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Conserved domains on  [gi|402379267|gb|EJV13082|]
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beta-ketoacyl-acyl-carrier-protein synthase II [Enterococcus faecalis ERV41]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase II( domain architecture ID 11496422)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 2-407 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: 663.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 402379267  401 NGVICLK 407
Cdd:TIGR03150 401 NASLVFK 407
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 2-407 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: 663.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 402379267  401 NGVICLK 407
Cdd:TIGR03150 401 NASLVFK 407
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 2-409 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: 622.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA-TRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDpEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:COG0304  241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:COG0304  321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400


                 ....*....
gi 402379267 401 NGVICLKKW 409
Cdd:COG0304  401 NASLVFKRY 409
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1-410 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 615.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAA 80
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  81 LEAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVT 160
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 161 ACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLE 239
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 240 ELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRV 319
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 320 FGERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGG 399
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                        410
                 ....*....|.
gi 402379267 400 HNGVICLKKWE 410
Cdd:PRK07314 401 TNASLVFKRYE 411
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 2-406 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: 601.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA-TRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDpEKASRPFDKDRDGFVLGEGAGVLVLES 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:cd00834  241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:cd00834  321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400


                 ....*.
gi 402379267 401 NGVICL 406
Cdd:cd00834  401 NASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 2-244 6.82e-58

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: 189.77  E-value: 6.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITK-----FDSEDTGVALAGEVK----------EFDPSAV-LERKE 65
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrwdpDKLYDPPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   66 QKRMDLFSQYGLVAALEAWEMSGLTEATIDPTRLGVIVGSGiggMTTLQDQVRVMDKKGAKRVTPFFVPMvIANMAAGNI 145
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSG---IGDYAALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  146 SIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALnTTEDATRASIPFDkerK 225
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGML-SPDGPCKAFDPFA---D 232

                         250
                  ....*....|....*....
gi 402379267  226 GFVMGEGAGMLVLEELEHA 244
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 4-401 9.59e-21

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: 91.62  E-value: 9.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267     4 VVITGMGAVTPLGNTVKEFWHNLVDGKLGIGkitkfdsedtgvalagevkEFDP-----SAvlerKEQKRMD----LFsq 74
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD-------------------LFDAaffgiSP----REAEAMDpqqrLL-- 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    75 ygLVAALEAWEMSGlteatIDPTRLgvivgsgiggmttlqdqvrvmdkkgAKRVTPFFVpmvianmaaGnisirLGAKGP 154
Cdd:smart00825  56 --LEVAWEALEDAG-----IDPESL-------------------------RGSRTGVFV---------G-----VSSSDY 89

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   155 SQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNttedATRASIPFDKERKGFVMGEGAG 234
Cdd:smart00825  90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVG 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   235 MLVLEELEHAQKRGATIYGEIVGYGSNCD--ASHMTAPlkdgSGaaaamemaiaeagitpeqigyinahgtstpandaae 312
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDgrSNGITAP----SG------------------------------------ 205

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   313 ttaikrvfgerASQIPISSTKSMTGHLLGAAG--GIeaIACVQTLQEGKAHPTVGYQVADPDCDLD----YVTEGARDIT 386
Cdd:smart00825 206 -----------PAQLLIGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWP 272

                          410
                   ....*....|....*....
gi 402379267   387 ADYTIS----NSFGFGGHN 401
Cdd:smart00825 273 PPGRPRragvSSFGFGGTN 291
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
 2-407 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: 663.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400


                  ....*..
gi 402379267  401 NGVICLK 407
Cdd:TIGR03150 401 NASLVFK 407
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 2-409 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: 622.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA-TRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDpEKASRPFDKDRDGFVLGEGAGVLVLEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:COG0304  241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:COG0304  321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400


                 ....*....
gi 402379267 401 NGVICLKKW 409
Cdd:COG0304  401 NASLVFKRY 409
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1-410 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 615.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAA 80
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  81 LEAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVT 160
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 161 ACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLE 239
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 240 ELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRV 319
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 320 FGERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGG 399
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                        410
                 ....*....|.
gi 402379267 400 HNGVICLKKWE 410
Cdd:PRK07314 401 TNASLVFKRYE 411
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 2-406 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: 601.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA-TRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDpEKASRPFDKDRDGFVLGEGAGVLVLES 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:cd00834  241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 321 GERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGGH 400
Cdd:cd00834  321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400


                 ....*.
gi 402379267 401 NGVICL 406
Cdd:cd00834  401 NASLVF 406
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-411 1.82e-177

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 501.45  E-value: 1.82e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKE--------FDPSAVLERKEQKRMDLF 72
Cdd:PRK06333   3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMDRF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  73 SQYGLVAALEAWEMSGLTEATI-DPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGA 151
Cdd:PRK06333  83 ILFAMAAAKEALAQAGWDPDTLeDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 152 KGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTT--EDATRASIPFDKERKGFVM 229
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfnDAPEQASRPFDRDRDGFVM 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 230 GEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPAND 309
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 310 AAETTAIKRVFGeRASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCD-LDYVTEGARDITAD 388
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401

                        410       420
                 ....*....|....*....|...
gi 402379267 389 YTISNSFGFGGHNGVICLKKWEE 411
Cdd:PRK06333 402 YALSNGFGFGGVNASILFRRWEP 424
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 1-408 3.04e-154

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 441.86  E-value: 3.04e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAA 80
Cdd:PRK08439   1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  81 LEAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVT 160
Cdd:PRK08439  81 REAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 161 ACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLE 239
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 240 ELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAgitpEQIGYINAHGTSTPANDAAETTAIKRV 319
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAGN----PKIDYINAHGTSTPYNDKNETAALKEL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 320 FGERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFGG 399
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGG 396


                 ....*....
gi 402379267 400 HNGVICLKK 408
Cdd:PRK08439 397 TNGVVIFKK 405
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 11-408 1.73e-139

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 404.84  E-value: 1.73e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  11 AVTPLGNTVKEFWHNLVDGKLGIGKITKFD-----------SEDTGVAL-----AGEVK--EFDPSAVlerKEQKRMDLF 72
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPkflpdcipeqkALENLVAAmpcqiAAEVDqsEFDPSDF---APTKRESRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  73 SQYGLVAALEAWEMSGLTEAT-IDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGA 151
Cdd:PTZ00050  78 THFAMAAAREALADAKLDILSeKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 152 KGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTT--EDATRASIPFDKERKGFVM 229
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKynDDPQRASRPFDKDRAGFVM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 230 GEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAG-ITPEQIGYINAHGTSTPAN 308
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 309 DAAETTAIKRVFGER-ASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTE-GARDIT 386
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGkTAHPLQ 397

                        410       420
                 ....*....|....*....|...
gi 402379267 387 A-DYTISNSFGFGGHNGVICLKK 408
Cdd:PTZ00050 398 SiDAVLSTSFGFGGVNTALLFTK 420
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
2-408 2.05e-127

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 373.95  E-value: 2.05e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:PRK08722   4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:PRK08722  84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLVLEE 240
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGAGMMVLEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 241 LEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVF 320
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 321 GERAS-QIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITA-DYTISNSFGFG 398
Cdd:PRK08722 324 GEAGSkQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESmEYAICNSFGFG 403

                        410
                 ....*....|
gi 402379267 399 GHNGVICLKK 408
Cdd:PRK08722 404 GTNGSLIFKK 413
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 2-401 1.61e-114

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 341.77  E-value: 1.61e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKIT----KFDSEDTGVAL----------AGEV-KEFDPSAVLERK-- 64
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTqddlKMKSEDEETQLytldqlpsrvAALVpRGTGPGDFDEELwl 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  65 EQKRMDLFSQYGLVAALEAwemsgLTEATIDPT------RLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIA 138
Cdd:PLN02836  86 NSRSSSRFIGYALCAADEA-----LSDARWLPSedeakeRTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 139 NMAAGNISIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA--TRA 216
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNScpTEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 217 SIPFDKERKGFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIG 296
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 297 YINAHGTSTPANDAAETTAIKRVFGERASQ--IPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCD 374
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD 400

                        410       420
                 ....*....|....*....|....*...
gi 402379267 375 LDYVTEGA-RDITADYTISNSFGFGGHN 401
Cdd:PLN02836 401 DGFVPLTAsKAMLIRAALSNSFGFGGTN 428
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 2-404 7.99e-109

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 330.79  E-value: 7.99e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTE---ATIDPTRLGVIVGSGIGGMTTLQDQVRVMdKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTI 158
Cdd:PLN02787 209 KALADGGITEdvmKELDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSI 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 159 VTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT-TEDATRASIPFDKERKGFVMGEGAGMLV 237
Cdd:PLN02787 288 STACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGEGAGVLL 367

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 238 LEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIK 317
Cdd:PLN02787 368 LEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALM 447

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 318 RVFGERaSQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGAR---DITAdyTISNS 394
Cdd:PLN02787 448 RCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKerlDIKV--ALSNS 524

                        410
                 ....*....|
gi 402379267 395 FGFGGHNGVI 404
Cdd:PLN02787 525 FGFGGHNSSI 534
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
1-407 3.19e-97

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 296.13  E-value: 3.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDS-EDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVA 79
Cdd:PRK09116   1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRyDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  80 ALEAWEMSGLTEatiDPTRLGVIVGSGIGGMTTLQDQVR----VMDKKGAKRVTP-FFVPMvIANMAAGNISIRLGAKGP 154
Cdd:PRK09116  81 SELALEDAGLLG---DPILTDGRMGIAYGSSTGSTDPIGafgtMLLEGSMSGITAtTYVRM-MPHTTAVNVGLFFGLKGR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 155 SQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEAtVCEIGIAGFAALNALNTTEDATRASI-PFDKERKGFVMGEGA 233
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPrPFDANRDGLVIGEGA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 234 GMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGaaAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAET 313
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 314 TAIKRVFGERasqIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDC-DLDYVTEGARDITADYTIS 392
Cdd:PRK09116 314 QATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVMS 390

                        410
                 ....*....|....*
gi 402379267 393 NSFGFGGHNGVICLK 407
Cdd:PRK09116 391 NNFAFGGINTSLIFK 405
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
4-401 7.13e-93

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 285.76  E-value: 7.13e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   4 VVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFD---PSAVlerkeqkrmDLFSQYGLVAA 80
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPespFGAS---------ALSEALARLAA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  81 LEAWEMSGLTEATID--------------PTRLGVIVGSGIGGMTTLQDQVRVMdkkGAKRVTPFFVPMVIANMAAgNIS 146
Cdd:PRK06501  84 EEALAQAGIGKGDFPgplflaappvelewPARFALAAAVGDNDAPSYDRLLRAA---RGGRFDALHERFQFGSIAD-RLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 147 IRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA-TRASIPFDKERK 225
Cdd:PRK06501 160 DRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPpEKASKPFSKDRD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 226 GFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTST 305
Cdd:PRK06501 240 GFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTST 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 306 PANDAAETTAIKRVFGERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDI 385
Cdd:PRK06501 320 PENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDA 399

                        410
                 ....*....|....*.
gi 402379267 386 TADYTISNSFGFGGHN 401
Cdd:PRK06501 400 RVTAVLSNSFGFGGQN 415
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
4-409 2.41e-88

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 273.91  E-value: 2.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   4 VVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITK-FDSE-DTGVALAGEVKEfDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDpFVEEfDLPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEatIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTA 161
Cdd:PRK07910  93 RVWENAGSPE--VDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 162 CASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTT--EDATRASIPFDKERKGFVMGEGAGMLVLE 239
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTnnDDPAGACRPFDKDRDGFVFGEGGALMVIE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 240 ELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRV 319
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 320 FG-ERASqipISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFG 398
Cdd:PRK07910 331 LGgHRPA---VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFG 407

                        410
                 ....*....|.
gi 402379267 399 GHNGVICLKKW 409
Cdd:PRK07910 408 GHNVALAFGRY 418
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 117-409 1.67e-87

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 269.29  E-value: 1.67e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 117 VRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEI 196
Cdd:PRK14691  46 VRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 197 GIAGFAALNALNTTEDAT--RASIPFDKERKGFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDG 274
Cdd:PRK14691 126 SLAGFAAARALSTHFNSTpeKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDG 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 275 SGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVFGErASQIPISSTKSMTGHLLGAAGGIEAIACVQT 354
Cdd:PRK14691 206 DGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLA 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 402379267 355 LQEGKAHPTVGYQVADPDCD-LDYVTEGARDITADYTISNSFGFGGHNGVICLKKW 409
Cdd:PRK14691 285 LRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
1-410 7.31e-84

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 261.91  E-value: 7.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKeFDPSAVLERKEQKRMDLFSQYGLVAA 80
Cdd:PRK07967   1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  81 LEAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVM-DKKGAKRVTPFFVPMVIANMAAGNISIRLGAKGPSQTIV 159
Cdd:PRK07967  80 EQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMrGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 160 TACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAgFAALNALNTTEDAT--RASIPFDKERKGFVMGEGAGMLV 237
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKYNDTpeKASRAYDANRDGFVIAGGGGVVV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 238 LEELEHAQKRGATIYGEIVGYGSNCDASHMTAPlkdgSGAAAAMEMAIAEAGI-TPeqIGYINAHGTSTPANDAAETTAI 316
Cdd:PRK07967 239 VEELEHALARGAKIYAEIVGYGATSDGYDMVAP----SGEGAVRCMQMALATVdTP--IDYINTHGTSTPVGDVKELGAI 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 317 KRVFGERASqiPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPD-CDLDYVTEGARDITADYTISNSF 395
Cdd:PRK07967 313 REVFGDKSP--AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSF 390

                        410
                 ....*....|....*
gi 402379267 396 GFGGHNGVICLKKWE 410
Cdd:PRK07967 391 GFGGTNATLVFRRYK 405
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 3-404 1.03e-81

"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: 256.60  E-value: 1.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   3 RVVITGMGAVTPLGN---TVKEFWHNLVDGKLGIGKITKFDSEDTgVALAGEVKEFDPsavlERKEQKR---MDLFSQYG 76
Cdd:cd00828    2 RVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARLKSRFD-RGVAGQIPTGDI----PGWDAKRtgiVDRTTLLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  77 LVAALEAWEMSGLTEAT-IDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFFvpMVIANMAAGNISIRL-GAKGP 154
Cdd:cd00828   77 LVATEEALADAGITDPYeVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKW--MLSPNTVAGWVNILLlSSHGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 155 SQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEiGIAGFAALNAL-NTTEDATRASIPFDKERKGFVMGEGA 233
Cdd:cd00828  155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEE-GLSGFANMGALsTAEEEPEEMSRPFDETRDGFVEAEGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 234 GMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLkDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAET 313
Cdd:cd00828  234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 314 TAIKRVFGERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDI--TADYTI 391
Cdd:cd00828  313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLnlKVRAAL 392

                        410
                 ....*....|...
gi 402379267 392 SNSFGFGGHNGVI 404
Cdd:cd00828  393 VNAFGFGGSNAAL 405
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 2-401 4.58e-73

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: 233.79  E-value: 4.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAGEVKEFDPSAVLERKEQKRMDLFSQYGLVAAL 81
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  82 EAWEMSGLTEATIDPTRLGVIVGSGIGGMTTLQDQVRVMDKKGAKRVTPFfvpMVIANMAA---GNISIRLGAKGPSQTI 158
Cdd:cd00832   81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAY---QSFAWFYAvntGQISIRHGMRGPSGVV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 159 VTACASATNAIGEAFRTIKYGlADMMVTGGTEATVCEIGIAGFAALNALNTTEDATRASIPFDKERKGFVMGEGAGMLVL 238
Cdd:cd00832  158 VAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 239 EELEHAQKRGATIYGEIVGYGSNCDASHMTAplkDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKR 318
Cdd:cd00832  237 EDAAAARERGARVYGEIAGYAATFDPPPGSG---RPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAA 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 319 VFGERAsqIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITADYTISNSFGFG 398
Cdd:cd00832  314 VFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRG 391


                 ...
gi 402379267 399 GHN 401
Cdd:cd00832  392 GFN 394
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
1-408 3.02e-72

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 231.09  E-value: 3.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNtVKEFWHNLVDGKLGIGKITKF-DSEDTGVALAGEvkefDPSAVLERKEQKRMDLFSQYGLVA 79
Cdd:PRK05952   1 MMKVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPFpELPPLPLGLIGN----QPSSLEDLTKTVVTAALKDAGLTP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  80 ALE--------------AWEMsgLTEATIDPTRLGVIVGSGIGGMTTLQDQVrvmdkkgakrvtpffvpmviANMAAGNI 145
Cdd:PRK05952  76 PLTdcgvvigssrgcqgQWEK--LARQMYQGDDSPDEELDLENWLDTLPHQA--------------------AIAAARQI 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 146 sirlGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALnttedATRASIPFDKERK 225
Cdd:PRK05952 134 ----GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGAL-----AKTGAYPFDRQRE 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 226 GFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTST 305
Cdd:PRK05952 205 GLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTAT 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 306 PANDAAETTAIKRVFGeraSQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQvaDPDCDLDYVTEgARDI 385
Cdd:PRK05952 285 RLNDQREANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFVRQ-AQQS 358

                        410       420
                 ....*....|....*....|...
gi 402379267 386 TADYTISNSFGFGGHNGVICLKK 408
Cdd:PRK05952 359 PLQNVLCLSFGFGGQNAAIALGK 381
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 1-408 1.14e-69

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 225.30  E-value: 1.14e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   1 MKRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITKFDSEDTGVALAG--------EVKEFDPSAVLERKEQKRMDLF 72
Cdd:PRK07103   1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAGAGlasafigaELDSLALPERLDAKLLRRASLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  73 SQYGLVAALEAWEMSGLteATIDPTRLGVIVGSGIGgmtTLQDQVRVMDkkgAKRVTPFFVP-----MVIANMAAGNISI 147
Cdd:PRK07103  81 AQAALAAAREAWRDAAL--GPVDPDRIGLVVGGSNL---QQREQALVHE---TYRDRPAFLRpsyglSFMDTDLVGLCSE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 148 RLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNT---TEDATRASIPFDKER 224
Cdd:PRK07103 153 QFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSdrfADEPEAACRPFDQDR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 225 KGFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPlkDGSGAAAAMEMAIAEAGITPEQIGYINAHGTS 304
Cdd:PRK07103 233 DGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTG 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 305 TPANDAAETTAIkrvFGERASQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVgyQVADP-DCDLDYVTEGAR 383
Cdd:PRK07103 311 SPLGDETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSR--NLDEPiDERFRWVGSTAE 385

                        410       420
                 ....*....|....*....|....*
gi 402379267 384 DITADYTISNSFGFGGHNGVICLKK 408
Cdd:PRK07103 386 SARIRYALSLSFGFGGINTALVLER 410
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
149-401 9.71e-65

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 212.01  E-value: 9.71e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 149 LGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEaTVCEIGIAGFAALNALnttedATRASIPFDKERKGFV 228
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVD-SLCRLTLNGFNSLESL-----SPQPCRPFSANRDGIN 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 229 MGEGAGMLVLEELEHAQKRgatiygeIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPAN 308
Cdd:PRK09185 221 IGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 309 DAAETTAIKRVFGERasqIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLDYVTEGARDITAD 388
Cdd:PRK09185 294 DAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIR 370

                        250
                 ....*....|...
gi 402379267 389 YTISNSFGFGGHN 401
Cdd:PRK09185 371 YVLSNSFAFGGNN 383
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 3-401 1.17e-61

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: 204.71  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   3 RVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITK--FDSED----------TGVALAG---EVKEFDPS--AVLERkE 65
Cdd:cd00833    2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEdrWDADGyypdpgkpgkTYTRRGGfldDVDAFDAAffGISPR-E 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  66 QKRMDLFSQYGLVAALEAWEMSGLTEATIDPTRlgvivgsGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNI 145
Cdd:cd00833   81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSR-------TGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 146 SIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNttedATRASIPFDKERK 225
Cdd:cd00833  154 SYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----PDGRCRPFDADAD 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 226 GFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCD--ASHMTAPlkDGSGAAAAMEMAIAEAGITPEQIGYINAHGT 303
Cdd:cd00833  230 GYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrTKGITAP--SGEAQAALIRRAYARAGVDPSDIDYVEAHGT 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 304 STPANDAAETTAIKRVFGERASQ---IPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQVADPDCDLD---- 376
Cdd:cd00833  308 GTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEespl 387

                        410       420
                 ....*....|....*....|....*....
gi 402379267 377 YVTEGARDITADYTIS----NSFGFGGHN 401
Cdd:cd00833  388 RVPTEARPWPAPAGPRragvSSFGFGGTN 416
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 2-244 6.82e-58

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: 189.77  E-value: 6.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    2 KRVVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITK-----FDSEDTGVALAGEVK----------EFDPSAV-LERKE 65
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrwdpDKLYDPPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   66 QKRMDLFSQYGLVAALEAWEMSGLTEATIDPTRLGVIVGSGiggMTTLQDQVRVMDKKGAKRVTPFFVPMvIANMAAGNI 145
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSG---IGDYAALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  146 SIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALnTTEDATRASIPFDkerK 225
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGML-SPDGPCKAFDPFA---D 232

                         250
                  ....*....|....*....
gi 402379267  226 GFVMGEGAGMLVLEELEHA 244
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 71-406 8.94e-48

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: 165.89  E-value: 8.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  71 LFSQYGLVAALEAWEMSGLTEATIDPTRlgvivGSGIGGMTTLQDQVRVMDKKGAKRVTPFFVPMVIANMAAGNISIRLG 150
Cdd:cd00825   10 YVSILGFEAAERAIADAGLSREYQKNPI-----VGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 151 AKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAgFAALNALNTTEDATRasiPFDKERKGFVMG 230
Cdd:cd00825   85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCE-FDAMGALSTPEKASR---TFDAAADGFVFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 231 EGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDA 310
Cdd:cd00825  161 DGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 311 AETTAIKRVFGERasQIPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVgyQVADPDCDLDYVTEGARDITADYT 390
Cdd:cd00825  241 KELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSI--HIEELDEAGLNIVTETTPRELRTA 316

                        330
                 ....*....|....*.
gi 402379267 391 ISNSFGFGGHNGVICL 406
Cdd:cd00825  317 LLNGFGLGGTNATLVL 332
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 252-366 2.95e-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: 2.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  252 YGEIVGYGSNCDASHMTAPLKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTSTPANDAAETTAIKRVFGERASQ--IPI 329
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 402379267  330 SSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGY 366
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 4-401 1.43e-39

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 151.18  E-value: 1.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    4 VVITGMGAVTPLGNTVKEFWHNLVDGKLGIGKITK--------FDSED-----TGVALAG---EVKEFDP-----SAvle 62
Cdd:COG3321     6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPAdrwdadayYDPDPdapgkTYVRWGGfldDVDEFDAlffgiSP--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   63 rKEQKRMD----LFsqyglvaaLE-AWEmsGLTEATIDPTRLGVIVgsgiggmT------TLQDQVRVMDKKGAKrVTPF 131
Cdd:COG3321    83 -REAEAMDpqqrLL--------LEvAWE--ALEDAGYDPESLAGSR-------TgvfvgaSSNDYALLLLADPEA-IDAY 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  132 FVPMVIANMAAGNISIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTE 211
Cdd:COG3321   144 ALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDG 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  212 DaTRAsipFDKERKGFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCD--ASHMTAP------------LKDGsga 277
Cdd:COG3321   224 R-CRA---FDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrSNGLTAPngpaqaavirraLADA--- 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  278 aaamemaiaeaGITPEQIGYINAHGTSTPANDAAETTAIKRVFGERASQ---IPISSTKSMTGHLLGAAG--GIeaIACV 352
Cdd:COG3321   297 -----------GVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGvaGL--IKAV 363

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 402379267  353 QTLQEGKAHPTVGYQVADPDCDLD----YVTEGARDITADYT-----ISnSFGFGGHN 401
Cdd:COG3321   364 LALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRPWPAGGGprragVS-SFGFGGTN 420
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 134-409 2.93e-29

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: 120.88  E-value: 2.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   134 PMVIANMAAGNISIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNTTEDA 213
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDI 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   214 TrasiPFDKERKGFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDA--SHMTAPLKDGSGaaAAMEMAIAEAGIT 291
Cdd:TIGR02813  258 Q----PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   292 PEQIGYINAHGTSTPANDAAETTAIKRVFGERASQ---IPISSTKSMTGHLLGAAGGIEAIACVQTLQEGKAHPTVGYQV 368
Cdd:TIGR02813  332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQ 411

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 402379267   369 ADPDCDLD----YVTEGAR------DITADYTISNSFGFGGHNGVICLKKW 409
Cdd:TIGR02813  412 PNPKLDIEnspfYLNTETRpwmqreDGTPRRAGISSFGFGGTNFHMVLEEY 462
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 141-406 3.69e-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: 3.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 141 AAGNISIRLG-AKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEAtvceigiagfaalnalnttedatrasip 219
Cdd:cd00327   46 AAGQLAYHLGiSGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 220 fdkerkgFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMtAPLKDGSGAAAAMEMAIAEAGITPEQIGYIN 299
Cdd:cd00327   98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 300 AHGTSTPANDAAETTAIKRVFGERAsqIPISSTKSMTGHLLGAAGGIEAIACVQTLqEGKAHPTVGyqvADPDCDLdyvt 379
Cdd:cd00327  170 AHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLML-EHEFIPPTP---REPRTVL---- 239

                        250       260
                 ....*....|....*....|....*..
gi 402379267 380 egarditadytiSNSFGFGGHNGVICL 406
Cdd:cd00327  240 ------------LLGFGLGGTNAAVVL 254
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 4-401 9.59e-21

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: 91.62  E-value: 9.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267     4 VVITGMGAVTPLGNTVKEFWHNLVDGKLGIGkitkfdsedtgvalagevkEFDP-----SAvlerKEQKRMD----LFsq 74
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD-------------------LFDAaffgiSP----REAEAMDpqqrLL-- 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267    75 ygLVAALEAWEMSGlteatIDPTRLgvivgsgiggmttlqdqvrvmdkkgAKRVTPFFVpmvianmaaGnisirLGAKGP 154
Cdd:smart00825  56 --LEVAWEALEDAG-----IDPESL-------------------------RGSRTGVFV---------G-----VSSSDY 89

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   155 SQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEIGIAGFAALNALNttedATRASIPFDKERKGFVMGEGAG 234
Cdd:smart00825  90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVG 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   235 MLVLEELEHAQKRGATIYGEIVGYGSNCD--ASHMTAPlkdgSGaaaamemaiaeagitpeqigyinahgtstpandaae 312
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDgrSNGITAP----SG------------------------------------ 205

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267   313 ttaikrvfgerASQIPISSTKSMTGHLLGAAG--GIeaIACVQTLQEGKAHPTVGYQVADPDCDLD----YVTEGARDIT 386
Cdd:smart00825 206 -----------PAQLLIGSVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWP 272

                          410
                   ....*....|....*....
gi 402379267   387 ADYTIS----NSFGFGGHN 401
Cdd:smart00825 273 PPGRPRragvSSFGFGGTN 291
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
139-343 1.90e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 62.28  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 139 NMAAGNISIRLGAKGPSQTIVTACASATNAIGEAFRTIKYGLADMMVTGGTEAT-------VCEIGiaGFAALNALNTTE 211
Cdd:PRK06519 152 NLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAerpdmllLYELG--GLLLKGGWAPVW 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267 212 DATrasipfDKERKGFVMGEGAGMLVLEELEHAQKRGATIYGEIVGYGSNcdashmTAPLKDGSgAAAAMEMAIAEAGIT 291
Cdd:PRK06519 230 SRG------GEDGGGFILGSGGAFLVLESREHAEARGARPYARISGVESD------RARRAPGD-LEASLERLLKPAGGL 296

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 402379267 292 PEQIGYINAhgtstpANDAAETTAIKRVFGERASQIPISSTKSMTGHLLGAA 343
Cdd:PRK06519 297 AAPTAVISG------ATGAHPATAEEKAALEAALAGPVRGIGTLFGHTMEAQ 342
FabG2 COG4982
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and ...
 159-353 6.76e-07

3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and metabolism];


Pssm-ID: 444006 [Multi-domain]  Cd Length: 3088  Bit Score: 51.99  E-value: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  159 VTACASATNAIGEAFRTIKYGLADMMVTGGTEATVCEiGIAGFAALNALNTTEDATRASI--PF-----DKERKGFVMGE 231
Cdd:COG4982  2728 VAACATAAVSVEEGVDKIRLGKADFVVAGGIDDIGVE-SITGFGDMNATADSEEMLAKGIddRFfsranDRRRGGFVEAQ 2806

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402379267  232 GAGMLVLEELEHAQKRGATIYGEIVGYGSNCDASHMTAP-------LKDGSGAAAAMEMAIAEAGITPEQIGYINAHGTS 304
Cdd:COG4982  2807 GGGTILLARGDVAAKLGLPVLGVVAFAQSFADGAHTSIPapglgalAAARGGKDSKLARDLAKLGVTADDIAVVSKHDTS 2886

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 402379267  305 TPANDAAET-------TAIKRvfgERASQIPISSTKSMTGHllgAAGGieaiACVQ 353
Cdd:COG4982  2887 TNANDPNESelherlaHAIGR---TDGNPLFVVSQKSLTGH---AKGG----AAAF 2932
 
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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