFREkIVELLAKAGfmIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQK 357
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 5-305 9.39e-09

Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.


Pssm-ID: 238427 [Multi-domain]  Cd Length: 361  Bit Score: 56.08  E-value: 9.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051   5 SRITAIGTHVPEQILS----------NHDLEKMIDTND--EWIVQRTGMKERRIA---SEDEYASN------------LA 57
Cdd:cd00831    2 ATILAIGTAVPPHRVPqselvdfyrrLFSSDHLPELKEklKRLCAKTGIETRYLVlpgGEETYAPRpemspslderndIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  58 IKAVENLCTTYKKNL--------EDVDCIIVATTTaDYVFPSVACQIQQYLNI-PHTMAFDLNAT-CAGFTYGLHVGNSL 127
Cdd:cd00831   82 LEEARELAEEAARGAldeaglrpSDIDHLVVNTST-GNPTPSLDAMLINRLGLrPDVKRYNLGGMgCSAGAIALDLAKDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 128 ITSGSHKKVLVVATETLSKVTDYTDR-----TTCiLFGDGAGAILL-----ERDENKPSF----IAYHMGTNGHGDIHLY 193
Cdd:cd00831  161 LEANPGARVLVVSTELCSLWYRGPDHrsmlvGNA-LFGDGAAAVLLsndprDRRRERPLFelvrAASTLLPDSEDAMGWH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 194 RTNLSTTMNDTPLQTnEKIVQNGREVYKWATRTVPAGIKELlhtanmqiDDIDWLIpHSANLRMIESICEKsqIPIQKTL 273
Cdd:cd00831  240 LGEEGLTFVLSRDVP-RLVEKNLERVLRKLLARLGIGLFKL--------AFDHWCV-HPGGRAVLDAVEKA--LGLSPED 307

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 447009051 274 TSVEYM-----GNTSSVSIPLALDLARKEGKLNNGDT 305
Cdd:cd00831  308 LEASRMvlrryGNMSSSSVLYVLAYMEAKGRVKRGDR 344
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 56-186 4.30e-04

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: 41.48  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051  56 LAIKAVENLCTTYKKNLEDVDCIIVATTTADYVFPSVACQIQQYLNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKK 135
Cdd:cd00829   19 LAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAIASGLADV 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 447009051 136 VLVVATETLSKVTDYTDrttcilFGDGAGAILLERDE--NKPSFIAY-------HMGTNG 186
Cdd:cd00829   99 VLVVGAEKMSDVPTGDE------AGGRASDLEWEGPEppGGLTPPALyalaarrYMHRYG 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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