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Conserved domains on  [gi|15830727|ref|NP_309500|]
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3-oxoacyl-[acyl-carrier-protein] synthase II [Escherichia coli O157:H7 str. Sakai]

Protein Classification

beta-ketoacyl-ACP synthase II( domain architecture ID 11482679)

beta-ketoacyl-[acyl-carrier-protein] synthase II catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP, part of the dissociated (or type II) fatty acid biosynthesis system

CATH:  3.40.47.10
EC:  2.3.1.179
Gene Symbol:  fabF
Gene Ontology:  GO:0004315|GO:0006633
PubMed:  11152607|11969206
SCOP:  4000245

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-413 0e+00

beta-ketoacyl-ACP synthase II;


:

Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 731.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    3 KRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   83 VQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIAT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  163 ACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  243 EYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTI 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  323 FGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCNSFGFG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARE-RKIDYALSNSFGFG 399
                        410
                 ....*....|.
gi 15830727  403 GTNGSLIFKKI 413
Cdd:PRK07314 400 GTNASLVFKRY 410
 
Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-413 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 731.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    3 KRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   83 VQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIAT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  163 ACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  243 EYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTI 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  323 FGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCNSFGFG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARE-RKIDYALSNSFGFG 399
                        410
                 ....*....|.
gi 15830727  403 GTNGSLIFKKI 413
Cdd:PRK07314 400 GTNASLVFKRY 410
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-411 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 679.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727     4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   324 GEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399

                  ....*...
gi 15830727   404 TNGSLIFK 411
Cdd:TIGR03150 400 TNASLVFK 407
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-413 0e+00

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 636.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 324 GEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399
                       410
                ....*....|
gi 15830727 404 TNGSLIFKKI 413
Cdd:COG0304 400 HNASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-410 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 596.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 324 GEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNSFGFGG 399

                ....*..
gi 15830727 404 TNGSLIF 410
Cdd:cd00834 400 HNASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-247 5.15e-61

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 197.86  E-value: 5.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727     4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY-----------ATKFAGLVKDFNCEDI---ISRKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLffgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    68 QRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLgliEENHTSLMNGGPRKISPFFVPsTIVNMVAGHL 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVG-TMPSVIAGRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   148 TIMYGLRGPSISIATACTSGvHNIGHAA-RIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTrnDNPQAASRPWDke 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSS-LVAIHAAvQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231
                         250       260
                  ....*....|....*....|.
gi 15830727   227 rDGFVLGDGAGMLVLEEYEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
157-409 2.69e-23

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 98.94  E-value: 2.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    157 SISIATACTSG---VHnigHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKERDGFVLG 233
Cdd:smart00825  90 SVTVDTACSSSlvaLH---LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRG 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    234 DGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAyhmtsppengagaalamanalRDAGIeasqigyvnahgtSTPAGdk 313
Cdd:smart00825 162 EGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDG---------------------RSNGI-------------TAPSG-- 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    314 aEAQavktifgeaasrVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLD----FVPHEARQVS 389
Cdd:smart00825 206 -PAQ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWP 272
                          250       260
                   ....*....|....*....|...
gi 15830727    390 GMEYTLC---NSFGFGGTNGSLI 409
Cdd:smart00825 273 PPGRPRRagvSSFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-413 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 731.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    3 KRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   83 VQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIAT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  163 ACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  243 EYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTI 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  323 FGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCNSFGFG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARE-RKIDYALSNSFGFG 399
                        410
                 ....*....|.
gi 15830727  403 GTNGSLIFKKI 413
Cdd:PRK07314 400 GTNASLVFKRY 410
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-411 0e+00

beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 274452 [Multi-domain]  Cd Length: 407  Bit Score: 679.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727     4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   324 GEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399

                  ....*...
gi 15830727   404 TNGSLIFK 411
Cdd:TIGR03150 400 TNASLVFK 407
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1-413 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 652.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIV 80
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   81 AGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISI 160
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  161 ATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLV 240
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  241 LEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVK 320
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  321 TIFGEAASR-VLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSF 399
Cdd:PRK08722 321 RALGEAGSKqVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAICNSF 400
                        410
                 ....*....|....
gi 15830727  400 GFGGTNGSLIFKKI 413
Cdd:PRK08722 401 GFGGTNGSLIFKKM 414
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-413 0e+00

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 636.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 324 GEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399
                       410
                ....*....|
gi 15830727 404 TNGSLIFKKI 413
Cdd:COG0304 400 HNASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-410 0e+00

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 596.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 324 GEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNSFGFGG 399

                ....*..
gi 15830727 404 TNGSLIF 410
Cdd:cd00834 400 HNASLVF 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-412 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 510.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKD--------FNCEDIISRKEQRKMD 72
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   73 AFIQYGIVAGVQAMQDSGLEI-TEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMY 151
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWDPdTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  152 GLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWDKERDGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  231 VLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPA 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  311 GDKAEAQAVKTIFGEAASrVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCD-LDFVPHEARQVS 389
Cdd:PRK06333 321 GDLGEVAAIKKVFGHVSG-LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
                        410       420
                 ....*....|....*....|...
gi 15830727  390 gMEYTLCNSFGFGGTNGSLIFKK 412
Cdd:PRK06333 400 -MDYALSNGFGFGGVNASILFRR 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
4-413 2.31e-169

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 480.00  E-value: 2.31e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA 163
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  164 CTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  244 YEHAKKRGAKIYAELVGFGMSSDAYHMTSP-PENGAGAALAMANALrdagiEASQIGYVNAHGTSTPAGDKAEAQAVKTI 322
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPaPEGPLRAMKAALEMA-----GNPKIDYINAHGTSTPYNDKNETAALKEL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  323 FGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFG 402
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAE-LNVVMSNSFGFG 395
                        410
                 ....*....|.
gi 15830727  403 GTNGSLIFKKI 413
Cdd:PRK08439 396 GTNGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
13-413 8.51e-148

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 426.03  E-value: 8.51e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   13 MLSPVGNTVESTWKALLAGQSGISLIDHFDT----------------SAYATKFAGLVK--DFNCEDIISRKeqrKMDAF 74
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDqsEFDPSDFAPTK---RESRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   75 IQYGIVAGVQAMQDSGLEITEE-NATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGL 153
Cdd:PTZ00050  78 THFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  154 RGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWDKERDGFVL 232
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  233 GDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSP-PENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAG 311
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPhPDGRGARRCMENALKDGANININDVDYVNAHATSTPIG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  312 DKAEAQAVKTIFGE-AASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQ-VS 389
Cdd:PTZ00050 318 DKIELKAIKKVFGDsGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHpLQ 397
                        410       420
                 ....*....|....*....|....
gi 15830727  390 GMEYTLCNSFGFGGTNGSLIFKKI 413
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4-410 3.52e-137

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 399.55  E-value: 3.52e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI-------DHFDTSAYA-------TKFAGLVKDFNCEDIISRK--- 66
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtqddlkmKSEDEETQLytldqlpSRVAALVPRGTGPGDFDEElwl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   67 EQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGP-RKISPFFVPSTIVNMVAG 145
Cdd:PLN02836  86 NSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRlRRLSPFFVPRILINMAAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  146 HLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWD 224
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  225 KERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAH 304
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  305 GTSTPAGDKAEAQAVKTIFGE--AASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVP 382
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEhaTSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
                        410       420
                 ....*....|....*....|....*...
gi 15830727  383 HEARQVSGMEYTLCNSFGFGGTNGSLIF 410
Cdd:PLN02836 406 LTASKAMLIRAALSNSFGFGGTNASLLF 433
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
1-410 7.15e-119

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 356.60  E-value: 7.15e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIV 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   81 AGVQAMQDSGleITEE-----NATRIGAAIGSGIGGLGLIEENHTSLmNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRG 155
Cdd:PLN02787 206 AGKKALADGG--ITEDvmkelDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMG 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDG 235
Cdd:PLN02787 283 PNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEG 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  236 AGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAE 315
Cdd:PLN02787 363 AGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKE 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  316 AQAVKTIFGEaASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTL 395
Cdd:PLN02787 443 YQALMRCFGQ-NPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIKVAL 521
                        410
                 ....*....|....*
gi 15830727  396 CNSFGFGGTNGSLIF 410
Cdd:PLN02787 522 SNSFGFGGHNSSILF 536
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4-411 1.80e-106

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 320.01  E-value: 1.80e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDT-SAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRyDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   83 VQAMQDSGLeITEENAT--RIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPffvpSTIVNMV----AGHLTIMYGLRGP 156
Cdd:PRK09116  82 ELALEDAGL-LGDPILTdgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMphttAVNVGLFFGLKGR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  157 SISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAStPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGA 236
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC-PTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  237 GMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPpeNGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEA 316
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  317 QAVKTIFGEaasRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGC-DLDFVPHEARQVSgMEYTL 395
Cdd:PRK09116 314 QATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREID-TEYVM 389
                        410
                 ....*....|....*.
gi 15830727  396 CNSFGFGGTNGSLIFK 411
Cdd:PRK09116 390 SNNFAFGGINTSLIFK 405
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4-412 5.67e-100

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 303.52  E-value: 5.67e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKdFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   84 QAMQDSGLEITEENATRIG-AAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIAT 162
Cdd:PRK07967  81 QAIADAGLSEEQVSNPRTGlIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  163 ACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGgFGAARALSTR-NDNPQAASRPWDKERDGFVLGDGAGMLVL 241
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  242 EEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEasqigYVNAHGTSTPAGDKAEAQAVKT 321
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTPID-----YINTHGTSTPVGDVKELGAIRE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  322 IFGEAASRvlVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEG-CDLDFVpHEARQVSGMEYTLCNSFG 400
Cdd:PRK07967 315 VFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIV-TETTDNAELTTVMSNSFG 391
                        410
                 ....*....|..
gi 15830727  401 FGGTNGSLIFKK 412
Cdd:PRK07967 392 FGGTNATLVFRR 403
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
126-412 1.13e-96

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 292.79  E-value: 1.13e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  126 GPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGA 205
Cdd:PRK14691  53 GPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  206 ARALSTR-NDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAM 284
Cdd:PRK14691 133 ARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAM 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  285 ANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASrVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVP 364
Cdd:PRK14691 213 KIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNA-LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVP 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15830727  365 PTINLDNPDEGCD-LDFVPHEArQVSGMEYTLCNSFGFGGTNGSLIFKK 412
Cdd:PRK14691 292 ATLNLENPDPAAKgLNIIAGNA-QPHDMTYALSNGFGFAGVNASILLKR 339
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
6-412 1.05e-94

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 290.48  E-value: 1.05e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    6 VVVTGLGMLSPVGNTVESTWKALLAGQSGI-----SLIDHFDTSayaTKFAG-LVKDFncEDIISRKEQRKMDAFIQYGI 79
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEFDLP---VRIGGhLLEEF--DHQLTRVELRRMSYLQRMST 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   80 VAGVQAMQDSGleITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSIS 159
Cdd:PRK07910  89 VLGRRVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  160 IATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARA-LSTRNDNPQAASRPWDKERDGFVLGDGAGM 238
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  239 LVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQA 318
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  319 VKTIFGeaASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCNS 398
Cdd:PRK07910 327 INNALG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRP-GNYRYAINNS 403
                        410
                 ....*....|....
gi 15830727  399 FGFGGTNGSLIFKK 412
Cdd:PRK07910 404 FGFGGHNVALAFGR 417
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
6-410 1.79e-91

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 282.29  E-value: 1.79e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    6 VVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVkDFNCEDIISRKEQRKMDAFIqygivAGVQA 85
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DFLPESPFGASALSEALARL-----AAEEA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   86 MQDSGLEIT---------------EENATRIGAAIGSGIGglgliEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIM 150
Cdd:PRK06501  87 LAQAGIGKGdfpgplflaappvelEWPARFALAAAVGDND-----APSYDRLLRAARGGRFDALHERFQFGSIADRLADR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  151 YGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGF 230
Cdd:PRK06501 162 FGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  231 VLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMT-SPPENGAGAALAMANALrDAGIEASQIGYVNAHGTSTP 309
Cdd:PRK06501 242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTrSSPDGSPAIGAIRAALA-DAGLTPEQIDYINAHGTSTP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  310 AGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEAR--Q 387
Cdd:PRK06501 321 ENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARdaR 400
                        410       420
                 ....*....|....*....|...
gi 15830727  388 VSGMeytLCNSFGFGGTNGSLIF 410
Cdd:PRK06501 401 VTAV---LSNSFGFGGQNASLVL 420
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
4-408 1.59e-73

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 235.41  E-value: 1.59e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   4 RRVVVTGLGMLSPVGN---TVESTWKALLAGQSGISLIDHFdTSAYATKFAGLVKDFNCEDIISRKEqRKMDAFIQYGIV 80
Cdd:cd00828   1 SRVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARL-KSRFDRGVAGQIPTGDIPGWDAKRT-GIVDRTTLLALV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  81 AGVQAMQDSGLEI-TEENATRIGAAIGSGIGGLGLIEenHTSLMNGgpRKISPFFVPSTIV--NMVAGHLTIMYGL-RGP 156
Cdd:cd00828  79 ATEEALADAGITDpYEVHPSEVGVVVGSGMGGLRFLR--RGGKLDA--RAVNPYVSPKWMLspNTVAGWVNILLLSsHGP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 157 SISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEkASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGA 236
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 237 GMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPeNGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEA 316
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 317 QAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYT-L 395
Cdd:cd00828 313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVRAaL 392
                       410
                ....*....|...
gi 15830727 396 CNSFGFGGTNGSL 408
Cdd:cd00828 393 VNAFGFGGSNAAL 405
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5-408 3.43e-72

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 231.09  E-value: 3.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    5 RVVVTGLGMLSPVGNtVESTWKALLAGQSGISLIDHF-DTSAYATkfaGLV--KDFNCEDIIsrkEQRKMDAFIQYGIVA 81
Cdd:PRK05952   3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPFpELPPLPL---GLIgnQPSSLEDLT---KTVVTAALKDAGLTP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   82 gvqAMQDSGLEITEENATRIGAAIGSGigglglieENHTSLMNGGPRKISPFFVpSTIVNMVAGHLTIMYGLRGPSISIA 161
Cdd:PRK05952  76 ---PLTDCGVVIGSSRGCQGQWEKLAR--------QMYQGDDSPDEELDLENWL-DTLPHQAAIAAARQIGTQGPVLAPM 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  162 TACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALStrndnpQAASRPWDKERDGFVLGDGAGMLVL 241
Cdd:PRK05952 144 AACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA------KTGAYPFDRQREGLVLGEGGAILVL 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  242 EEYEHAKKRGAKIYAELVGFGMSSDAYHMTSP-PENGAGAALAMANALRdAGIEASQIGYVNAHGTSTPAGDKAEAQAVK 320
Cdd:PRK05952 218 ESAELAQKRGAKIYGQILGFGLTCDAYHMSAPePDGKSAIAAIQQCLAR-SGLTPEDIDYIHAHGTATRLNDQREANLIQ 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  321 TIFGeaaSRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDegCDLDFVpHEARQvSGMEYTLCNSFG 400
Cdd:PRK05952 297 ALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFV-RQAQQ-SPLQNVLCLSFG 369

                 ....*...
gi 15830727  401 FGGTNGSL 408
Cdd:PRK05952 370 FGGQNAAI 377
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
5-412 2.64e-65

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 214.12  E-value: 2.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    5 RVVVTGLGMLSPVGNTVESTWKALLAGQSGI------------SLIDHFDTSAYATKFAGLVKdfncEDIISRKEQRKMD 72
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgrqvpdDAGAGLASAFIGAELDSLAL----PERLDAKLLRRAS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   73 AFIQYGIVAGVQAMQDSGLEITEENatRIGAAIGSGIGGLGLIEENHTSLMNGgPRKISPFFVPSTIVNMVAGHLTIMYG 152
Cdd:PRK07103  79 LSAQAALAAAREAWRDAALGPVDPD--RIGLVVGGSNLQQREQALVHETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  153 LRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRN--DNPQAASRPWDKERDGF 230
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  231 VLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPpeNGAGAALAMANALRDAGIEASQIGYVNAHGTSTPA 310
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  311 GDKAEAQAvktIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNP-DEGCdlDFVPHEARQVS 389
Cdd:PRK07103 314 GDETELAA---LFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESAR 388
                        410       420
                 ....*....|....*....|...
gi 15830727  390 gMEYTLCNSFGFGGTNGSLIFKK 412
Cdd:PRK07103 389 -IRYALSLSFGFGGINTALVLER 410
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
4-409 1.08e-63

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 209.52  E-value: 1.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISP------FFVPSTivnmvaGHLTIMYGLRGPS 157
Cdd:cd00832  81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAyqsfawFYAVNT------GQISIRHGMRGPS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 158 ISIATACTSGVHNIGHAARIIAYGdADVMVAGGAEKASTPLGVGGFGAARALSTrNDNPQAASRPWDKERDGFVLGDGAG 237
Cdd:cd00832 155 GVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 238 MLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANalrDAGIEASQIGYVNAHGTSTPAGDKAEAQ 317
Cdd:cd00832 233 ILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPGLARAIRLALA---DAGLTPEDVDVVFADAAGVPELDRAEAA 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 318 AVKTIFGeaASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCN 397
Cdd:cd00832 310 ALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRP-AALRTALVL 386
                       410
                ....*....|..
gi 15830727 398 SFGFGGTNGSLI 409
Cdd:cd00832 387 ARGRGGFNSALV 398
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
152-410 3.53e-63

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 208.16  E-value: 3.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  152 GLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAS-TPLGvgGFGAARALSTRndnpqaASRPWDKERDGF 230
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCrLTLN--GFNSLESLSPQ------PCRPFSANRDGI 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  231 VLGDGAGMLVLEeyehakkRGAKIYAELVGFGMSSDAYHMTSP-PENGAGAALAMANAlRDAGIEASQIGYVNAHGTSTP 309
Cdd:PRK09185 220 NIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPhPEGLGAILAMQQAL-ADAGLAPADIGYINLHGTATP 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  310 AGDKAEAQAVKTIFGEaasRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvS 389
Cdd:PRK09185 292 LNDAMESRAVAAVFGD---GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQA-L 367
                        250       260
                 ....*....|....*....|.
gi 15830727  390 GMEYTLCNSFGFGGTNGSLIF 410
Cdd:PRK09185 368 AIRYVLSNSFAFGGNNCSLIF 388
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
5-409 7.01e-62

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 205.48  E-value: 7.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   5 RVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY----------ATKFAGLVKDFNCEDI----ISRKEQ 68
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpeDRWDADGYypdpgkpgktYTRRGGFLDDVDAFDAaffgISPREA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  69 RKMDA----FIQygiVAgVQAMQDSGLeiteenaTRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVA 144
Cdd:cd00833  82 EAMDPqqrlLLE---VA-WEALEDAGY-------SPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 145 GHLTIMYGLRGPSISIATACTSG---VHnigHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALStrndnPQAASR 221
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSlvaLH---LACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCR 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 222 PWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAY--HMTSPpeNGAGAALAMANALRDAGIEASQIG 299
Cdd:cd00833 223 PFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDID 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 300 YVNAHGTSTPAGDKAEAQAVKTIFGE---AASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGC 376
Cdd:cd00833 301 YVEAHGTGTPLGDPIEVEALAKVFGGsrsADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKI 380
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15830727 377 DLD----FVPHEAR---QVSGMEYTLCNSFGFGGTNGSLI 409
Cdd:cd00833 381 DFEesplRVPTEARpwpAPAGPRRAGVSSFGFGGTNAHVI 420
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-247 5.15e-61

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 197.86  E-value: 5.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727     4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY-----------ATKFAGLVKDFNCEDI---ISRKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLffgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    68 QRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLgliEENHTSLMNGGPRKISPFFVPsTIVNMVAGHL 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVG-TMPSVIAGRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   148 TIMYGLRGPSISIATACTSGvHNIGHAA-RIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTrnDNPQAASRPWDke 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSS-LVAIHAAvQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231
                         250       260
                  ....*....|....*....|.
gi 15830727   227 rDGFVLGDGAGMLVLEEYEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
77-409 3.50e-46

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: 162.03  E-value: 3.50e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  77 YGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPStivnmVAGHLTIMYGLRGP 156
Cdd:cd00825  14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLGIHGP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 157 SISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKERDGFVLGDGA 236
Cdd:cd00825  89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDGA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 237 GMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEA 316
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKEL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 317 QAVKTIFGEaaSRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEgcDLDFVPHEARQvSGMEYTLC 396
Cdd:cd00825 244 KLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTP-RELRTALL 318
                       330
                ....*....|...
gi 15830727 397 NSFGFGGTNGSLI 409
Cdd:cd00825 319 NGFGLGGTNATLV 331
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
119-405 2.84e-45

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 168.13  E-value: 2.84e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  119 HTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSG---VHnigHAARIIAYGDADVMVAGGAEKAS 195
Cdd:COG3321  129 YALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSlvaVH---LACQSLRSGECDLALAGGVNLML 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  196 TPLGVGGFGAARALStrndnPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSD--------- 266
Cdd:COG3321  206 TPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrsngltap 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  267 -----------AYhmtsppengagaalamanalRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASR---VLV 332
Cdd:COG3321  281 ngpaqaavirrAL--------------------ADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAI 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  333 SSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLD----FVPHEARQVSGMEYTLC---NSFGFGGTN 405
Cdd:COG3321  341 GSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRPWPAGGGPRRagvSSFGFGGTN 420
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
255-370 3.14e-40

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 139.24  E-value: 3.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   255 YAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASR--VLV 332
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15830727   333 SSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLD 370
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
136-412 1.17e-30

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.


Pssm-ID: 274311 [Multi-domain]  Cd Length: 2582  Bit Score: 125.12  E-value: 1.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    136 PSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDn 215
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    216 pqaaSRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEA 295
Cdd:TIGR02813  257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    296 SQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASR---VLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNP 372
Cdd:TIGR02813  333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 15830727    373 DEGCDLDFVPH----EAR----QVSGMEYTL-CNSFGFGGTNGSLIFKK 412
Cdd:TIGR02813  413 NPKLDIENSPFylntETRpwmqREDGTPRRAgISSFGFGGTNFHMVLEE 461
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
152-409 3.85e-26

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: 105.99  E-value: 3.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 152 GLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKastplgvggfgaaralstrndnpqaasrpwdkerdgFV 231
Cdd:cd00327  56 ISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 232 LGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRdAGIEASQIGYVNAHGTSTPAG 311
Cdd:cd00327 100 FGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAVSGEGLARAARKALEG-AGLTPSDIDYVEAHGTGTPIG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 312 DKAEAQAVKTIFGEAAsrVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTinldnpdegcdldfvPHEARQVsgm 391
Cdd:cd00327 179 DAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------PREPRTV--- 238
                       250
                ....*....|....*...
gi 15830727 392 eytLCNSFGFGGTNGSLI 409
Cdd:cd00327 239 ---LLLGFGLGGTNAAVV 253
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
157-409 2.69e-23

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 98.94  E-value: 2.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    157 SISIATACTSG---VHnigHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKERDGFVLG 233
Cdd:smart00825  90 SVTVDTACSSSlvaLH---LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRG 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    234 DGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAyhmtsppengagaalamanalRDAGIeasqigyvnahgtSTPAGdk 313
Cdd:smart00825 162 EGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDG---------------------RSNGI-------------TAPSG-- 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    314 aEAQavktifgeaasrVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLD----FVPHEARQVS 389
Cdd:smart00825 206 -PAQ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWP 272
                          250       260
                   ....*....|....*....|...
gi 15830727    390 GMEYTLC---NSFGFGGTNGSLI 409
Cdd:smart00825 273 PPGRPRRagvSSFGFGGTNAHVI 295
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
1-260 5.90e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 63.82  E-value: 5.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727    1 MSKRRVVVTGLGMLSPVGNTVESTWkALLAGQSGISLIDhfdtsayATKFA-----GLVK-DFNCEdIISRKEQRKMDAF 74
Cdd:PRK06519   3 MQPNDVVITGIGLVSSLGEGLDAHW-NALSAGRPQPNVD-------TETFApypvhPLPEiDWSQQ-IPKRGDQRQMETW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727   75 IQYGIVAGVQAMQDSGLEITEEnatrigaaigsgigglglieenHTSLMN------GGPRKISpffVPSTIV-------- 140
Cdd:PRK06519  74 QRLGTYAAGLALDDAGIKGNEE----------------------LLSTMDmivaagGGERDIA---VDTAILnearkrnd 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  141 -----------------------NMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTP 197
Cdd:PRK06519 129 rgvllnerlmtelrptlflaqlsNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERP 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830727  198 LGVGGFGAARALSTRNDNPQAASRPWDKerDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVG 260
Cdd:PRK06519 209 DMLLLYELGGLLLKGGWAPVWSRGGEDG--GGFILGSGGAFLVLESREHAEARGARPYARISG 269
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
156-244 4.25e-04

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 42.36  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAST-PLGVGGFGAARALSTRNDNPQAASRPWDkERDGFVLGD 234
Cdd:COG0183  80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRaPMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGE 158
                        90
                ....*....|
gi 15830727 235 GAGMLVlEEY 244
Cdd:COG0183 159 TAENVA-ERY 167
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
136-263 6.81e-04

3-oxoacyl-(acyl carrier protein) synthase; Validated


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 41.54  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  136 PSTIVNMVAGHLTimYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTrNDN 215
Cdd:PRK06147 107 EERLLRELEARLG--LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT-SQN 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15830727  216 PqaasrpwdkerDGFVLGDGAGMLVLEEYEHAKKRGAKIYAelVGFGM 263
Cdd:PRK06147 184 S-----------NGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGR 218
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
156-244 7.38e-04

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 41.31  E-value: 7.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727 156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAS-TPLGVGGfgaaRALSTRNDNPQAASRPWDKERDGFVL-- 232
Cdd:cd00751  76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSrAPYLLPK----ARRGGRLGLNTLDGMLDDGLTDPFTGls 151
                        90
                ....*....|...
gi 15830727 233 -GDGAGMLVlEEY 244
Cdd:cd00751 152 mGITAENVA-EKY 163
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
221-360 9.05e-04

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 41.23  E-value: 9.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830727  221 RPWDKERDGFV-------LGDGAGMLVLEEYEHAKKRGAKIYAELVGFGmssDAyhmTSPPEN-GAGAALAMANALRDAG 292
Cdd:PLN02644 232 RPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYA---DA---AQAPELfTTAPALAIPKALKHAG 305
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830727  293 IEASQIGY--VNahgtstpagdkaEAQAV-----KTIFGEAASRVLVSSTKSMTGHLLGAAGA--VESIYSILALRD 360
Cdd:PLN02644 306 LEASQVDYyeIN------------EAFSVvalanQKLLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKN 370
PRK05790 PRK05790
putative acyltransferase; Provisional
156-192 9.76e-04

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 40.91  E-value: 9.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15830727  156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAE 192
Cdd:PRK05790  80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
152-206 1.92e-03

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 39.94  E-value: 1.92e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15830727 152 GLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAA 206
Cdd:cd00829  65 LLGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGR 119
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
156-195 2.10e-03

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 39.94  E-value: 2.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 15830727  156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAS 195
Cdd:PRK09050  82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMS 121
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
156-199 3.86e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 39.35  E-value: 3.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 15830727  156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAS-TPLG 199
Cdd:PRK07661  82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSlVPMM 126
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
156-195 6.92e-03

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: 38.05  E-value: 6.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15830727   156 PSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKAS 195
Cdd:pfam00108  77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMS 116
 
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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