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Conserved domains on  [gi|1370990834|emb|SPJ08356|]
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oxoacyl-ACP synthase [Plasmodium sp. DRC-Itaito]

Protein Classification

ketoacyl-ACP synthase III( domain architecture ID 10093604)

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
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 52-369 9.09e-146

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: 415.02  E-value: 9.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:cd00830     3 RILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:cd00830    83 DYLFpATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIrsGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGAGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNvNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:cd00830   163 VVLEATE--EDPGILDSVLGSDGSGADLLTIPAGGSRSPFEDAE-GGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:cd00830   240 PDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAAL 319


                  .
gi 1370990834 369 L 369
Cdd:cd00830   320 L 320
 
Name Accession Description Interval E-value
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 52-369 9.09e-146

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: 415.02  E-value: 9.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:cd00830     3 RILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:cd00830    83 DYLFpATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIrsGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGAGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNvNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:cd00830   163 VVLEATE--EDPGILDSVLGSDGSGADLLTIPAGGSRSPFEDAE-GGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:cd00830   240 PDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAAL 319


                  .
gi 1370990834 369 L 369
Cdd:cd00830   320 L 320
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
48-371 3.97e-136

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 390.59  E-value: 3.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  48 KIGGKIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINA 127
Cdd:PRK09352    1 MMYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 128 SSTPQNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGD 204
Cdd:PRK09352   81 TTTPDYAFpSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIrsGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 205 AAGAVVLQRTEGKEenkIFNYYLGSDSELNDLLTINFDhdkynlDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQN 284
Cdd:PRK09352  161 GAGAVVLGASEEPG---ILSTHLGSDGSYGDLLYLPGG------GSRGPASPGYLRMEGREVFKFAVRELAKVAREALEA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 285 SNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSY 364
Cdd:PRK09352  232 AGLTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTW 311


                  ....*..
gi 1370990834 365 GCVILKY 371
Cdd:PRK09352  312 GAALVRW 318
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 52-371 3.99e-136

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: 391.01  E-value: 3.99e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:COG0332     4 RILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFLN--RYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:COG0332    84 DYLFpSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRsgQAKNVLVVGAETLSRIVDWTDRSTCVLFGDGAGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDHDKYNLDnPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:COG0332   164 VVLEASE--EGPGILGSVLGSDGSGADLLVVPAGGSRNPPS-PVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:COG0332   241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320


                  ...
gi 1370990834 369 LKY 371
Cdd:COG0332   321 LRW 323
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
 52-371 4.92e-109

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: 322.03  E-value: 4.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:TIGR00747   4 GILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVATTTP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:TIGR00747  84 DHAFpSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIesGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDGAGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDhdkynlDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:TIGR00747 164 VVLGESE--DPGGIISTHLGADGTQGEALYLPAG------GRPTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:TIGR00747 236 PEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAAL 315


                  ...
gi 1370990834 369 LKY 371
Cdd:TIGR00747 316 VRF 318
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
 282-371 5.47e-41

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430060  Cd Length: 90  Bit Score: 139.17  E-value: 5.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 282 IQNSNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAG 361
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80

                          90
                  ....*....|
gi 1370990834 362 MSYGCVILKY 371
Cdd:pfam08541  81 LTWGAALLRW 90
 
Name Accession Description Interval E-value
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 52-369 9.09e-146

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: 415.02  E-value: 9.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:cd00830     3 RILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:cd00830    83 DYLFpATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIrsGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGAGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNvNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:cd00830   163 VVLEATE--EDPGILDSVLGSDGSGADLLTIPAGGSRSPFEDAE-GGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:cd00830   240 PDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAAL 319


                  .
gi 1370990834 369 L 369
Cdd:cd00830   320 L 320
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
48-371 3.97e-136

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 390.59  E-value: 3.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  48 KIGGKIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINA 127
Cdd:PRK09352    1 MMYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 128 SSTPQNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGD 204
Cdd:PRK09352   81 TTTPDYAFpSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIrsGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 205 AAGAVVLQRTEGKEenkIFNYYLGSDSELNDLLTINFDhdkynlDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQN 284
Cdd:PRK09352  161 GAGAVVLGASEEPG---ILSTHLGSDGSYGDLLYLPGG------GSRGPASPGYLRMEGREVFKFAVRELAKVAREALEA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 285 SNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSY 364
Cdd:PRK09352  232 AGLTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTW 311


                  ....*..
gi 1370990834 365 GCVILKY 371
Cdd:PRK09352  312 GAALVRW 318
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 52-371 3.99e-136

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: 391.01  E-value: 3.99e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:COG0332     4 RILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFLN--RYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:COG0332    84 DYLFpSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRsgQAKNVLVVGAETLSRIVDWTDRSTCVLFGDGAGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDHDKYNLDnPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:COG0332   164 VVLEASE--EGPGILGSVLGSDGSGADLLVVPAGGSRNPPS-PVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:COG0332   241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320


                  ...
gi 1370990834 369 LKY 371
Cdd:COG0332   321 LRW 323
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
 50-371 8.68e-127

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


Pssm-ID: 215185  Cd Length: 379  Bit Score: 369.45  E-value: 8.68e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  50 GGKIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASS 129
Cdd:PLN02326   47 GSKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 130 TPQNLFGDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFLN--RYKNILIVGSDALSNFVDWRDRNTCVLFGDAAG 207
Cdd:PLN02326  127 SPDDLFGSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRggGYKNVLVIGADALSRYVDWTDRGTCILFGDGAG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 208 AVVLQRTeGKEENKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNVN----------KYGKLHMNGKEVFKYTISNIPKI 277
Cdd:PLN02326  207 AVVLQAC-DDDEDGLLGFDMHSDGNGHKHLHATFKGEDDDSSGGNTNgvgdfppkkaSYSCIQMNGKEVFKFAVRCVPQV 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 278 LKKAIQNSNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCG 357
Cdd:PLN02326  286 IESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAG 365

                         330
                  ....*....|....
gi 1370990834 358 FGAGMSYGCVILKY 371
Cdd:PLN02326  366 FGAGLTWGSAIVRW 379
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 52-370 2.22e-116

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 340.69  E-value: 2.22e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:PRK12879    6 RITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVATTTP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:PRK12879   86 DYLFpSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLItsGLYKKVLVIGAERLSKVTDYTDRTTCILFGDGAGA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTI-NFDHDkynLDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNI 287
Cdd:PRK12879  166 VVLEATE--NEPGFIDYVLGTDGDGGDILYRtGLGTT---MDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 288 NIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCV 367
Cdd:PRK12879  241 TKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAAL 320


                  ...
gi 1370990834 368 ILK 370
Cdd:PRK12879  321 LVK 323
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
 52-371 4.92e-109

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: 322.03  E-value: 4.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTP 131
Cdd:TIGR00747   4 GILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVATTTP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGA 208
Cdd:TIGR00747  84 DHAFpSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIesGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDGAGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 209 VVLQRTEgkEENKIFNYYLGSDSELNDLLTINFDhdkynlDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNIN 288
Cdd:TIGR00747 164 VVLGESE--DPGGIISTHLGADGTQGEALYLPAG------GRPTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 289 IEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSYGCVI 368
Cdd:TIGR00747 236 PEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAAL 315


                  ...
gi 1370990834 369 LKY 371
Cdd:TIGR00747 316 VRF 318
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
 50-371 7.16e-106

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


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 314.19  E-value: 7.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  50 GGKIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASS 129
Cdd:CHL00203    2 GVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 130 TPQNLFGDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNF--LNRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAG 207
Cdd:CHL00203   82 TPDDLFGSASQLQAEIGATRAVAFDITAACSGFILALVTATQFiqNGSYKNILVVGADTLSKWIDWSDRKTCILFGDGAG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 208 AVVLQRTEgkeENKIFNYYLGSDSELNDLLTINF---DHDKYNLDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQN 284
Cdd:CHL00203  162 AAIIGASY---ENSILGFKLCTDGKLNSHLQLMNkpvNNQSFGTTKLPQGQYQSISMNGKEVYKFAVFQVPAVIIKCLNA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 285 SNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSY 364
Cdd:CHL00203  239 LNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTW 318


                  ....*..
gi 1370990834 365 GCVILKY 371
Cdd:CHL00203  319 GAIVLKW 325
PRK05963 PRK05963
beta-ketoacyl-ACP synthase III;
48-370 1.74e-57

beta-ketoacyl-ACP synthase III;


Pssm-ID: 180328 [Multi-domain]  Cd Length: 326  Bit Score: 189.93  E-value: 1.74e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  48 KIGGKIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINA 127
Cdd:PRK05963    1 VCSSRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 128 SSTPQNLF-GDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFLNRY-KNILIVGSDALSNFVDWRDRNTCVLFGDA 205
Cdd:PRK05963   81 TSTPDHLLpPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQgKPVLVVAANILSRRINMAERASAVLFADA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 206 AGAVVLQRTEgKEENKIFNYYLGSDSELNDLLTINfDHDKYNLDNPNVNKyGKLHM---NGKEVFKYTISNIPKILKKAI 282
Cdd:PRK05963  161 AGAVVLAPSA-KANSGVLGSQLISDGSHYDLIKIP-AGGSARPFAPERDA-SEFLMtmqDGRAVFTEAVRMMSGASQNVL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 283 QNSNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGM 362
Cdd:PRK05963  238 ASAAMTPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGM 317


                  ....*...
gi 1370990834 363 SYGCVILK 370
Cdd:PRK05963  318 TGGAVVMR 325
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
52-371 4.31e-48

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 165.78  E-value: 4.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILkRDENISMLQIDSATQALKTSSLKPSDIDMVINASST- 130
Cdd:PRK07204    6 SIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFV-DGETSSYMGAEAAKKAVEDAKLTLDDIDCIICASGTi 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 131 PQNLFGDANNISNKIGCKNS--VNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAA 206
Cdd:PRK07204   85 QQAIPCTASLIQEQLGLQHSgiPCFDINSTCLSFITALDTISYAIecGRYKRVLIISSEISSVGLNWGQNESCILFGDGA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 207 GAVVLQRteGKEENKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNVNKYGKL--HMNGKEVFKYTISNIPKILKKAIQN 284
Cdd:PRK07204  165 AAVVITK--GDHSSRILASHMETYSSGAHLSEIRGGGTMIHPREYSEERKEDFlfDMNGRAIFKLSSKYLMKFIDKLLMD 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 285 SNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSY 364
Cdd:PRK07204  243 AGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSI 322


                  ....*..
gi 1370990834 365 GCVILKY 371
Cdd:PRK07204  323 GGILLEY 329
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 53-369 1.61e-47

"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: 163.76  E-value: 1.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  53 IIGHGHSYPSTEIYNDELKKYVdtNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTPQ 132
Cdd:cd00827     4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 133 NLFGD-ANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVlFGDAAGAV 209
Cdd:cd00827    82 DKGKSaATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVesGPWRYALVVASDIASYLLDEGSALEPT-LGDGAAAM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 210 VLQRTEGKEENKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNVNKYGKLHMNGKEVFKYTISNIPKILKKAIQNSNINi 289
Cdd:cd00827   161 LVSRNPGILAAGIVSTHSTSDPGYDFSPYPVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALDRAGLS- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 290 EDINYFIFHQANI-RIIETIAKNLNIPMSKV----LVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMSY 364
Cdd:cd00827   240 EDIDYFVPHQPNGkKILEAVAKKLGGPPEKAsqtrWILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTA 319


                  ....*
gi 1370990834 365 GCVIL 369
Cdd:cd00827   320 EAFVL 324
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
 282-371 5.47e-41

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430060  Cd Length: 90  Bit Score: 139.17  E-value: 5.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 282 IQNSNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAG 361
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80

                          90
                  ....*....|
gi 1370990834 362 MSYGCVILKY 371
Cdd:pfam08541  81 LTWGAALLRW 90
PRK12880 PRK12880
beta-ketoacyl-ACP synthase III;
52-371 1.17e-32

beta-ketoacyl-ACP synthase III;


Pssm-ID: 171793  Cd Length: 353  Bit Score: 125.08  E-value: 1.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  52 KIIGHGHSYPSTEIYNDELKKYVDTNDEWIRTR----TGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINA 127
Cdd:PRK12880    9 KISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 128 SSTPQNLF-GDANNISNKIGCK-NSVNMDLTAACTGFIFAFVTAYNFL-NRYKNILIVGSDALSNFVDWRDRNTCVLFGD 204
Cdd:PRK12880   89 TQSPDFFMpSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIqSGLGKILLICGDTLSKFIHPKNMNLAPIFGD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 205 AAGAVVLQRTEgkeENKIFnYYLGSDSELNDLLTI------NFDHDKYNLDN----PNVNKYGKLHMNGKEVFKYTISNI 274
Cdd:PRK12880  169 GVSATLIEKTD---FNEAF-FELGSDGKYFDKLIIpkgamrIPKADIFNDDSlmqtEEFRQLENLYMDGANIFNMALECE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 275 PKILKKAIQNSNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVL-VNLDEYANTSAASIPLCFSENIKNGKIKTNdii 353
Cdd:PRK12880  245 PKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFKAS--- 321

                         330
                  ....*....|....*...
gi 1370990834 354 cMCGFGAGMSYGCVILKY 371
Cdd:PRK12880  322 -LSAFGAGLSWGSAVLNF 338
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
 153-230 1.86e-32

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: 116.46  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 153 MDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGAVVLQRTEGkEENKIFNYYLGSD 230
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIrsGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDE-PGARILDSVLGSD 79
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 79-370 6.69e-31

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 120.75  E-value: 6.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  79 EWIRTRTGIKKR----------------RILKR-DENISMLQ---IDSATQALKTSSLKPSDIDMVINASSTPQNLF-GD 137
Cdd:PRK07515   55 EFIEKASGIKSRyvmdkegildpdrmrpRIPERsNDELSIQAemgVAAARQALARAGRTAEDIDAVIVACSNMQRAYpAM 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 138 ANNISNKIGCKnSVNMDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSDALSNFVDWRDRNTCVLFGDAAGAVVLQRTE 215
Cdd:PRK07515  135 AIEIQQALGIE-GFAFDMNVACSSATFGIQTAANAIrsGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERAD 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 216 GKEENKIFNyYLGSdselnDLLT-----I--NFDHDKyNLDNPNVNKYGKL-HMNGKEVFKYTISNIPKILKKAIQNSNI 287
Cdd:PRK07515  214 TATSAGGFE-ILGT-----RLFTqfsnnIrnNFGFLN-RADPEGIGARDKLfVQEGRKVFKEVCPMVAEHIVEHLAENGL 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 288 NIEDINYFIFHQANIRIIETIAKnlnipmsKVL----------VNLDEYANTSAASIPLCFSENikNGKIKTNDIICMCG 357
Cdd:PRK07515  287 TPADVKRFWLHQANINMNQLIGK-------KVLgrdatpeeapVILDEYANTSSAGSIIAFHKH--SDDLAAGDLGVICS 357

                         330
                  ....*....|...
gi 1370990834 358 FGAGMSYGCVILK 370
Cdd:PRK07515  358 FGAGYSIGSVIVR 370
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
53-371 8.16e-17

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 80.43  E-value: 8.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  53 IIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTPQ 132
Cdd:PRK06840    7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVIYIGSEHK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 133 N--LFGDANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL---NRYKNILIVGSDALSNFVDWRDRNTCVLF--GDA 205
Cdd:PRK06840   87 DypVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLysdPSIENVLLVGGYRNSDLVDYDNPRTRFMFnfAAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 206 AGAVVLQRTEGKeeNKIFNYYLGSDSELNDLLTINFDHDKYNLDNPNV-NKYGKLHMNGKEVFK-----YTISNIPKILK 279
Cdd:PRK06840  167 GSAALLKKDAGK--NRILGSAIITDGSFSEDVRVPAGGTKQPASPETVeNRQHYLDVIDPESMKerldeVSIPNFLKVIR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 280 KAIQNSNINIEDINYF-IFH---QANIRIIEtiakNLNIPMSKVlVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICM 355
Cdd:PRK06840  245 EALRKSGYTPKDIDYLaILHmkrSAHIALLE----GLGLTEEQA-IYLDEYGHLGQLDQILSLHLALEQGKLKDGDLVVL 319

                         330
                  ....*....|....*.
gi 1370990834 356 CGFGAGMSYGCVILKY 371
Cdd:PRK06840  320 VSAGTGYTWAATVIRW 335
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 85-361 5.81e-12

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


Pssm-ID: 181732  Cd Length: 338  Bit Score: 66.06  E-value: 5.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  85 TGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINASSTPQNLF-GDANNISNKIGC-KNSVNMDLTAACTGF 162
Cdd:PRK09258   47 TGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEpATACRVHHNLGLpKSCANFDVSNACLGF 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 163 IFAFVTAYNFLNR--YKNILIVGSDALSNFVDW------RDRNTCVLF---------GDAAGAVVLQRTEGKEENKIfny 225
Cdd:PRK09258  127 LNGMLDAANMIELgqIDYALVVSGESAREIVEAtidrllAPETTREDFaqsfatltlGSGAAAAVLTRGSLHPRGHR--- 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 226 YLG----SDSELNDLLtinfdhdkynldnpnvnKYGKLHM--NGKEVFKYTISNIPKILKKAIQNSNINIEDINYFIFHQ 299
Cdd:PRK09258  204 LLGgvtrAATEHHELC-----------------QGGRDGMrtDAVGLLKEGVELAVDTWEAFLAQLGWAVEQVDRVICHQ 266

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370990834 300 ANIRIIETIAKNLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAG 361
Cdd:PRK09258  267 VGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSG 328
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 53-363 1.25e-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: 59.16  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  53 IIGHGHSYPSTEIYNDELKKYV--DTNDE----------WIRTRTGIKKRRIL---------KRDENISMLQ-------- 103
Cdd:cd00831     4 ILAIGTAVPPHRVPQSELVDFYrrLFSSDhlpelkeklkRLCAKTGIETRYLVlpggeetyaPRPEMSPSLDerndiale 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 104 ------IDSATQALKTSSLKPSDIDMVINASSTpqnlFGDANNIS----NKIGCKNSVN------MdltaACTGFIFAFV 167
Cdd:cd00831    84 earelaEEAARGALDEAGLRPSDIDHLVVNTST----GNPTPSLDamliNRLGLRPDVKrynlggM----GCSAGAIALD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 168 TAYNFL--NRYKNILIVGSDALSNFVDWRD-RNTCV---LFGDAAGAVVL--QRTEGKEENKIFNyYLGSDSEL--NDLL 237
Cdd:cd00831   156 LAKDLLeaNPGARVLVVSTELCSLWYRGPDhRSMLVgnaLFGDGAAAVLLsnDPRDRRRERPLFE-LVRAASTLlpDSED 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 238 TINFDHDKynldnpnvnkyGKLHMN-GKEVFKYTISNIPKILKKAIQNSNINI--EDINYFIFHQANIRIIETIAKNLNI 314
Cdd:cd00831   235 AMGWHLGE-----------EGLTFVlSRDVPRLVEKNLERVLRKLLARLGIGLfkLAFDHWCVHPGGRAVLDAVEKALGL 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370990834 315 PMSKVLVN---LDEYANTSAASIPLCFSENIKNGKIKTNDIICMCGFGAGMS 363
Cdd:cd00831   304 SPEDLEASrmvLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
PRK06816 PRK06816
StlD/DarB family beta-ketosynthase;
278-355 1.28e-06

StlD/DarB family beta-ketosynthase;


Pssm-ID: 235866  Cd Length: 378  Bit Score: 49.91  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 278 LKKAIQNSNINIEDINYFIFHQANIRIIETIAK-----NLNIPMSKVLVNLDEYANTSAASIPLCFSENIKNGKIKTND- 351
Cdd:PRK06816  278 LLELVDKRNLDPDDIDYFLPHYSSEYFREKIVEllakaGFMIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQk 357


                  ....
gi 1370990834 352 IICM 355
Cdd:PRK06816  358 ILCF 361
PRK04262 PRK04262
hypothetical protein; Provisional
 53-361 7.52e-05

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 44.13  E-value: 7.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834  53 IIGHGHSYPSTEIYNDELKKYVDTNDEWIRTRTGIKKRRILKRDENISMLQIDSATQALKTSSLKPSDIDMVINAS-STP 131
Cdd:PRK04262    5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGSeSHP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 132 QNLFGDANNISNKIGCKNSVN-MDLTAACTGFIFAFVTAYNFL--NRYKNILIVGSD-ALSNFVDwrdrntcVL-FGDAA 206
Cdd:PRK04262   85 YAVKPTATIVAEALGATPDLTaADLEFACKAGTAALQAAMGLVksGMIKYALAIGADtAQGAPGD-------ALeYTAAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 207 GAVVLqrTEGKEEN-KIFN--YYLGSDselndllTINF---DHDKYnldnpnvnkygKLHMNG----KEVFKYTISNIPK 276
Cdd:PRK04262  158 GGAAF--IIGKEEViAEIEatYSYTTD-------TPDFwrrEGEPY-----------PRHGGRftgePAYFKHIISAAKG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 277 ILKKaiqnSNINIEDINYFIFHQANIRIIETIAKNLNIPMSKVLVNL--DEYANTSAASIPLCFSENIKNGkiKTNDIIC 354
Cdd:PRK04262  218 LMEK----LGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGLAAVLDVA--KPGDRIL 291


                  ....*..
gi 1370990834 355 MCGFGAG 361
Cdd:PRK04262  292 VVSFGSG 298
ASKHA_NBD_HSP70_DDRA cd24030
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ...
 268-315 6.44e-03

nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) and similar proteins; DDRA, also called DDR large subunit, diol dehydratase-reactivase large subunit, diol dehydratase-reactivating factor alpha subunit, or DDR alpha subunit, is the large subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivating inactivated DD holoenzyme in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one. DDR has weak ATPase activity which is required for DD reactivation. DDRA contains the adenosine nucleotide binding site. DDRA has four domains, the ATPase domain, the swiveling domain, the linker domain, and the insert domain. The model corresponds to the ATPase domain. DDRA belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation.


Pssm-ID: 466880  Cd Length: 260  Bit Score: 37.96  E-value: 6.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370990834 268 KYTISNIPKI---LKKAIQNSNINIEDINYFIFHQANIRIIETIAKNLNIP 315
Cdd:cd24030    39 KGTLQNVPGIikaLELALEKAGINLSDIDLIRLNEAMQQIARELEEELGIP 89
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 102-188 7.54e-03

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: 38.01  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370990834 102 LQIDSATQALKTSSLKPSDIDMVINASSTPQNLFGD-ANNISNKIGCKNSVNMDLTAACTGFIFAFVTAYNFL--NRYKN 178
Cdd:cd00829    19 LAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFpGALIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAIasGLADV 98

                          90
                  ....*....|
gi 1370990834 179 ILIVGSDALS 188
Cdd:cd00829    99 VLVVGAEKMS 108
 
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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