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Conserved domains on  [gi|491222589|ref|WP_005080899|]
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3-oxoacyl-ACP synthase III family protein [Mycobacteroides abscessus]

Protein Classification

3-oxoacyl-ACP synthase III family protein( domain architecture ID 11417379)

3-oxoacyl-ACP synthase III family protein such as Pseudomonas aeruginosa 2-heptyl-4(1H)-quinolone synthase subunit PqsC, which with PqsB, forms a complex that catalyzes the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to form 2-heptyl-4(1H)-quinolone

CATH:  3.40.47.10
EC:  2.3.1.180|2.3.1.-
Gene Ontology:  GO:0004315|GO:0006633
PubMed:  10593943|10600651|14523010|11969206|1354266
SCOP:  4000864

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 3-325 1.16e-55

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: 184.16  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   3 RTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginLATGEQThslADMATSAARQALSRADIDPSEIG 82
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRI---AAPDETT---SDLAVEAARKALEAAGIDPEDID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  83 FLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL-TEERPLGLVIGADACYKHL-PLDRESS 160
Cdd:COG0332   75 LIIVATVTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIrSGQAKNVLVVGAETLSRIVdWTDRSTC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 161 samppselvnfVLFGDGAGAAVLALDDTDAQL----------GITALVNRFSGLGRDPGQQIEWfglaDRHLEQPGlNED 230
Cdd:COG0332  155 -----------VLFGDGAGAVVLEASEEGPGIlgsvlgsdgsGADLLVVPAGGSRNPPSPVDEG----DHYLRMDG-REV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 231 YK-AIEHWVpllskDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASNsREISVVADTGNNGNALPFLQIDA 309
Cdd:COG0332  219 FKfAVRNLP-----EVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEE-KVVVNIDRYGNTSAASIPLALDE 292

                        330
                 ....*....|....*...
gi 491222589 310 LSRE--VQPGERAAVVAI 325
Cdd:COG0332  293 ALREgrIKPGDLVLLAGF 310
 
Name Accession Description Interval E-value
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 3-325 1.16e-55

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: 184.16  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   3 RTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginLATGEQThslADMATSAARQALSRADIDPSEIG 82
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRI---AAPDETT---SDLAVEAARKALEAAGIDPEDID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  83 FLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL-TEERPLGLVIGADACYKHL-PLDRESS 160
Cdd:COG0332   75 LIIVATVTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIrSGQAKNVLVVGAETLSRIVdWTDRSTC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 161 samppselvnfVLFGDGAGAAVLALDDTDAQL----------GITALVNRFSGLGRDPGQQIEWfglaDRHLEQPGlNED 230
Cdd:COG0332  155 -----------VLFGDGAGAVVLEASEEGPGIlgsvlgsdgsGADLLVVPAGGSRNPPSPVDEG----DHYLRMDG-REV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 231 YK-AIEHWVpllskDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASNsREISVVADTGNNGNALPFLQIDA 309
Cdd:COG0332  219 FKfAVRNLP-----EVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEE-KVVVNIDRYGNTSAASIPLALDE 292

                        330
                 ....*....|....*...
gi 491222589 310 LSRE--VQPGERAAVVAI 325
Cdd:COG0332  293 ALREgrIKPGDLVLLAGF 310
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 7-325 2.20e-53

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: 178.12  E-value: 2.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   7 VLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginLATGEQThslADMATSAARQALSRADIDPSEIGFLVL 86
Cdd:cd00830    4 ILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRI---ADPGETT---SDLAVEAAKKALEDAGIDADDIDLIIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  87 GTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTeerpLG-----LVIGADACYKHL-PLDRESS 160
Cdd:cd00830   78 ATSTPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIR----SGgaknvLVVGAETLSRILdWTDRSTA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 161 samppselvnfVLFGDGAGAAVLALDDTDAQLGITALVNRFSGL------GRDPGQQIEWFGLADRHLEQPGlNEDYKai 234
Cdd:cd00830  154 -----------VLFGDGAGAVVLEATEEDPGILDSVLGSDGSGAdlltipAGGSRSPFEDAEGGDPYLVMDG-REVFK-- 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 235 ehWVPLLSKDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASNsREISVVADTGNNGNA-LPFlqidALSR- 312
Cdd:cd00830  220 --FAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEE-KVVVNLDRYGNTSAAsIPL----ALDEa 292

                        330
                 ....*....|....*..
gi 491222589 313 ----EVQPGERAAVVAI 325
Cdd:cd00830  293 ieegKLKKGDLVLLLGF 309
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
7-324 4.63e-41

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 145.99  E-value: 4.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   7 VLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFGinlATGEQThslADMATSAARQALSRADIDPSEIGFLVL 86
Cdd:PRK09352   6 ILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIA---APDETT---SDLATEAAKKALEAAGIDPEDIDLIIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  87 GTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL---TEERplGLVIGADACYKHL-PLDRESSsa 162
Cdd:PRK09352  80 ATTTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIrsgAYKN--VLVIGAEKLSRIVdWTDRSTC-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 163 mppselvnfVLFGDGAGAAVLALDDTDaqlGITALVNRFSGLGRD----PGQQIEWfGLADRHLEQPGlNEDYKaieHWV 238
Cdd:PRK09352 156 ---------VLFGDGAGAVVLGASEEP---GILSTHLGSDGSYGDllylPGGGSRG-PASPGYLRMEG-REVFK---FAV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 239 PLLSKdVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNA-LPfLQIDALSRE--VQ 315
Cdd:PRK09352 219 RELAK-VAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGL-PMEKVVVTVDKYGNTSAAsIP-LALDEAVRDgrIK 295


                 ....*....
gi 491222589 316 PGERAAVVA 324
Cdd:PRK09352 296 RGDLVLLEG 304
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
 3-325 1.73e-38

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: 139.06  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589    3 RTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginlATGEQTHSlaDMATSAARQALSRADIDPSEIG 82
Cdd:TIGR00747   1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRI----AADDETSS--TMGFEAAKRAIENAGISKDDID 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   83 FLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTEerplG-----LVIGADacykhlpldr 157
Cdd:TIGR00747  75 LIIVATTTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIES----GkyktvLVVGAE---------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  158 ESSSAMPPSELVNFVLFGDGAGAAVLALDDTDAQLGITALV--NRFSGLGRDPGQQIEWFGlADRHLEQPGlNEDYKaie 235
Cdd:TIGR00747 141 KLSSTLDWTDRGTCVLFGDGAGAVVLGESEDPGGIISTHLGadGTQGEALYLPAGGRPTSG-PSPFITMEG-NEVFK--- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  236 HWVPLLSKDVlTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNALPFLQIDALSRE-- 313
Cdd:TIGR00747 216 HAVRKMGDVV-EETLEANGLDPEDIDWFVPHQANLRIIEALAKRLEL-DMSQVVKTVHKYGNTSAASIPLALDELLRTgr 293

                         330
                  ....*....|..
gi 491222589  314 VQPGERAAVVAI 325
Cdd:TIGR00747 294 IKPGDLLLLVAF 305
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
 114-183 1.26e-07

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: 48.67  E-value: 1.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491222589  114 FQLQSGCSGAVAAFDVGSHLLTEERP-LGLVIGADACYKHL-PLDRESSsamppselvnfVLFGDGAGAAVL 183
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAkNVLVIGAETLSKILdWTDRSTA-----------VLFGDGAGAVVL 61
 
Name Accession Description Interval E-value
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 3-325 1.16e-55

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: 184.16  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   3 RTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginLATGEQThslADMATSAARQALSRADIDPSEIG 82
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRI---AAPDETT---SDLAVEAARKALEAAGIDPEDID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  83 FLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL-TEERPLGLVIGADACYKHL-PLDRESS 160
Cdd:COG0332   75 LIIVATVTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIrSGQAKNVLVVGAETLSRIVdWTDRSTC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 161 samppselvnfVLFGDGAGAAVLALDDTDAQL----------GITALVNRFSGLGRDPGQQIEWfglaDRHLEQPGlNED 230
Cdd:COG0332  155 -----------VLFGDGAGAVVLEASEEGPGIlgsvlgsdgsGADLLVVPAGGSRNPPSPVDEG----DHYLRMDG-REV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 231 YK-AIEHWVpllskDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASNsREISVVADTGNNGNALPFLQIDA 309
Cdd:COG0332  219 FKfAVRNLP-----EVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEE-KVVVNIDRYGNTSAASIPLALDE 292

                        330
                 ....*....|....*...
gi 491222589 310 LSRE--VQPGERAAVVAI 325
Cdd:COG0332  293 ALREgrIKPGDLVLLAGF 310
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 7-325 2.20e-53

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: 178.12  E-value: 2.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   7 VLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginLATGEQThslADMATSAARQALSRADIDPSEIGFLVL 86
Cdd:cd00830    4 ILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRI---ADPGETT---SDLAVEAAKKALEDAGIDADDIDLIIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  87 GTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTeerpLG-----LVIGADACYKHL-PLDRESS 160
Cdd:cd00830   78 ATSTPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIR----SGgaknvLVVGAETLSRILdWTDRSTA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 161 samppselvnfVLFGDGAGAAVLALDDTDAQLGITALVNRFSGL------GRDPGQQIEWFGLADRHLEQPGlNEDYKai 234
Cdd:cd00830  154 -----------VLFGDGAGAVVLEATEEDPGILDSVLGSDGSGAdlltipAGGSRSPFEDAEGGDPYLVMDG-REVFK-- 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 235 ehWVPLLSKDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASNsREISVVADTGNNGNA-LPFlqidALSR- 312
Cdd:cd00830  220 --FAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEE-KVVVNLDRYGNTSAAsIPL----ALDEa 292

                        330
                 ....*....|....*..
gi 491222589 313 ----EVQPGERAAVVAI 325
Cdd:cd00830  293 ieegKLKKGDLVLLLGF 309
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
7-324 4.63e-41

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 145.99  E-value: 4.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   7 VLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFGinlATGEQThslADMATSAARQALSRADIDPSEIGFLVL 86
Cdd:PRK09352   6 ILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIA---APDETT---SDLATEAAKKALEAAGIDPEDIDLIIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  87 GTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL---TEERplGLVIGADACYKHL-PLDRESSsa 162
Cdd:PRK09352  80 ATTTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIrsgAYKN--VLVIGAEKLSRIVdWTDRSTC-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 163 mppselvnfVLFGDGAGAAVLALDDTDaqlGITALVNRFSGLGRD----PGQQIEWfGLADRHLEQPGlNEDYKaieHWV 238
Cdd:PRK09352 156 ---------VLFGDGAGAVVLGASEEP---GILSTHLGSDGSYGDllylPGGGSRG-PASPGYLRMEG-REVFK---FAV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 239 PLLSKdVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNA-LPfLQIDALSRE--VQ 315
Cdd:PRK09352 219 RELAK-VAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGL-PMEKVVVTVDKYGNTSAAsIP-LALDEAVRDgrIK 295


                 ....*....
gi 491222589 316 PGERAAVVA 324
Cdd:PRK09352 296 RGDLVLLEG 304
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
 3-325 1.73e-38

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: 139.06  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589    3 RTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginlATGEQTHSlaDMATSAARQALSRADIDPSEIG 82
Cdd:TIGR00747   1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRI----AADDETSS--TMGFEAAKRAIENAGISKDDID 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   83 FLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTEerplG-----LVIGADacykhlpldr 157
Cdd:TIGR00747  75 LIIVATTTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIES----GkyktvLVVGAE---------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  158 ESSSAMPPSELVNFVLFGDGAGAAVLALDDTDAQLGITALV--NRFSGLGRDPGQQIEWFGlADRHLEQPGlNEDYKaie 235
Cdd:TIGR00747 141 KLSSTLDWTDRGTCVLFGDGAGAVVLGESEDPGGIISTHLGadGTQGEALYLPAGGRPTSG-PSPFITMEG-NEVFK--- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  236 HWVPLLSKDVlTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNALPFLQIDALSRE-- 313
Cdd:TIGR00747 216 HAVRKMGDVV-EETLEANGLDPEDIDWFVPHQANLRIIEALAKRLEL-DMSQVVKTVHKYGNTSAASIPLALDELLRTgr 293

                         330
                  ....*....|..
gi 491222589  314 VQPGERAAVVAI 325
Cdd:TIGR00747 294 IKPGDLLLLVAF 305
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 11-324 1.64e-37

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 136.53  E-value: 1.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  11 GTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginLATGEQThslADMATSAARQALSRADIDPSEIGFLVLGTAT 90
Cdd:PRK12879  11 GTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRI---AHVEEYT---SDLAIKAAERALARAGLDAEDIDLIIVATTT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  91 PDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTEerplG-----LVIGADACYKHLPL-DRESSsamp 164
Cdd:PRK12879  85 PDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITS----GlykkvLVIGAERLSKVTDYtDRTTC---- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 165 pselvnfVLFGDGAGAAVlaLDDTDAQLGITALVNRFSGLGRD------PGQQIEWFGLADRH-LEQPGlNEDYKAIEHW 237
Cdd:PRK12879 157 -------ILFGDGAGAVV--LEATENEPGFIDYVLGTDGDGGDilyrtgLGTTMDRDALSGDGyIVQNG-REVFKWAVRT 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 238 VPllskDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNA-LPFLQIDALSR-EVQ 315
Cdd:PRK12879 227 MP----KGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGI-PMEKTLVSVEYYGNTSAAtIPLALDLALEQgKIK 301


                 ....*....
gi 491222589 316 PGERAAVVA 324
Cdd:PRK12879 302 PGDTLLLYG 310
PRK05963 PRK05963
beta-ketoacyl-ACP synthase III;
2-319 8.87e-30

beta-ketoacyl-ACP synthase III;


Pssm-ID: 180328 [Multi-domain]  Cd Length: 326  Bit Score: 115.97  E-value: 8.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   2 SRTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginlATGEQThsLADMATSAARQALSRADIDPSEI 81
Cdd:PRK05963   1 VCSSRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRW----AAPDET--LSDLAASAGDMALSDAGIERSDI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  82 GFLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTEERPLGLVIGADAcykhlpLDRESSs 161
Cdd:PRK05963  75 ALTLLATSTPDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQGKPVLVVAANI------LSRRIN- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 162 ampPSELVNFVLFGDGAGAAVLA--LDDTDAQLGiTALVNRFSGLGRdpgQQIEWFGLADRHLEQPGLNEDYKAIEHWVP 239
Cdd:PRK05963 148 ---MAERASAVLFADAAGAVVLApsAKANSGVLG-SQLISDGSHYDL---IKIPAGGSARPFAPERDASEFLMTMQDGRA 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 240 LLSKDV------LTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASnSREISVVADTGNNGNA-LPF-LQIDALS 311
Cdd:PRK05963 221 VFTEAVrmmsgaSQNVLASAAMTPQDIDRFFPHQANARIVDKVCETIGIPR-AKAASTLETYGNSSAAtIPLsLSLANLE 299


                 ....*...
gi 491222589 312 REVQPGER 319
Cdd:PRK05963 300 QPLREGER 307
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 6-324 7.54e-28

"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: 110.60  E-value: 7.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   6 YVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRtrHFGINlatgeqTHSLADMATSAARQALSRADIDPSEIGFLV 85
Cdd:cd00827    3 GIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQR--HMAGD------DEDVPTMAVEAARRALERAGIDPDDIGLLI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  86 LGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTEERP-LGLVIGADACYkhlPLDRESSSAMP 164
Cdd:cd00827   75 VATESPIDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWrYALVVASDIAS---YLLDEGSALEP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 165 pselvnfvLFGDGAGAAVLALDDTDAQLGITALVNRFSGLGR-------DPGQQIEWFGLADRHLEQPGLnedYKAIEHW 237
Cdd:cd00827  152 --------TLGDGAAAMLVSRNPGILAAGIVSTHSTSDPGYDfspypvmDGGYPKPCKLAYAIRLTAEPA---GRAVFEA 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 238 VPLLSKDVLTDLLATAGLQrEDLDYLLPPQLSGKMTQRVVKQMEIASNSR----EISVVADTGNNGNALPFLQIDAL--S 311
Cdd:cd00827  221 AHKLIAKVVRKALDRAGLS-EDIDYFVPHQPNGKKILEAVAKKLGGPPEKasqtRWILLRRVGNMYAASILLGLASLleS 299

                        330
                 ....*....|...
gi 491222589 312 REVQPGERAAVVA 324
Cdd:cd00827  300 GKLKAGDRVLLFS 312
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
 6-318 1.61e-25

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


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 104.64  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   6 YVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginlaTGEQThSLADMATSAARQALSRADIDPSEIGFLV 85
Cdd:CHL00203   4 HILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHL-----APSST-SLTKLAAEAANKALDKAHMDPLEIDLII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  86 LGTATPDHLMPTSANLVADaLGLEGIPTFQLQSGCSGAVAAFDVGSHLLTeerpLG-----LVIGADACYKHLPLDRESS 160
Cdd:CHL00203  78 LATSTPDDLFGSASQLQAE-IGATRAVAFDITAACSGFILALVTATQFIQ----NGsykniLVVGADTLSKWIDWSDRKT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 161 SamppselvnfVLFGDGAGAAVLALDDTDAQLGIT----ALVNRFSGLGRDP--GQQIEWFGLADRHLEQPGLN--EDYK 232
Cdd:CHL00203 153 C----------ILFGDGAGAAIIGASYENSILGFKlctdGKLNSHLQLMNKPvnNQSFGTTKLPQGQYQSISMNgkEVYK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 233 AIEHWVPLLSKDVLTDLlataGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNALPFLQIDAL-- 310
Cdd:CHL00203 223 FAVFQVPAVIIKCLNAL----NISIDEVDWFILHQANKRILEAIANRLSV-PNSKMITNLEKYGNTSAASIPLALDEAiq 297


                 ....*...
gi 491222589 311 SREVQPGE 318
Cdd:CHL00203 298 NNKIQPGQ 305
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
 11-321 5.78e-20

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


Pssm-ID: 215185  Cd Length: 379  Bit Score: 89.80  E-value: 5.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  11 GTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHfginLATGEQThsLADMATSAARQALSRADIDPSEIGFLVLGTAT 90
Cdd:PLN02326  54 GSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRR----VLSGDET--LTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  91 PDHLMpTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLteeRPLG----LVIGADACYKHLPL-DRESSsampp 165
Cdd:PLN02326 128 PDDLF-GSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFI---RGGGyknvLVIGADALSRYVDWtDRGTC----- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 166 selvnfVLFGDGAGAAVL--ALDDTDAQLGITA---------LVNRFSGLGRD----PGQQIEWFGLADRHLEQPGLN-- 228
Cdd:PLN02326 199 ------ILFGDGAGAVVLqaCDDDEDGLLGFDMhsdgnghkhLHATFKGEDDDssggNTNGVGDFPPKKASYSCIQMNgk 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 229 EDYKAIEHWVPllskDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIASNsREISVVADTGNNGNALPFLQID 308
Cdd:PLN02326 273 EVFKFAVRCVP----QVIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPE-KVISNLANYGNTSAASIPLALD 347

                        330
                 ....*....|....*
gi 491222589 309 ALSRE--VQPGERAA 321
Cdd:PLN02326 348 EAVRSgkVKKGDVIA 362
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
1-338 7.28e-20

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 88.74  E-value: 7.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   1 MSRTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginlATGEQThslADMATSAARQALSRADIDPSE 80
Cdd:PRK07204   1 MKRYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHF----VDGETS---SYMGAEAAKKAVEDAKLTLDD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  81 IGFLVLGTATPDHLMPTSANLVADALGLE--GIPTFQLQSGCSGAVAAFDVGSHLLTEER-PLGLVIGADAcykhlpldr 157
Cdd:PRK07204  74 IDCIICASGTIQQAIPCTASLIQEQLGLQhsGIPCFDINSTCLSFITALDTISYAIECGRyKRVLIISSEI--------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 158 eSSSAMPPSELVNFVLFGDGAGAAVLALDDTDAQLgITALVNRFSgLG------RDPGQQIEWFGLADRHLEQPGLNEDY 231
Cdd:PRK07204 145 -SSVGLNWGQNESCILFGDGAAAVVITKGDHSSRI-LASHMETYS-SGahlseiRGGGTMIHPREYSEERKEDFLFDMNG 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 232 KAIEHWVPLLSKDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNA-LPFLQIDAL 310
Cdd:PRK07204 222 RAIFKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGV-DEERFVTIFEDHGNMIAAsIPVALFEAI 300

                        330       340
                 ....*....|....*....|....*....
gi 491222589 311 -SREVQPGERAAVVAIeSSKWIEGGMVLE 338
Cdd:PRK07204 301 kQKKVQRGNKILLLGT-SAGLSIGGILLE 328
PRK06816 PRK06816
StlD/DarB family beta-ketosynthase;
6-340 7.38e-20

StlD/DarB family beta-ketosynthase;


Pssm-ID: 235866  Cd Length: 378  Bit Score: 89.20  E-value: 7.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   6 YVLSTGTALPGPAIDNRSLCE---RIGAQPEWIDTFV----GTRTRHFGINlATGEQTHSLADMATSAARQALSRADIDP 78
Cdd:PRK06816   4 YITSTGAFLPGEPVSNDEMEAylgLINGKPSRARRIIlrnnGIKTRHYALD-PEGRPTHSNAQMAAEAIRDLLDDAGFSL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  79 SEIGFLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGS-HLLTEERPLGLVIGAD---------- 147
Cdd:PRK06816  83 GDIELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYlSVKAGESRNAVATASElasrwfrasr 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 148 --ACYKHLPLDRESSSAMPPSELVNFVLfGDGAGAAVLA-----------LDDTDaqlgITALVNRF-----SGLGRDPG 209
Cdd:PRK06816 163 feAEEEKLAELEENPEIAFEKDFLRWML-SDGAGAVLLEnkprpdglslrIDWID----LRSYAGELpvcmyAGAEKNED 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 210 QQIE-W--FGLADRHlEQPGLN--EDYKAIEHWVPLLSKDVLTDLLATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIA- 283
Cdd:PRK06816 238 GSLKgWsdYPPEEAE-AASALSlkQDVRLLNENIVVYTIKPLLELVDKRNLDPDDIDYFLPHYSSEYFREKIVELLAKAg 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491222589 284 ---SNSREISVVADTGNNGNALPFLQIDAL--SREVQPGERAAVVAIESSKWIEGGMVLEGV 340
Cdd:PRK06816 317 fmiPEEKWFTNLATVGNTGSASIYIMLDELlnSGRLKPGQKILCFVPESGRFSTAFMLLTVV 378
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 46-147 1.26e-12

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: 67.90  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  46 FGINLATGEQthSLAD-------MATSAARQALSRADIDPSEIGFLVLGTAT-PDHLMPTSAnLVADALGL-EGIPTFQL 116
Cdd:COG3425   33 YTKGLGQEEK--SVPPpdedavtMAANAARRALDRAGIDPSDIGAVYVGTESgPDASKPIAT-YVHGALGLpPNCRAFEL 109

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491222589 117 QSGCSGAVAAF-DVGSHLLTEERPLGLVIGAD 147
Cdd:COG3425  110 KFACYAGTAALqAALGWVASGPNKKALVIASD 141
BH0617 COG3424
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ...
 4-192 1.52e-11

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


Pssm-ID: 442650 [Multi-domain]  Cd Length: 351  Bit Score: 64.39  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   4 TTYVLSTGTALPGPAIDNRSLCERIGAQP----EWIDTF------VGTRTRHFGINLATGEQTHSLA-----------DM 62
Cdd:COG3424    1 SARILSIATAVPPHRYTQEEIAEFAAELFgldeRDRRRLrrlfenSGIETRHSVLPLEWYLEPPSFGernalyieealEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  63 ATSAARQALSRADIDPSEIGFLVL----GTATP--DHLmptsanlVADALGLEG----IPTFQLqsGCSGAVAAFDVGSH 132
Cdd:COG3424   81 AEEAARRALDKAGLDPEDIDHLVTvsctGFAAPglDAR-------LINRLGLRPdvrrLPVGGM--GCAAGAAGLRRAAD 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491222589 133 LLTEE-RPLGLVIGADACYKHLPLDRESssampPSELVNFVLFGDGAGAAVLALDDTDAQL 192
Cdd:COG3424  152 FLRADpDAVVLVVCVELCSLTFQRDDDS-----KDNLVANALFGDGAAAVVVSGDPRPGPG 207
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
1-198 7.61e-11

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 62.33  E-value: 7.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589   1 MSRTTYVLSTGTALPGPAIDNRSLCERIGAQPEWIDTFVGTRTRHFginlaTGEQTHSlADMATSAARQALSRADIDPSE 80
Cdd:PRK06840   1 MEMNVGIVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPV-----PGPEDHT-SDMAIAAAKPALKQAGVDPAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  81 IGFLV-LGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLLTEERPLGLVIGADACykhlpldREs 159
Cdd:PRK06840  75 IDVVIyIGSEHKDYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLYSDPSIENVLLVGGY-------RN- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491222589 160 ssamppSELVN-------FVL-FGDGAGAAVLALDDTDAQLGITALV 198
Cdd:PRK06840 147 ------SDLVDydnprtrFMFnFAAGGSAALLKKDAGKNRILGSAII 187
PRK04262 PRK04262
hypothetical protein; Provisional
 60-324 1.42e-09

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 58.76  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  60 ADMATSAARQALSRADIDPSEIGFLVLGTATPDHLMPTSANLVADALGLegipTFQLQS-----GCSGAVAAFD-----V 129
Cdd:PRK04262  52 ATIAVEAARNALKRAGIDPKEIGAVYVGSESHPYAVKPTATIVAEALGA----TPDLTAadlefACKAGTAALQaamglV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 130 GSHLLTeerpLGLVIGADAcykhlpldreSSSAmpPSELVNFVLfGDGAGAAVLALDDTDAQL-GITALV---------- 198
Cdd:PRK04262 128 KSGMIK----YALAIGADT----------AQGA--PGDALEYTA-AAGGAAFIIGKEEVIAEIeATYSYTtdtpdfwrre 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 199 --------NRFSGlgrDPGQQiewfgladRHLeqpglnedYKAIehwvpllskdvlTDLLATAGLQREDLDYLLPPQLSG 270
Cdd:PRK04262 191 gepyprhgGRFTG---EPAYF--------KHI--------ISAA------------KGLMEKLGLKPSDYDYAVFHQPNG 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491222589 271 KMTQRVVKQMEIASNSREIS-VVADTGNNGNALPFLQIDALSREVQPGERAAVVA 324
Cdd:PRK04262 240 KFPLRVAKMLGFTKEQVKPGlLTPYIGNTYSGSALLGLAAVLDVAKPGDRILVVS 294
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 58-185 2.82e-09

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: 57.66  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  58 SLADMATSAARQALSRADIDPSEIGFLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL-TE 136
Cdd:cd00829   15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAIaSG 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491222589 137 ERPLGLVIGADAcYKHLPLDRESSSAMPPSELVNFVLFGDGAGAAVLAL 185
Cdd:cd00829   95 LADVVLVVGAEK-MSDVPTGDEAGGRASDLEWEGPEPPGGLTPPALYAL 142
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 61-190 3.48e-08

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


Pssm-ID: 238427 [Multi-domain]  Cd Length: 361  Bit Score: 54.54  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  61 DMATSAARQALSRADIDPSEIGFLVLGTATpDHLMPTSANLVADALGL-EGIPTFQL-QSGCSGAVAAFDVGSHLLtEER 138
Cdd:cd00831   87 ELAEEAARGALDEAGLRPSDIDHLVVNTST-GNPTPSLDAMLINRLGLrPDVKRYNLgGMGCSAGAIALDLAKDLL-EAN 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491222589 139 P--LGLVIGAdacykhlpldrESSSAM--PPSELVNFV---LFGDGAGAAVLALDDTDA 190
Cdd:cd00831  165 PgaRVLVVST-----------ELCSLWyrGPDHRSMLVgnaLFGDGAAAVLLSNDPRDR 212
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
 114-183 1.26e-07

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: 48.67  E-value: 1.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491222589  114 FQLQSGCSGAVAAFDVGSHLLTEERP-LGLVIGADACYKHL-PLDRESSsamppselvnfVLFGDGAGAAVL 183
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAkNVLVIGAETLSKILdWTDRSTA-----------VLFGDGAGAVVL 61
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 54-129 3.86e-07

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


Pssm-ID: 181732  Cd Length: 338  Bit Score: 51.03  E-value: 3.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491222589  54 EQTHSLADMATSAARQALSRADIDPSEIGFLVLGTATPDHLMPTSANLVADALGLegiptfqlqsgcSGAVAAFDV 129
Cdd:PRK09258  56 PEGTQLSDGAIAAGRKALAEAGIDPSDIGLLINTSVCRDYLEPATACRVHHNLGL------------PKSCANFDV 119
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
 250-325 6.05e-06

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: 44.03  E-value: 6.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491222589  250 LATAGLQREDLDYLLPPQLSGKMTQRVVKQMEIaSNSREISVVADTGNNGNALPFLQIDALSRE--VQPGERAAVVAI 325
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGL-PPEKVVVNLDEYGNTSAASIPLALDEAVEEgkLKPGDLVLLVGF 77
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 59-202 4.15e-05

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 44.87  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  59 LADMATSAARQALSRADIDPSEIGFLVLGTATPDHLMPTSANLVADALGLEGIpTFQLQSGCSGA----VAAFDV---GS 131
Cdd:PRK07515  95 QAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGF-AFDMNVACSSAtfgiQTAANAirsGS 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491222589 132 HllteeRPLgLVIGADACYKHLPL-DRESssamppselvNFVlFGDGAGAAVLALDDTDAQLGI-----TALVNRFS 202
Cdd:PRK07515 174 A-----RRV-LVVNPEICSGHLNFrDRDS----------HFI-FGDVATAVIVERADTATSAGGfeilgTRLFTQFS 233
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 63-184 4.73e-05

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: 44.36  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  63 ATSAARQALSRADIDPSEIGFLVLGTATPDHLMPTSANLVADALGLEGIPTFQLQSGCSGAVAAFDVGSHLL-TEERPLG 141
Cdd:cd00327   11 GFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVqNGKADIV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491222589 142 LVIGADACykhlpldresssamppselvnfvLFGDGAGAAVLA 184
Cdd:cd00327   91 LAGGSEEF-----------------------VFGDGAAAAVVE 110
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 62-326 1.70e-04

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: 43.01  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  62 MATSAARQALSRADIDP----SEIGFLVLGTATPDHL---------------------MPTSANLVADALGLEGiPTFQL 116
Cdd:cd00825   14 LGFEAAERAIADAGLSReyqkNPIVGVVVGTGGGSPRfqvfgadamravgpyvvtkamFPGASGQIATPLGIHG-PAYDV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 117 QSGCSGAVAAFDVGSHLL-TEERPLGLVIGADA--------CYKHLPLDRESSSAMPPSELVNFVLFGDGAGAAVLA-LD 186
Cdd:cd00825   93 SAACAGSLHALSLAADAVqNGKQDIVLAGGSEElaapmdceFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEeLE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589 187 DTDAQLGITALVNRFSGLGRDPgqqiewfglADRHLEQPGLNEDYKAIEhwvpllskdvltDLLATAGLQREDLDYLLPP 266
Cdd:cd00825  173 HALARGAHIYAEIVGTAATIDG---------AGMGAFAPSAEGLARAAK------------EALAVAGLTVWDIDYLVAH 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491222589 267 QLSGKMTQRVVKQM---EIASNSREISVV-ADTGNNGNALPFLQIDALSREVQPGERAAVVAIE 326
Cdd:cd00825  232 GTGTPIGDVKELKLlrsEFGDKSPAVSATkAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIE 295
PRK12880 PRK12880
beta-ketoacyl-ACP synthase III;
54-187 2.55e-04

beta-ketoacyl-ACP synthase III;


Pssm-ID: 171793  Cd Length: 353  Bit Score: 42.26  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491222589  54 EQTHSLADMATSAARQALSRADIDPSEIGFLVLGTATPDHLMPTSANLVADALGLE-GIPTFQLQSGCSGAVAAFDVGSH 132
Cdd:PRK12880  55 DENTCVSDLGKHAANTLLQGLNIDKNSLDALIVVTQSPDFFMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHS 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491222589 133 LLTEERPLGLVIGADACykhlpldresSSAMPPSELVNFVLFGDGAGAAVLALDD 187
Cdd:PRK12880 135 LIQSGLGKILLICGDTL----------SKFIHPKNMNLAPIFGDGVSATLIEKTD 179
 
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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