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Conserved domains on  [gi|579654827|gb|EUW99603|]
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3-oxoacyl-[acyl-carrier-protein] synthase 3 [Staphylococcus aureus M0310]

Protein Classification

beta-ketoacyl-ACP synthase III( domain architecture ID 11483998)

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
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
1-312 0e+00

beta-ketoacyl-ACP synthase 3;


:

Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 505.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:PRK09352   2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:PRK09352  82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEvSEGRGIISYEMGSDGTGGKHLYLD-------KDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDID 233
Cdd:PRK09352 162 AGAVVLGA-SEEPGILSTHLGSDGSYGDLLYLPgggsrgpASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDID 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579654827 234 LFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTIKWG 312
Cdd:PRK09352 241 WLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRWP 319
 
Name Accession Description Interval E-value
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
1-312 0e+00

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 505.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:PRK09352   2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:PRK09352  82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEvSEGRGIISYEMGSDGTGGKHLYLD-------KDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDID 233
Cdd:PRK09352 162 AGAVVLGA-SEEPGILSTHLGSDGSYGDLLYLPgggsrgpASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDID 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579654827 234 LFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTIKWG 312
Cdd:PRK09352 241 WLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRWP 319
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
1-311 4.15e-166

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: 464.20  E-value: 4.15e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:COG0332   81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEVSEGRGIISYEMGSDGTGGKHLYL------------DKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLT 228
Cdd:COG0332  161 AGAVVLEASEEGPGILGSVLGSDGSGADLLVVpaggsrnppspvDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 229 SDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMT 308
Cdd:COG0332  241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320

                 ...
gi 579654827 309 IKW 311
Cdd:COG0332  321 LRW 323
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
2-309 3.04e-160

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: 449.30  E-value: 3.04e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   2 NVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATA 81
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  82 TGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGA 161
Cdd:cd00830   81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 162 GAVIIGEVSEGRGIISYEMGSDGTGGKHLYL------------DKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTS 229
Cdd:cd00830  161 GAVVLEATEEDPGILDSVLGSDGSGADLLTIpaggsrspfedaEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 230 DDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTI 309
Cdd:cd00830  241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
1-311 2.47e-145

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: 411.78  E-value: 2.47e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827    1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:TIGR00747   1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:TIGR00747  81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  161 AGAVIIGEVSEGRGIISYEMGSDGTGGKHLYLDKD-------TGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDID 233
Cdd:TIGR00747 161 AGAVVLGESEDPGGIISTHLGADGTQGEALYLPAGgrptsgpSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579654827  234 LFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTIKW 311
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
223-311 3.22e-43

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: 143.41  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  223 EKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGL 302
Cdd:pfam08541   2 EKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAGL 81

                  ....*....
gi 579654827  303 TWGAMTIKW 311
Cdd:pfam08541  82 TWGAALLRW 90
 
Name Accession Description Interval E-value
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
1-312 0e+00

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 505.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:PRK09352   2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:PRK09352  82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEvSEGRGIISYEMGSDGTGGKHLYLD-------KDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDID 233
Cdd:PRK09352 162 AGAVVLGA-SEEPGILSTHLGSDGSYGDLLYLPgggsrgpASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDID 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579654827 234 LFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTIKWG 312
Cdd:PRK09352 241 WLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRWP 319
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
1-311 4.15e-166

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: 464.20  E-value: 4.15e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:COG0332   81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEVSEGRGIISYEMGSDGTGGKHLYL------------DKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLT 228
Cdd:COG0332  161 AGAVVLEASEEGPGILGSVLGSDGSGADLLVVpaggsrnppspvDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 229 SDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMT 308
Cdd:COG0332  241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320

                 ...
gi 579654827 309 IKW 311
Cdd:COG0332  321 LRW 323
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
2-309 3.04e-160

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: 449.30  E-value: 3.04e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   2 NVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATA 81
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  82 TGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGA 161
Cdd:cd00830   81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 162 GAVIIGEVSEGRGIISYEMGSDGTGGKHLYL------------DKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTS 229
Cdd:cd00830  161 GAVVLEATEEDPGILDSVLGSDGSGADLLTIpaggsrspfedaEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 230 DDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTI 309
Cdd:cd00830  241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
1-312 4.51e-147

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 416.19  E-value: 4.51e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:PRK12879   3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:PRK12879  83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEVSEGRGIISYEMGSDGTGGKHLY-----------LDKDTGKLKMNGREVFKFAVRIMGDASTRVVEKANLTS 229
Cdd:PRK12879 163 AGAVVLEATENEPGFIDYVLGTDGDGGDILYrtglgttmdrdALSGDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 230 DDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTI 309
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322

                 ...
gi 579654827 310 KWG 312
Cdd:PRK12879 323 KWG 325
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
1-311 2.47e-145

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: 411.78  E-value: 2.47e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827    1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:TIGR00747   1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   81 ATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:TIGR00747  81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  161 AGAVIIGEVSEGRGIISYEMGSDGTGGKHLYLDKD-------TGKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDID 233
Cdd:TIGR00747 161 AGAVVLGESEDPGGIISTHLGADGTQGEALYLPAGgrptsgpSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579654827  234 LFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTIKW 311
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
5-311 6.49e-100

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


Pssm-ID: 215185  Cd Length: 379  Bit Score: 298.57  E-value: 6.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   5 IKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGD 84
Cdd:PLN02326  50 LVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSSPD 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  85 MPFPTvANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGAGAV 164
Cdd:PLN02326 130 DLFGS-APQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAGAV 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 165 IIGEVSEGR-GIISYEMGSDGTGGKHL-----YLDKDTGK------------------LKMNGREVFKFAVRIMGDASTR 220
Cdd:PLN02326 209 VLQACDDDEdGLLGFDMHSDGNGHKHLhatfkGEDDDSSGgntngvgdfppkkasyscIQMNGKEVFKFAVRCVPQVIES 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 221 VVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGG 300
Cdd:PLN02326 289 ALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGFGA 368
                        330
                 ....*....|.
gi 579654827 301 GLTWGAMTIKW 311
Cdd:PLN02326 369 GLTWGSAIVRW 379
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
1-311 5.80e-97

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


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 289.15  E-value: 5.80e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:CHL00203   1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATGDMPFPTvANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:CHL00203  81 STPDDLFGS-ASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEVSEGrGIISYEMGSDGTGGKHLYL------DKDTGKLK----------MNGREVFKFAVRIMGDASTRVVEK 224
Cdd:CHL00203 160 AGAAIIGASYEN-SILGFKLCTDGKLNSHLQLmnkpvnNQSFGTTKlpqgqyqsisMNGKEVYKFAVFQVPAVIIKCLNA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 225 ANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTW 304
Cdd:CHL00203 239 LNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTW 318

                 ....*..
gi 579654827 305 GAMTIKW 311
Cdd:CHL00203 319 GAIVLKW 325
PRK05963 PRK05963
beta-ketoacyl-ACP synthase III;
5-311 1.51e-88

beta-ketoacyl-ACP synthase III;


Pssm-ID: 180328 [Multi-domain]  Cd Length: 326  Bit Score: 267.74  E-value: 1.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   5 IKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGD 84
Cdd:PRK05963   6 IAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATSTPD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  85 MPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDyHNILVVGADKLSKITDLTDRSTAVLFGDGAGAV 164
Cdd:PRK05963  86 HLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAGAV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 165 IIGEVS-EGRGIISYEMGSDG---------TGGKHL--YLDKDTGKLKM---NGREVFKFAVRIMGDASTRVVEKANLTS 229
Cdd:PRK05963 165 VLAPSAkANSGVLGSQLISDGshydlikipAGGSARpfAPERDASEFLMtmqDGRAVFTEAVRMMSGASQNVLASAAMTP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 230 DDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTI 309
Cdd:PRK05963 245 QDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVM 324

                 ..
gi 579654827 310 KW 311
Cdd:PRK05963 325 RV 326
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
2-309 1.85e-61

"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: 198.43  E-value: 1.85e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   2 NVGIKGFGAYAPEKIIDNAYFEQFLdtSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATA 81
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  82 TGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDlTDRSTAVLFGDGA 161
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLD-EGSALEPTLGDGA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 162 GAVIIG--EVSEGRGIISYEMGSDGTGGKHLY--LDKDTGK-----------LKMNGREVFKFAVRIMGDASTRVVEKAN 226
Cdd:cd00827  158 AAMLVSrnPGILAAGIVSTHSTSDPGYDFSPYpvMDGGYPKpcklayairltAEPAGRAVFEAAHKLIAKVVRKALDRAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 227 LtSDDIDLFIPHQANI-RIMESARERLGISKDKMSVS----VNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGG 301
Cdd:cd00827  238 L-SEDIDYFVPHQPNGkKILEAVAKKLGGPPEKASQTrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSG 316

                 ....*...
gi 579654827 302 LTWGAMTI 309
Cdd:cd00827  317 FTAEAFVL 324
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
3-311 4.55e-58

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 189.66  E-value: 4.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   3 VGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQdTSDLAYEASVKAIADAGIQPEDIDMIIVATAT 82
Cdd:PRK07204   5 ISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVDGET-SSYMGAEAAKKAVEDAKLTLDDIDCIICASGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  83 GDMPFPTVANMLQERLGTGK--VASMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDG 160
Cdd:PRK07204  84 IQQAIPCTASLIQEQLGLQHsgIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGDG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 161 AGAVIIGEVSEGRGIISYEMGSDGTGG--------------KHLYLDKDTGKL-KMNGREVFKFAVRIMGDASTRVVEKA 225
Cdd:PRK07204 164 AAAVVITKGDHSSRILASHMETYSSGAhlseirgggtmihpREYSEERKEDFLfDMNGRAIFKLSSKYLMKFIDKLLMDA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 226 NLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWG 305
Cdd:PRK07204 244 GYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSIG 323

                 ....*.
gi 579654827 306 AMTIKW 311
Cdd:PRK07204 324 GILLEY 329
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
223-311 3.22e-43

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: 143.41  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  223 EKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGL 302
Cdd:pfam08541   2 EKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAGL 81

                  ....*....
gi 579654827  303 TWGAMTIKW 311
Cdd:pfam08541  82 TWGAALLRW 90
PRK12880 PRK12880
beta-ketoacyl-ACP synthase III;
33-311 3.65e-37

beta-ketoacyl-ACP synthase III;


Pssm-ID: 171793  Cd Length: 353  Bit Score: 135.86  E-value: 3.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  33 ISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLG-TGKVASMDQLAA 111
Cdd:PRK12880  42 MKKVIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVVTQSPDFFMPSTACYLHQLLNlSSKTIAFDLGQA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 112 CSGFMYSMITAKQYVQSGdYHNILVVGADKLSKITDLTDRSTAVLFGDGAGAVIIGEVSEGRGIisYEMGSDGTG----- 186
Cdd:PRK12880 122 CAGYLYGLFVAHSLIQSG-LGKILLICGDTLSKFIHPKNMNLAPIFGDGVSATLIEKTDFNEAF--FELGSDGKYfdkli 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 187 ---GKHLYLDKDT---------------GKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANIRIMESA 248
Cdd:PRK12880 199 ipkGAMRIPKADIfnddslmqteefrqlENLYMDGANIFNMALECEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCI 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579654827 249 RERLGISKDKM-SVSVNKYGNTSAASIPlSIDQELKNGKlkdDDTIVLVGFGGGLTWGAMTIKW 311
Cdd:PRK12880 279 KEELKLNDDKVpNFIMEKYANLSACSLP-ALLCELDTPK---EFKASLSAFGAGLSWGSAVLNF 338
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
1-312 9.62e-34

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 126.27  E-value: 9.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNayfEQFLDTSD--EWI--SKMtGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMI 76
Cdd:PRK06840   3 MNVGIVGTGVYLPKDVMTA---EEIAEKTGipEEVviEKF-GIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  77 I-VATATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAK-QYVQSGDYHNILVVGADKLSKITDLTDRSTA 154
Cdd:PRK06840  79 IyIGSEHKDYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKdLLYSDPSIENVLLVGGYRNSDLVDYDNPRTR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 155 VLF--GDGAGAVIIGEVSEGRGIISYEMGSDGT----------GGKHL-----------YLD-KDTGKLKMNGREV---- 206
Cdd:PRK06840 159 FMFnfAAGGSAALLKKDAGKNRILGSAIITDGSfsedvrvpagGTKQPaspetvenrqhYLDvIDPESMKERLDEVsipn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 207 FKFAVRimgdastRVVEKANLTSDDID-LFIPH---QANIRIMEsareRLGISKDKmSVSVNKYGNTSAASIPLSIDQEL 282
Cdd:PRK06840 239 FLKVIR-------EALRKSGYTPKDIDyLAILHmkrSAHIALLE----GLGLTEEQ-AIYLDEYGHLGQLDQILSLHLAL 306
                        330       340       350
                 ....*....|....*....|....*....|
gi 579654827 283 KNGKLKDDDTIVLVGFGGGLTWGAMTIKWG 312
Cdd:PRK06840 307 EQGKLKDGDLVVLVSAGTGYTWAATVIRWG 336
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
36-311 2.38e-32

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


Pssm-ID: 181732  Cd Length: 338  Bit Score: 122.30  E-value: 2.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  36 MTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLG-TGKVASMDQLAACSG 114
Cdd:PRK09258  46 LTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGlPKSCANFDVSNACLG 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 115 FMYSMITAKQYVQSGDYHNILVVGADKLSKITDLT------DRSTAVLF---------GDGAGAVIIGEVSEGRGIISYE 179
Cdd:PRK09258 126 FLNGMLDAANMIELGQIDYALVVSGESAREIVEATidrllaPETTREDFaqsfatltlGSGAAAAVLTRGSLHPRGHRLL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 180 MGSDGTGGKHLYL---DKDtgKLKMNGREVFKFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANIRIMESARERLGISK 256
Cdd:PRK09258 206 GGVTRAATEHHELcqgGRD--GMRTDAVGLLKEGVELAVDTWEAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDP 283
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 579654827 257 DKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLTWGAMTIKW 311
Cdd:PRK09258 284 EKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSGLNCSMLEVKW 338
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
106-184 3.26e-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: 114.54  E-value: 3.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  106 MDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGAGAVIIGEV-SEGRGIISYEMGSDG 184
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATdEPGARILDSVLGSDG 80
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
54-307 6.09e-30

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: 115.81  E-value: 6.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  54 LAYEASVKAIADAGIQPED----IDMIIVATATGD---------------------MPFPTVANMLQERLGTGKVAsMDQ 108
Cdd:cd00825   14 LGFEAAERAIADAGLSREYqknpIVGVVVGTGGGSprfqvfgadamravgpyvvtkAMFPGASGQIATPLGIHGPA-YDV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 109 LAACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITD------------------LTDRSTAVLFGDGAGAVIIGEVS 170
Cdd:cd00825   93 SAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDcefdamgalstpekasrtFDAAADGFVFGDGAGALVVEELE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 171 EGR--------GIISYEMGSDGTGGkhlyldkdtGKLKMNGREVfkfaVRIMGDAstrvVEKANLTSDDIDLFIPHQANI 242
Cdd:cd00825  173 HALargahiyaEIVGTAATIDGAGM---------GAFAPSAEGL----ARAAKEA----LAVAGLTVWDIDYLVAHGTGT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 243 RIMESARERLGISKDK---MSVSVNK--YGNTSAASIPLSIDQELKNGKLKDD-------------------------DT 292
Cdd:cd00825  236 PIGDVKELKLLRSEFGdksPAVSATKamTGNLSSAAVVLAVDEAVLMLEHGFIppsihieeldeaglnivtettprelRT 315
                        330
                 ....*....|....*
gi 579654827 293 IVLVGFGGGLTWGAM 307
Cdd:cd00825  316 ALLNGFGLGGTNATL 330
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
52-309 4.65e-29

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: 111.77  E-value: 4.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  52 SDLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDY 131
Cdd:cd00327    8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 132 HNILVVGADKlskitdltdrstaVLFGDGAGAVIIGEVSEG--RGIISYEMgsdgTGGKHLYLDKDTGKLKMNGREvfkf 209
Cdd:cd00327   88 DIVLAGGSEE-------------FVFGDGAAAAVVESEEHAlrRGAHPQAE----IVSTAATFDGASMVPAVSGEG---- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 210 AVRIMGDAstrvVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDK---MSVSVNK--YGNTSAASIPLSIDQELKN 284
Cdd:cd00327  147 LARAARKA----LEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvrsPAVSATLimTGHPLGAAGLAILDELLLM 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 579654827 285 GKLKDD-------DTIVLVGFGGGLTWGAMTI 309
Cdd:cd00327  223 LEHEFIpptprepRTVLLLGFGLGGTNAAVVL 254
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
17-303 2.45e-27

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: 109.24  E-value: 2.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  17 IDNAYFEqfLDTSDEW----ISKMTGIKERHwADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGdMPFPTVAN 92
Cdd:cd00831   50 IETRYLV--LPGGEETyaprPEMSPSLDERN-DIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTG-NPTPSLDA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  93 MLQERLG---TGKVASMDQLaACSGFMYSMITAKQYVQSGDYHNILVV----------GADKLSKItdltdRSTAvLFGD 159
Cdd:cd00831  126 MLINRLGlrpDVKRYNLGGM-GCSAGAIALDLAKDLLEANPGARVLVVstelcslwyrGPDHRSML-----VGNA-LFGD 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 160 GAGAVIIGEVSEGRGIISYEMGSDGTGGKHLYLDKD--TGKLKMNGREVF--KFAVRIMGDASTRVVEKA------NLTS 229
Cdd:cd00831  199 GAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSEDamGWHLGEEGLTFVlsRDVPRLVEKNLERVLRKLlarlgiGLFK 278
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579654827 230 DDIDLFIPHQANIRIMESARERLGISKDKMSVS---VNKYGNTSAASIPLSIDQELKNGKLKDDDTIVLVGFGGGLT 303
Cdd:cd00831  279 LAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASrmvLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
1-301 9.61e-27

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 108.04  E-value: 9.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDN--------AYFEQF----------------LDTSDEWISKMTGIKERHWAD---------- 46
Cdd:PRK07515   1 HNVVISGTGLYTPPESISNeelvasfnAYVERFnaenaaaiaagevealQPSSSEFIEKASGIKSRYVMDkegildpdrm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  47 --------DDQ--DTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVAsMDQLAACSGFM 116
Cdd:PRK07515  81 rpripersNDElsIQAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGFA-FDMNVACSSAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 117 YSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLFGDGAGAVIIGEVSEGRGIISYEMgsdgtGGKHL------ 190
Cdd:PRK07515 160 FGIQTAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATSAGGFEI-----LGTRLftqfsn 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 191 -------YLDK-------DTGKL-KMNGREVFKFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANIRIMES-ARERLG- 253
Cdd:PRK07515 235 nirnnfgFLNRadpegigARDKLfVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKRFWLHQANINMNQLiGKKVLGr 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 579654827 254 -ISKDKMSVSVNKYGNTSAA-SIplsIDQELKNGKLKDDDTIVLVGFGGG 301
Cdd:PRK07515 315 dATPEEAPVILDEYANTSSAgSI---IAFHKHSDDLAAGDLGVICSFGAG 361
BH0617 COG3424
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ...
20-311 3.32e-24

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


Pssm-ID: 442650 [Multi-domain]  Cd Length: 351  Bit Score: 100.60  E-value: 3.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  20 AYFEQFLDTSDEWISKM------TGIKERHWA----DDDQDTS-------------DLAYEASVKAIADAGIQPEDIDMI 76
Cdd:COG3424   23 EFAAELFGLDERDRRRLrrlfenSGIETRHSVlpleWYLEPPSfgernalyieealELAEEAARRALDKAGLDPEDIDHL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  77 IVATATG------------DMPF-PTVanmlqERLGtgkVASMDQLAACSGfmysMITAKQYVQSGDYHNILVVgADKLS 143
Cdd:COG3424  103 VTVSCTGfaapgldarlinRLGLrPDV-----RRLP---VGGMGCAAGAAG----LRRAADFLRADPDAVVLVV-CVELC 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 144 KIT---DLTDRSTAV---LFGDGAGAVIIgeVSEGRGIISYEMGSDGTggkHLYLD---------KDTGkLKMN-GREVF 207
Cdd:COG3424  170 SLTfqrDDDSKDNLVanaLFGDGAAAVVV--SGDPRPGPGPRILAFRS---YLIPDtedvmgwdvGDTG-FRMVlSPEVP 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 208 KFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVSVN---KYGNTSAASIPLSIDQELKN 284
Cdd:COG3424  244 DLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREvlrEYGNMSSATVLFVLERLLEE 323
                        330       340
                 ....*....|....*....|....*..
gi 579654827 285 GKLKDDDTIVLVGFGGGLTWGAMTIKW 311
Cdd:COG3424  324 GAPAPGERGLAMAFGPGFTAELVLLRW 350
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
1-301 5.77e-23

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442651 [Multi-domain]  Cd Length: 382  Bit Score: 97.56  E-value: 5.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEkiidnayfeQFLDTSD---EW------ISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPE 71
Cdd:COG3425    1 MKVGIDAIGFYIPR---------YRLDLEElaeARgvdpekYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  72 DIDMIIVATATG---DMPfptVANMLQERLGTGKVASMDQLA-ACSGFMYSMITAKQYVQSGDYHNILVVGADklskiTD 147
Cdd:COG3425   72 DIGAVYVGTESGpdaSKP---IATYVHGALGLPPNCRAFELKfACYAGTAALQAALGWVASGPNKKALVIASD-----IA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 148 LTDRSTA--VLFGDGAGAVIIGEvsEGRgIISYEMGSdGTGGKHLYldkDTgkLKMNGRevfKFAV-----------RIM 214
Cdd:COG3425  144 RYGPGSAgeYTQGAGAVAMLVGA--DPR-IAEIEGGS-GSYTTDVM---DF--WRPNGS---DYPLvdgrfsepaylDHL 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 215 GDASTRVVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDKM-----------SVSVNKY-GNTSAASIPLSIDQEL 282
Cdd:COG3425  212 EEAVKDYKEKTGLKPDDFDYFVFHQPFGKMPKKAAKKLGRKAGREiqedfeeqvepSLIYSRRiGNTYTGSLYLGLASLL 291
                        330
                 ....*....|....*....
gi 579654827 283 KNGKLKDDDTIVLVGFGGG 301
Cdd:COG3425  292 DNAKDLPGDRIGLFSYGSG 310
PRK06816 PRK06816
StlD/DarB family beta-ketosynthase;
1-295 1.94e-21

StlD/DarB family beta-ketosynthase;


Pssm-ID: 235866  Cd Length: 378  Bit Score: 93.05  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKM-------TGIKERHWA-DDDQDT----SDLAYEASVKAIADAGI 68
Cdd:PRK06816   1 MNVYITSTGAFLPGEPVSNDEMEAYLGLINGKPSRArriilrnNGIKTRHYAlDPEGRPthsnAQMAAEAIRDLLDDAGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  69 QPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVasmdQLAACSGFMYSMITAKQY----VQSGDYHNILVVGADKLSK 144
Cdd:PRK06816  81 SLGDIELLACGTSQPDQLMPGHASMVHGELGAPPI----EVVSSAGVCAAGMMALKYaylsVKAGESRNAVATASELASR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 145 I------------TDLTDRSTAVLF---------GDGAGAVII------GEVS---EGRGIISY------------EMGS 182
Cdd:PRK06816 157 WfrasrfeaeeekLAELEENPEIAFekdflrwmlSDGAGAVLLenkprpDGLSlriDWIDLRSYagelpvcmyagaEKNE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 183 DGTGGKHLYLDKDTGK------LKMNGREVFKFAVRIMGDASTRVVEKANLTSDDIDLFIPHQANirimESARERL---- 252
Cdd:PRK06816 237 DGSLKGWSDYPPEEAEaasalsLKQDVRLLNENIVVYTIKPLLELVDKRNLDPDDIDYFLPHYSS----EYFREKIvell 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 579654827 253 -----GISKDKMSVSVNKYGNTSAASIPLSIDQELKNGKLKDDDTIVL 295
Cdd:PRK06816 313 akagfMIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
PRK04262 PRK04262
hypothetical protein; Provisional
1-301 2.92e-16

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 78.02  E-value: 2.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   1 MNVGIKGFGAYAPEKIIDNAYFEQFLDTSDEWISKMTGIKERHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVAT 80
Cdd:PRK04262   1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  81 ATgdMPF---PTvANMLQERLGTGKVA-SMDQLAACSGFMYSMITAKQYVQSGDYHNILVVGADklskiTDLTDRSTAVL 156
Cdd:PRK04262  81 ES--HPYavkPT-ATIVAEALGATPDLtAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGAD-----TAQGAPGDALE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 157 FGDGAGAV--IIGE---VSEGRGIIS---------------YEMGSDGTGGKHLYldkdtgklkmngrevFKfavRIMGd 216
Cdd:PRK04262 153 YTAAAGGAafIIGKeevIAEIEATYSyttdtpdfwrregepYPRHGGRFTGEPAY---------------FK---HIIS- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 217 ASTRVVEKANLTSDDIDLFIPHQANIRIMESARERLGISKDKMS--VSVNKYGNTSAASIPLSIDQELKNGklKDDDTIV 294
Cdd:PRK04262 214 AAKGLMEKLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKpgLLTPYIGNTYSGSALLGLAAVLDVA--KPGDRIL 291

                 ....*..
gi 579654827 295 LVGFGGG 301
Cdd:PRK04262 292 VVSFGSG 298
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
36-150 1.83e-15

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: 76.15  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  36 MTGIKERhwadDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVASMDQLAACSGF 115
Cdd:cd00829    5 MTPFGRR----SDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 579654827 116 MYSMITAKQYVQSGDYHNILVVGADKLSKITDLTD 150
Cdd:cd00829   81 SAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDE 115
PLN03168 PLN03168
chalcone synthase; Provisional
54-310 1.26e-10

chalcone synthase; Provisional


Pssm-ID: 178712 [Multi-domain]  Cd Length: 389  Bit Score: 61.59  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  54 LAYEASVKAIADAGIQPEDIDMIIVATATGdMPFPTVANMLQERLG---TGKVASMDQlAACSGFMYSMITAKQYVQSGD 130
Cdd:PLN03168 104 LAAEAAQKAIKEWGGRKSDITHIVFATTSG-VNMPGADHALAKLLGlkpTVKRVMMYQ-TGCFGGASVLRVAKDLAENNK 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 131 YHNILVVGadklSKITDLTDRST----------AVLFGDGAGAVIIG-----EVSE--------GRGIISYemgSDGTGG 187
Cdd:PLN03168 182 GARVLAVA----SEVTAVTYRAPsenhldglvgSALFGDGAGVYVVGsdpkpEVEKalfevhwaGETILPE---SDGAID 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 188 KHL-------YLDKDTGKLKMNGREVFKFAVRimgdastrvveKANLTSDDIDLFIP-HQANIRIMESARERLGISKDKM 259
Cdd:PLN03168 255 GHLteaglifHLMKDVPGLISKNIEKFLNEAR-----------KCVGSPDWNEMFWAvHPGGPAILDQVEAKLKLTKDKM 323
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579654827 260 SVS---VNKYGNTSAASIPLSIDQ------ELKNGKL-KDDDTIVLVGFGGGLTWGAMTIK 310
Cdd:PLN03168 324 QGSrdiLSEFGNMSSASVLFVLDQirqrsvKMGASTLgEGSEFGFFIGFGPGLTLEVLVLR 384
PLN03171 PLN03171
chalcone synthase-like protein; Provisional
53-309 2.47e-08

chalcone synthase-like protein; Provisional


Pssm-ID: 178715 [Multi-domain]  Cd Length: 399  Bit Score: 54.62  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  53 DLAYEASVKAIADAGIQPEDIDMIIVATATGdMPFPTVANMLQERLGTGKVA--SMDQLAACSGFMYSMITAKQYVQSGD 130
Cdd:PLN03171 110 ELAAEAAKKAIAEWGRPAADITHLVVTTNSG-AHIPGVDFRLVPLLGLRPSVrrTMLHLNGCFAGAAALRLAKDLAENNR 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 131 YHNILVVGADKLSKITDLTD----RSTAV--LFGDGAGAVIIGE------------VSEGRGIISYemgSDGTGGKHLYL 192
Cdd:PLN03171 189 GARVLVVAAEITLLLFNGPDegcfQTLLNqgLFGDGAAAVIVGAdadaaerplfeiVSAAQAIIPE---SDDAINMHFTE 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 193 DKDTGKLkmNGREVfkfaVRIMGDASTRVVEK--ANLTSDDI-----DLFIP-HQANIRIMESARERLGISKDKMSVS-- 262
Cdd:PLN03171 266 GGLDGNI--GTRQV----PGLIGDNIERCLLDafAPLLGGDGgaewnDLFWAvHPGSSAILDQVDAALGLEPEKLAASrr 339
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 579654827 263 -VNKYGNTSAASIPLSIDqELKNGKLKDDDT------IVLVGFGGGLTWGAMTI 309
Cdd:PLN03171 340 vLSDYGNMFGATVIFALD-ELRRQMEEAAAAgawpelGVMMAFGPGLTVDAMLL 392
PRK12578 PRK12578
thiolase domain-containing protein;
47-162 9.07e-08

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 52.93  E-value: 9.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  47 DDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATA----TGDMPFPTVAnmlqERLG-TGKVaSMDQLAACSGFMYSMIT 121
Cdd:PRK12578  17 DDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTayrgIELYPAPIVA----EYSGlTGKV-PLRVEAMCATGLAASLT 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 579654827 122 AKQYVQSGDYHNILVVGADKLSKItdltDRSTAVLFGDGAG 162
Cdd:PRK12578  92 AYTAVASGLVDMAIAVGVDKMTEV----DTSTSLAIGGRGG 128
PRK06064 PRK06064
thiolase domain-containing protein;
53-143 2.46e-06

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 48.35  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  53 DLAYEASVKAIADAGIQPEDIDMIIVATATGDMpF---PTVANMLQERLGTGKVASMDQLAACSGFMYSMITAKQYVQSG 129
Cdd:PRK06064  24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGL-FvsqEHIAALIADYAGLAPIPATRVEAACASGGAALRQAYLAVASG 102
                         90
                 ....*....|....
gi 579654827 130 DYHNILVVGADKLS 143
Cdd:PRK06064 103 EADVVLAAGVEKMT 116
PLN03169 PLN03169
chalcone synthase family protein; Provisional
53-310 4.21e-06

chalcone synthase family protein; Provisional


Pssm-ID: 215612 [Multi-domain]  Cd Length: 391  Bit Score: 47.77  E-value: 4.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  53 DLAYEASVKAIADAGIQPEDIDMIiVATATGDMPFPTVANMLQERLG----TGKVasMDQLAACSGFMYSMITAKQYVQS 128
Cdd:PLN03169 108 QMAVEASLACIKEWGRPVSDITHL-VYVSSSEARLPGGDLYLAKQLGlspdVQRV--MLYFLGCSGGVAGLRVAKDIAEN 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 129 GDYHNILVVgadkLSKITDLTDRST----------AVLFGDGAGAVIIG----EVSEG------RGIISYEMGSDGTGGK 188
Cdd:PLN03169 185 NPGSRVLLT----TSETTILGFRPPspdrpydlvgAALFGDGAAAVIIGadpiPVSESpffelhTAIQQFLPGTEKTIDG 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 189 HLYLDKDTGKLkmnGRE--------VFKFAVRIMGdastrvveKANLTSDDI-DLFIP-HQANIRIMESARERLGISKDK 258
Cdd:PLN03169 261 RLTEEGINFKL---GRElpqkiednIEGFCKKLMK--------KAGLVEKDYnDLFWAvHPGGPAILNRLEKKLKLAPEK 329
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 579654827 259 MSVS---VNKYGNTSAASIPLSID---QELKNGKLKDDDTIVLVGFGGGLTWGAMTIK 310
Cdd:PLN03169 330 LECSrraLMDYGNVSSNTIVYVLEymrEELKKKGEEDEEWGLILAFGPGITFEGILAR 387
PLN03170 PLN03170
chalcone synthase; Provisional
54-303 9.49e-06

chalcone synthase; Provisional


Pssm-ID: 178714 [Multi-domain]  Cd Length: 401  Bit Score: 46.63  E-value: 9.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  54 LAYEASVKAIADAGIQPEDIDMIIVATATG-DMPFP--TVANMLQERLGTGKVASMDQlaACSGFMYSMITAKQYVQSGD 130
Cdd:PLN03170 109 LGKAAAQKAIKEWGQPKSKITHLVFCTTSGvDMPGAdyQLTKMLGLRPSVNRLMMYQQ--GCFAGGTVLRVAKDLAENNR 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 131 YHNILVVgadkLSKITDLTDRSTA----------VLFGDGAGAVIIGE-------------VSEGRGIISYEMGS-DG-- 184
Cdd:PLN03170 187 GARVLVV----CSEITAVTFRGPSeshldsmvgqALFGDGAAAVIVGAdpderverplfqlVSASQTILPDSEGAiDGhl 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 185 -TGGKHLYLDKDTGKLkmngreVFKFAVRIMGDASTRVvekaNLTSDDIDLFIPHQANIRIMESARERLGISKDKMSVS- 262
Cdd:PLN03170 263 rEVGLTFHLLKDVPGL------ISKNIERSLEEAFKPL----GITDYNSIFWVAHPGGPAILDQVEAKVGLEKERMRATr 332
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 579654827 263 --VNKYGNTSAASIPLSIDqELKNGKLKDD--------DTIVLVGFGGGLT 303
Cdd:PLN03170 333 hvLSEYGNMSSACVLFILD-EMRKRSAEDGqattgegfDWGVLFGFGPGLT 382
Chal_sti_synt_N pfam00195
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ...
54-167 3.77e-05

Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.


Pssm-ID: 395142  Cd Length: 225  Bit Score: 44.07  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   54 LAYEASVKAIADAGIQPEDIDMIIVATATG-DMPFPTVanMLQERLG---TGKVASMDQLAaCSGFMYSMITAKQYVQSG 129
Cdd:pfam00195 102 LGAEAALKAIKEWGQPKSKITHLVFCTTSGvRMPGADY--QLAKLLGlrpSVKRVMLYFQG-CYGGATVLRTAKDIAENN 178
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 579654827  130 DYHNILVVgadkLSKITDLTDRST----------AVLFGDGAGAVIIG 167
Cdd:pfam00195 179 PGARVLVV----CSEITVLGFRGPskdrldslvgAALFGDGAAAVIIG 222
PLN03173 PLN03173
chalcone synthase; Provisional
54-303 1.21e-04

chalcone synthase; Provisional


Pssm-ID: 178717 [Multi-domain]  Cd Length: 391  Bit Score: 43.14  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  54 LAYEASVKAIADAGIQPEDIDMIIVATATG-DMPFP--TVANMLQERLGTGKVASMDQLAACSGFMYSMitAKQYVQSGD 130
Cdd:PLN03173 105 LGKEAAAKAIKEWGQPKSKITHLVFCTTSGvDMPGAdyQLTKLLGLRSSVKRFMMYQQGCFAGGTVLRL--AKDLAENNK 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 131 YHNILVVgadkLSKITDLTDRSTA----------VLFGDGAGAVIIGE-------------VSEGRGIISyemGSDGTGG 187
Cdd:PLN03173 183 GARVLVV----CSEITAVTFRGPSdthldslvgqALFGDGAAAIIIGSdpvlgvekplfelVSAAQTILP---DSDGAID 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827 188 KHL-------YLDKDT-GKLKMNGREVFKFAVRIMGdastrvvekanlTSDDIDLF-IPHQANIRIMESARERLGISKDK 258
Cdd:PLN03173 256 GHLrevgltfHLLKDVpGLISKNVEKSLTEAFKPLG------------ISDWNSLFwIAHPGGPAILDQVEAKLALKPEK 323
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 579654827 259 MSVS---VNKYGNTSAASIPLSIDQELKNGKLKDDDTI-------VLVGFGGGLT 303
Cdd:PLN03173 324 LRATrhvLSEYGNMSSACVLFILDEMRKKSAEDGLKSTgeglewgVLFGFGPGLT 378
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
42-140 1.65e-04

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 42.75  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  42 RHWADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMpFPTvanmlQERLGTGKVASMDQL---------AAC 112
Cdd:PRK06289  17 RNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGEL-FAG-----QGHLGAMPATVHPALwgvpasrheAAC 90
                         90       100
                 ....*....|....*....|....*....
gi 579654827 113 -SGFMySMITAKQYVQSGDYHNILVVGAD 140
Cdd:PRK06289  91 aSGSV-ATLAAMADLRAGRYDVALVVGVE 118
PRK07516 PRK07516
thiolase domain-containing protein;
47-158 3.24e-04

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 41.86  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  47 DDQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMP---FPTvANMLQERLGTGKVASMDQLAACSGFMYSMITAK 123
Cdd:PRK07516  18 DAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSpqdFPA-SLVLQADPALRFKPATRVENACATGSAAVYAAL 96
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 579654827 124 QYVQSGDYHNILVVGADKLSKITdlTDRSTAVLFG 158
Cdd:PRK07516  97 DAIEAGRARIVLVVGAEKMTATP--TAEVGDILLG 129
PRK06158 PRK06158
thiolase; Provisional
53-136 3.35e-04

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 41.94  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  53 DLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVAnmlqERLGTGKVASMDQLAACSGFMYSMITAKQYVQSGDYH 132
Cdd:PRK06158  30 ELLAQAAHRALADAGLTMADVDGLFTASPDDALWGLSVA----EYLGIRPRFVDGTMIGGSSFLAHLLPAALALEAGLCD 105

                 ....
gi 579654827 133 NILV 136
Cdd:PRK06158 106 VALI 109
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
48-146 9.49e-04

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 39.98  E-value: 9.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827   48 DQDTSDLAYEASVKAIADAGIQPEDIDMIIVATATGDMPFPTVANMLQERLGTGKVAS---MDQLaaCSGFMYSMITAKQ 124
Cdd:pfam00108  20 DVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPavtINKV--CGSGLKAVYLAAQ 97
                          90       100
                  ....*....|....*....|..
gi 579654827  125 YVQSGDYHNILVVGADKLSKIT 146
Cdd:pfam00108  98 SIASGDADVVLAGGVESMSHAP 119
PRK08313 PRK08313
thiolase domain-containing protein;
38-163 2.20e-03

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 39.33  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  38 GIKERHWADDDQDTS--DLAYEASVKAIADAGIQPEDIDMIIVatatGDMP--FPTVAN---MLQERLGTGKVASMDQLA 110
Cdd:PRK08313   9 GTGQTKYVAKRQDVSmaGLVREAIDRALADAGLTWDDIDAVVV----GKAPdfFEGVMMpelFLADALGATGKPLIRVHT 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 579654827 111 ACSGFMYSMITAKQYVQSGDYHNILVVGADKLSKITDLTDRSTAVLF--GDGAGA 163
Cdd:PRK08313  85 AGSVGGSTAVVAASLVQSGVYRRVLAVAWEKQSESNAMWALSIPVPFtkPVGAGA 139
PRK06059 PRK06059
lipid-transfer protein; Provisional
44-144 2.63e-03

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 38.98  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579654827  44 WADDDQDTSDLAYEASVKAIADAGIQPEDIDMIIVA-TATGDMPFPTVANMLQERLGTGKVASMDQLAACSGFMYSMITA 122
Cdd:PRK06059  16 WGKWGRDFVEYGVVAARAALADAGLDWRDVQLVVGAdTIRNGYPGFVAGATFAQALGWNGAPVSSSYAACASGSQALQSA 95
                         90       100
                 ....*....|....*....|..
gi 579654827 123 KQYVQSGDYHNILVVGADKLSK 144
Cdd:PRK06059  96 RAQILAGLCDVALVVGADTTPK 117
 
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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