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Conserved domains on  [gi|738072904|ref|WP_036031771|]
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MULTISPECIES: beta-ketoacyl-ACP synthase II [Burkholderia]

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;
3-411 0e+00

beta-ketoacyl-ACP synthase II;


:

Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 738.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   3 RRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  83 MQAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 163 ACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 243 EYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRA 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 323 FGDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                 ....*....
gi 738072904 403 TNGTLVFKR 411
Cdd:PRK07314 401 TNASLVFKR 409
 
Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-411 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 738.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   3 RRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  83 MQAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 163 ACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 243 EYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRA 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 323 FGDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                 ....*....
gi 738072904 403 TNGTLVFKR 411
Cdd:PRK07314 401 TNASLVFKR 409
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-410 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: 713.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904    4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*..
gi 738072904  404 NGTLVFK 410
Cdd:TIGR03150 401 NASLVFK 407
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-412 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: 649.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:COG0304  241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:COG0304  321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400

                 ....*....
gi 738072904 404 NGTLVFKRA 412
Cdd:COG0304  401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-409 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: 587.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:cd00834  241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:cd00834  321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400

                 ....*.
gi 738072904 404 NGTLVF 409
Cdd:cd00834  401 NASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-247 4.48e-57

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: 187.84  E-value: 4.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904    4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANI--TKFDATNY---STRFAGEVKG--------FNVEEYL---PAKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLFfgiSPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   68 ARHMDTFIHYGIAAGMQAMKDSGIEVTEENAERFGVVVGSGIGGLpmiEVTQTELLNRGPRRISPFFVPAsIINMISGHL 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  148 SIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQrnDDPATASRPWDkdr 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231
                         250       260
                  ....*....|....*....|
gi 738072904  228 DGFVLGEGAGVMVLEEYEHA 247
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
158-408 1.25e-14

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: 73.90  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   158 LAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSqrnddPATASRPWDKDRDGFVLGEGAG 237
Cdd:smart00825  91 VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVG 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   238 VMVLEEYEHAKARGAKIYAEVSGYGMSADAYH--MTAPvedgDGARRCML-----------AAlrnAGVnpdevnylnah 304
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAP----SGPAQLLIgsvksnighleAA---AGV----------- 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   305 gtsTQLgdlaetigIKrafgdrakqmvvnstksmtghllggagglesvfTVLAVHNQVSPPTINIFNQDPECDLD----Y 380
Cdd:smart00825 228 ---AGL--------IK---------------------------------VVLALKHGVIPPTLHFETPNPHIDLEesplR 263
                          250       260       270
                   ....*....|....*....|....*....|..
gi 738072904   381 CANEARDMKID----VALKNSFGFGGTNGTLV 408
Cdd:smart00825 264 VPTELTPWPPPgrprRAGVSSFGFGGTNAHVI 295
 
Name Accession Description Interval E-value
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-411 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 738.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   3 RRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAG 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  83 MQAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 163 ACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 243 EYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRA 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 323 FGDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400

                 ....*....
gi 738072904 403 TNGTLVFKR 411
Cdd:PRK07314 401 TNASLVFKR 409
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-410 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: 713.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904    4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*..
gi 738072904  404 NGTLVFK 410
Cdd:TIGR03150 401 NASLVFK 407
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-412 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: 649.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:COG0304    1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:COG0304   81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:COG0304  241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:COG0304  321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400

                 ....*....
gi 738072904 404 NGTLVFKRA 412
Cdd:COG0304  401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-409 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: 587.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:cd00834    1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:cd00834   81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:cd00834  241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:cd00834  321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400

                 ....*.
gi 738072904 404 NGTLVF 409
Cdd:cd00834  401 NASLVF 406
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1-411 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 544.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   1 MSRRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIA 80
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  81 AGMQAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAI 160
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 161 VTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMV 240
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 241 LEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIK 320
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 321 RAFGDR-AKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMK-IDVALKNSF 398
Cdd:PRK08722 321 RALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSF 400
                        410
                 ....*....|...
gi 738072904 399 GFGGTNGTLVFKR 411
Cdd:PRK08722 401 GFGGTNGSLIFKK 413
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-411 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 534.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   1 MSRRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVK--------GFNVEEYLPAKEARHMD 72
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  73 TFIHYGIAAGMQAMKDSGI-EVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKF 151
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWdPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 152 GLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQR-NDDPATASRPWDKDRDGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 231 VLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQL 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 311 GDLAETIGIKRAFGdRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECD-LDYCANEARDMK 389
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
                        410       420
                 ....*....|....*....|..
gi 738072904 390 IDVALKNSFGFGGTNGTLVFKR 411
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRR 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
4-411 8.39e-175

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 493.87  E-value: 8.39e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 244 YEHAKARGAKIYAEVSGYGMSADAYHMTAPVEdgDGARRCMLAALRNAGvNPdEVNYLNAHGTSTQLGDLAETIGIKRAF 323
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAG-NP-KIDYINAHGTSTPYNDKNETAALKELF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 324 GDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGGT 403
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397

                 ....*...
gi 738072904 404 NGTLVFKR 411
Cdd:PRK08439 398 NGVVIFKK 405
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
13-411 1.79e-150

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 432.58  E-value: 1.79e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  13 LISPVGNNVADGWANLVAGRSGIANITKFDA----------------TNYSTRFAGEVKG--FNVEEYLPAKearHMDTF 74
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDQseFDPSDFAPTK---RESRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  75 IHYGIAAGMQAMKDSGIEVTEE-NAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGL 153
Cdd:PTZ00050  78 THFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 154 KGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQR-NDDPATASRPWDKDRDGFVL 232
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 233 GEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAG-VNPDEVNYLNAHGTSTQLG 311
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 312 DLAETIGIKRAFGDR-AKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANE-ARDMK 389
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKtAHPLQ 397
                        410       420
                 ....*....|....*....|...
gi 738072904 390 -IDVALKNSFGFGGTNGTLVFKR 411
Cdd:PTZ00050 398 sIDAVLSTSFGFGGVNTALLFTK 420
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4-409 3.70e-137

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 399.55  E-value: 3.70e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDA--------------TNYSTRFAGEV-KGFNVEEYLPAK-- 66
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVpRGTGPGDFDEELwl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  67 EARHMDTFIHYGIAAGMQAMKDSGIEVTE-ENAERFGVVVGSGIGGLPMI-EVTQTELLNRGpRRISPFFVPASIINMIS 144
Cdd:PLN02836  86 NSRSSSRFIGYALCAADEALSDARWLPSEdEAKERTGVSIGGGIGSITDIlEAAQLICEKRL-RRLSPFFVPRILINMAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 145 GHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQR-NDDPATASRPW 223
Cdd:PLN02836 165 GHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPF 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 224 DKDRDGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNA 303
Cdd:PLN02836 245 DCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNA 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 304 HGTSTQLGDLAETIGIKRAFGDRAKQ--MVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYC 381
Cdd:PLN02836 325 HATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFV 404
                        410       420
                 ....*....|....*....|....*....
gi 738072904 382 A-NEARDMKIDVALKNSFGFGGTNGTLVF 409
Cdd:PLN02836 405 PlTASKAMLIRAALSNSFGFGGTNASLLF 433
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
1-409 4.12e-125

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 372.39  E-value: 4.12e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   1 MSRRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIA 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  81 AGMQAMKDSGIevTEENAERFGVVVGSGIGGLPM--IEV--TQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGP 156
Cdd:PLN02787 206 AGKKALADGGI--TEDVMKELDKTKCGVLIGSAMggMKVfnDAIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGP 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 157 NLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGA 236
Cdd:PLN02787 284 NYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGA 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 237 GVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAET 316
Cdd:PLN02787 364 GVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEY 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 317 IGIKRAFGdRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLD-YCANEARDMKIDVALK 395
Cdd:PLN02787 444 QALMRCFG-QNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALS 522
                        410
                 ....*....|....
gi 738072904 396 NSFGFGGTNGTLVF 409
Cdd:PLN02787 523 NSFGFGGHNSSILF 536
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4-411 8.17e-106

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 318.54  E-value: 8.17e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKgFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFG-VVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVT 162
Cdd:PRK07967  81 QAIADAGLSEEQVSNPRTGlIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 163 ACTTGLHCIGEAARLIEYGDADLMIAGGAEA---TVSPLgiggFAAARALS-QRNDDPATASRPWDKDRDGFVLGEGAGV 238
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEEldwEMSCL----FDAMGALStKYNDTPEKASRAYDANRDGFVIAGGGGV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 239 MVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPveDGDGARRCMLAALrnAGVNPDeVNYLNAHGTSTQLGDLAETIG 318
Cdd:PRK07967 237 VVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATVDTP-IDYINTHGTSTPVGDVKELGA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 319 IKRAFGDRAKQmvVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPE-CDLDYCANEARDMKIDVALKNS 397
Cdd:PRK07967 312 IREVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNS 389
                        410
                 ....*....|....
gi 738072904 398 FGFGGTNGTLVFKR 411
Cdd:PRK07967 390 FGFGGTNATLVFRR 403
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
124-411 1.84e-98

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 297.41  E-value: 1.84e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 124 NRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGF 203
Cdd:PRK14691  51 SRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGF 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 204 AAARALSQR-NDDPATASRPWDKDRDGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARR 282
Cdd:PRK14691 131 AAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYR 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 283 CMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAFGDrAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQV 362
Cdd:PRK14691 211 AMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQI 289
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 738072904 363 SPPTINIFNQDPECD-LDYCANEARDMKIDVALKNSFGFGGTNGTLVFKR 411
Cdd:PRK14691 290 VPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
6-411 2.73e-91

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 281.90  E-value: 2.73e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   6 VVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEY----LPAKEARhmdtfihygiAA 81
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFgasaLSEALAR----------LA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  82 GMQAMKDSGIE--------------VTEENAERFGVVVGSGIGGlpmiEVTQTELLNRGPRRISPFFVPASIINMISGHL 147
Cdd:PRK06501  83 AEEALAQAGIGkgdfpgplflaappVELEWPARFALAAAVGDND----APSYDRLLRAARGGRFDALHERFQFGSIADRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 148 SIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPATASRPWDKDR 227
Cdd:PRK06501 159 ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 228 DGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTS 307
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 308 TQLGDLAETIGIKRAFGDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARD 387
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARD 398
                        410       420
                 ....*....|....*....|....
gi 738072904 388 MKIDVALKNSFGFGGTNGTLVFKR 411
Cdd:PRK06501 399 ARVTAVLSNSFGFGGQNASLVLTA 422
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4-410 1.75e-87

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 271.48  E-value: 1.75e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANIT---KFDATNysTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIA 80
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPewdRYDGLN--TRLAAPIDDFELPAHYTRKKIRSMGRVSLMATR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  81 AGMQAMKDSGI--EVTEENAERFGVVVGSGIGGLPMIEVTqTELLNRGPRRISPffvpASIINMISgH-----LSIKFGL 153
Cdd:PRK09116  80 ASELALEDAGLlgDPILTDGRMGIAYGSSTGSTDPIGAFG-TMLLEGSMSGITA----TTYVRMMP-HttavnVGLFFGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 154 KGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEAtVSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLG 233
Cdd:PRK09116 154 KGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 234 EGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPveDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDL 313
Cdd:PRK09116 233 EGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDI 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 314 AETIGIKRAFGDRakqMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPEC-DLDYCANEARDMKIDV 392
Cdd:PRK09116 311 AESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEY 387
                        410
                 ....*....|....*...
gi 738072904 393 ALKNSFGFGGTNGTLVFK 410
Cdd:PRK09116 388 VMSNNFAFGGINTSLIFK 405
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
6-412 2.15e-87

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 271.60  E-value: 2.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   6 VVVTGLGLISPVGNNVADGWANLVAGRSGIANITK--FDATNYSTRFAGEVKGfNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDpfVEEFDLPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGieVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTA 163
Cdd:PRK07910  93 RVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARA-LSQRNDDPATASRPWDKDRDGFVLGEGAGVMVLE 242
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 243 EYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRA 322
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 323 FGdrAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFGFGG 402
Cdd:PRK07910 331 LG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGG 408
                        410
                 ....*....|
gi 738072904 403 TNGTLVFKRA 412
Cdd:PRK07910 409 HNVALAFGRY 418
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
4-408 8.58e-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: 233.48  E-value: 8.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADG---WANLVAGRSGIANITKFDATnYSTRFAGEVKGFNVEEYLpAKEARHMDTFIHYGIA 80
Cdd:cd00828    1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSR-FDRGVAGQIPTGDIPGWD-AKRTGIVDRTTLLALV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  81 AGMQAMKDSGIEV-TEENAERFGVVVGSGIGglpMIEVTQTELLNRGpRRISPFFVPASI--INMISGHLSIKFGLK-GP 156
Cdd:cd00828   79 ATEEALADAGITDpYEVHPSEVGVVVGSGMG---GLRFLRRGGKLDA-RAVNPYVSPKWMlsPNTVAGWVNILLLSShGP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 157 NLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATvSPLGIGGFAAARALSQRNDDPATASRPWDKDRDGFVLGEGA 236
Cdd:cd00828  155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 237 GVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVeDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAET 316
Cdd:cd00828  234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 317 IGIKRAFGDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARD--MKIDVAL 394
Cdd:cd00828  313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDlnLKVRAAL 392
                        410
                 ....*....|....
gi 738072904 395 KNSFGFGGTNGTLV 408
Cdd:cd00828  393 VNAFGFGGSNAALV 406
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
4-408 4.70e-70

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: 226.09  E-value: 4.70e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:cd00832    1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMKDSGIEVTEENAERFGVVVGSGIGGLpmiEVTQTELLN---RGPRRISPFFVPASIINMISGHLSIKFGLKGPNLAI 160
Cdd:cd00832   81 WALADAGVDPAALPPYDMGVVTASAAGGF---EFGQRELQKlwsKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 161 VTACTTGLHCIGEAARLIEYGdADLMIAGGAEATVSPLGIGGFAAARALSqRNDDPATASRPWDKDRDGFVLGEGAGVMV 240
Cdd:cd00832  158 VAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLS-TSDDPARAYLPFDAAAAGYVPGEGGAILV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 241 LEEYEHAKARGAKIYAEVSGYGMSADAyhmtAPVED-GDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGI 319
Cdd:cd00832  236 LEDAAAARERGARVYGEIAGYAATFDP----PPGSGrPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAAL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 320 KRAFGDRAkqMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKIDVALKNSFG 399
Cdd:cd00832  312 AAVFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARG 389

                 ....*....
gi 738072904 400 FGGTNGTLV 408
Cdd:cd00832  390 RGGFNSALV 398
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5-411 1.17e-67

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 219.54  E-value: 1.17e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   5 RVVVTGLGLISPVGNnVADGWANLVAGRSGIANITKFdatnystrfaGEVKGFNVEeyLPAKEARHMDTFIHYGIAAgmq 84
Cdd:PRK05952   3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPF----------PELPPLPLG--LIGNQPSSLEDLTKTVVTA--- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  85 AMKDSGIEVTEENA--------------ERFGVVVGSGIGGLPMIEVTQtELLNRGPRRISpfFVPASIInmisghlsik 150
Cdd:PRK05952  67 ALKDAGLTPPLTDCgvvigssrgcqgqwEKLARQMYQGDDSPDEELDLE-NWLDTLPHQAA--IAAARQI---------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 151 fGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQrnddpaTASRPWDKDRDGF 230
Cdd:PRK05952 134 -GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 231 VLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQL 310
Cdd:PRK05952 207 VLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRL 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 311 GDLAETIGIKRAFGDRakqMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIfnQDPECDLDYcANEARDMKI 390
Cdd:PRK05952 287 NDQREANLIQALFPHR---VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNF-VRQAQQSPL 360
                        410       420
                 ....*....|....*....|.
gi 738072904 391 DVALKNSFGFGGTNGTLVFKR 411
Cdd:PRK05952 361 QNVLCLSFGFGGQNAAIALGK 381
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
5-411 1.40e-57

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 194.09  E-value: 1.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   5 RVVVTGLGLISPVGNNVADGWANLVAGRSGI--------ANITKFDATNYSTRFAGEVKGFNVEEYLPAKEARHMDTFIH 76
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgrQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  77 YGIAAGMQAMKDS----------GIEVTEENaerfgvvvgsgigglpmieVTQTELLNRGPR-RISPFFVPASII----- 140
Cdd:PRK07103  83 AALAAAREAWRDAalgpvdpdriGLVVGGSN-------------------LQQREQALVHETyRDRPAFLRPSYGlsfmd 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 141 NMISGHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARAL-SQRN-DDPAT 218
Cdd:PRK07103 144 TDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgSDRFaDEPEA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 219 ASRPWDKDRDGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPveDGDGARRCMLAALRNAGVNPDEV 298
Cdd:PRK07103 224 ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 299 NYLNAHGTSTQLGDLAEtigIKRAFGDRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQ-DPECd 377
Cdd:PRK07103 302 DYVNPHGTGSPLGDETE---LAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF- 377
                        410       420       430
                 ....*....|....*....|....*....|....
gi 738072904 378 lDYCANEARDMKIDVALKNSFGFGGTNGTLVFKR 411
Cdd:PRK07103 378 -RWVGSTAESARIRYALSLSFGFGGINTALVLER 410
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-247 4.48e-57

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: 187.84  E-value: 4.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904    4 RRVVVTGLGLISPVGNNVADGWANLVAGRSGIANI--TKFDATNY---STRFAGEVKG--------FNVEEYL---PAKE 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLFfgiSPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   68 ARHMDTFIHYGIAAGMQAMKDSGIEVTEENAERFGVVVGSGIGGLpmiEVTQTELLNRGPRRISPFFVPAsIINMISGHL 147
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  148 SIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQrnDDPATASRPWDkdr 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231
                         250       260
                  ....*....|....*....|
gi 738072904  228 DGFVLGEGAGVMVLEEYEHA 247
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
151-412 7.75e-57

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 191.59  E-value: 7.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 151 FGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEaTVSPLGIGGFAAARALSqrnddpATASRPWDKDRDGF 230
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVD-SLCRLTLNGFNSLESLS------PQPCRPFSANRDGI 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 231 VLGEGAGVMVLEeyehakaRGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQL 310
Cdd:PRK09185 220 NIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPL 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 311 GDLAETIGIKRAFGDRakqMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPECDLDYCANEARDMKI 390
Cdd:PRK09185 293 NDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAI 369
                        250       260
                 ....*....|....*....|..
gi 738072904 391 DVALKNSFGFGGTNGTLVFKRA 412
Cdd:PRK09185 370 RYVLSNSFAFGGNNCSLIFGRA 391
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
5-408 4.66e-56

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: 190.08  E-value: 4.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   5 RVVVTGLGLISPVGNNVADGWANLVAGRSGIANITK--FDATNYS----------TRFAG---EVKGFNVEEY-LPAKEA 68
Cdd:cd00833    2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEdrWDADGYYpdpgkpgktyTRRGGfldDVDAFDAAFFgISPREA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  69 RHMD------------TFIHYGIAAGMQAMKDSGIEVTEENAERfgvvvgsgigglpmievtqTELLNRGPRRISPFFVP 136
Cdd:cd00833   82 EAMDpqqrlllevaweALEDAGYSPESLAGSRTGVFVGASSSDY-------------------LELLARDPDEIDAYAAT 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 137 ASIINMISGHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSqrnddP 216
Cdd:cd00833  143 GTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----P 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 217 ATASRPWDKDRDGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAY--HMTAPveDGDGARRCMLAALRNAGVN 294
Cdd:cd00833  218 DGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVD 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 295 PDEVNYLNAHGTSTQLGDLAETIGIKRAFGDRAKQM---VVNSTKS----------MTghllggaggleSVF-TVLAVHN 360
Cdd:cd00833  296 PSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADqplLIGSVKSnighleaaagLA-----------GLIkVVLALEH 364
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738072904 361 QVSPPTINIFNQDPECDLDYCANEARDMKID--------VALKNSFGFGGTNGTLV 408
Cdd:cd00833  365 GVIPPNLHFETPNPKIDFEESPLRVPTEARPwpapagprRAGVSSFGFGGTNAHVI 420
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
76-408 7.68e-51

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: 173.98  E-value: 7.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  76 HYGIAAGMQAMKDSGIEVTEENAERFGVVVGSGIGGLPMIEVTQTELLNRGPRRISPFFVPASiinmiSGHLSIKFGLKG 155
Cdd:cd00825   13 ILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLGIHG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 156 PNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSqrnddPATASRPWDKDRDGFVLGEG 235
Cdd:cd00825   88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 236 AGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAE 315
Cdd:cd00825  163 AGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 316 TIGIKRAFGDRakQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQDPecDLDYCANEARDMKIDVALK 395
Cdd:cd00825  243 LKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALL 318
                        330
                 ....*....|...
gi 738072904 396 NSFGFGGTNGTLV 408
Cdd:cd00825  319 NGFGLGGTNATLV 331
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1-404 9.63e-44

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 163.50  E-value: 9.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904    1 MSRRRVVVTGLGLISPVGNNVADGWANLVAGRSGIANITK--------FDA------TNYSTR--FAGEVKGFNVEEY-L 63
Cdd:COG3321     1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPAdrwdadayYDPdpdapgKTYVRWggFLDDVDEFDALFFgI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   64 PAKEARHMDtfihygiaagMQ----------AMKDSGIEVTEENAER---FgvvvgsgigglpmIEVTQTE---LLNRGP 127
Cdd:COG3321    81 SPREAEAMD----------PQqrlllevaweALEDAGYDPESLAGSRtgvF-------------VGASSNDyalLLLADP 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  128 RRISPFFVPASIINMISGHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAAR 207
Cdd:COG3321   138 EAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  208 ALSqrnddPATASRPWDKDRDGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSAD-AYH-MTAPveDGDGARRCML 285
Cdd:COG3321   218 MLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAP--NGPAQAAVIR 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  286 AALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAFG-DRAKQ--MVVNSTKSMtghllggagglesvF--------- 353
Cdd:COG3321   291 RALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGqGRPADqpCAIGSVKSN--------------Ighleaaagv 356
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738072904  354 -----TVLAVHNQVSPPTINiFNQ-DPECDLD----YCANEARDMKID----VALKNSFGFGGTN 404
Cdd:COG3321   357 aglikAVLALRHGVLPPTLH-FETpNPHIDFEnspfYVNTELRPWPAGggprRAGVSSFGFGGTN 420
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
255-369 1.50e-35

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: 126.91  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  255 YAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNPDEVNYLNAHGTSTQLGDLAETIGIKRAFGDRAKQ--MVV 332
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 738072904  333 NSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINI 369
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
136-410 4.97e-34

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: 135.13  E-value: 4.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   136 PASIINMISGHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDd 215
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   216 pataSRPWDKDRDGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSADAYHMTAPVEDGDGARRCMLAALRNAGVNP 295
Cdd:TIGR02813  257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   296 DEVNYLNAHGTSTQLGDLAETIGIKRAFG---DRAKQMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTINIFNQ 372
Cdd:TIGR02813  333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 738072904   373 DPECDLD----YCANEAR------DMKIDVALKNSFGFGGTNGTLVFK 410
Cdd:TIGR02813  413 NPKLDIEnspfYLNTETRpwmqreDGTPRRAGISSFGFGGTNFHMVLE 460
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
144-408 3.91e-24

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: 100.21  E-value: 3.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 144 SGHLSIKFGLK-GPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEAtvsplgiggfaaaralsqrnddpatasrp 222
Cdd:cd00327   47 AGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE----------------------------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 223 wdkdrdgFVLGEGAGVMVLEEYEHAKARGAKIYAEVSGYGMSAD-AYHMTAPVedGDGARRCMLAALRNAGVNPDEVNYL 301
Cdd:cd00327   98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVS--GEGLARAARKALEGAGLTPSDIDYV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 302 NAHGTSTQLGDLAETIGIKRAFGDRAkqMVVNSTKSMTGHLLGGAGGLESVFTVLAVHNQVSPPTinifNQDPECdldyc 381
Cdd:cd00327  169 EAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----PREPRT----- 237
                        250       260
                 ....*....|....*....|....*..
gi 738072904 382 aneardmkidvALKNSFGFGGTNGTLV 408
Cdd:cd00327  238 -----------VLLLGFGLGGTNAAVV 253
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
158-408 1.25e-14

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: 73.90  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   158 LAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSqrnddPATASRPWDKDRDGFVLGEGAG 237
Cdd:smart00825  91 VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVG 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   238 VMVLEEYEHAKARGAKIYAEVSGYGMSADAYH--MTAPvedgDGARRCML-----------AAlrnAGVnpdevnylnah 304
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAP----SGPAQLLIgsvksnighleAA---AGV----------- 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   305 gtsTQLgdlaetigIKrafgdrakqmvvnstksmtghllggagglesvfTVLAVHNQVSPPTINIFNQDPECDLD----Y 380
Cdd:smart00825 228 ---AGL--------IK---------------------------------VVLALKHGVIPPTLHFETPNPHIDLEesplR 263
                          250       260       270
                   ....*....|....*....|....*....|..
gi 738072904   381 CANEARDMKID----VALKNSFGFGGTNGTLV 408
Cdd:smart00825 264 VPTELTPWPPPgrprRAGVSSFGFGGTNAHVI 295
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
4-300 6.73e-10

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


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 60.03  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   4 RRVVVTGLGLISPVGnnvADGWANLVAGRSGIANITKfdatnysTRFAGEVKGfnveEYLPAKEARHMDTFIHYGIAAGM 83
Cdd:PRK06147   3 RALAIVGSGMVTAVG---LDAPSSCAAIRARLDNFQE-------TRFIDPPGG----EWLIGAPVPLPPPWRGPERLAEM 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  84 QAMkdsgieVTEENAErfgvvvgsgigGLPMIEVTQTELLNRGP---RRISPFFVPASIINMISGHLSIKFGlkgPNLAI 160
Cdd:PRK06147  69 AAP------AIAEALE-----------GLPALDASEAPLLLCVAeeeRPGRPPDLEERLLRELEARLGLRLE---PGSAV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 161 VTACTTGLHC-IGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALsqrnddpATASRPwdkdrDGFVLGEGAGVM 239
Cdd:PRK06147 129 IARGRVSGAVaLAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRL-------LTSQNS-----NGFIPGEAAAAV 196
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738072904 240 VLEEYEHAKARGAKIYaevsGYGMSADAyhmtAPVED-------GDGARRCMLAALRNAGVNPDEVNY 300
Cdd:PRK06147 197 LLGRPAGGEAPGLPLL----GLGLGREP----APVGEsedlplrGDGLTQAIRAALAEAGCGLEDMDY 256
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
1-260 1.05e-08

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 56.50  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904   1 MSRRRVVVTGLGLISPVGNNVADGWANLvAGRSGIANItkfDATNYSTRFAGEVKGFNVEEYLPAK-EARHMDTFIHYGI 79
Cdd:PRK06519   3 MQPNDVVITGIGLVSSLGEGLDAHWNAL-SAGRPQPNV---DTETFAPYPVHPLPEIDWSQQIPKRgDQRQMETWQRLGT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904  80 -AAGMqAMKDSGIEVTEE------------NAER--------FGVVVGSGIGGLPMIEVTQTELlnrgprRISPFFVPAS 138
Cdd:PRK06519  79 yAAGL-ALDDAGIKGNEEllstmdmivaagGGERdiavdtaiLNEARKRNDRGVLLNERLMTEL------RPTLFLAQLS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738072904 139 iiNMISGHLSIKFGLKGPNLAIVTACTTGLHCIGEAARLIEYGDADLMIAGGAEATVSPLGIGGFAAARALSQRNDDPAT 218
Cdd:PRK06519 152 --NLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGWAPVW 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 738072904 219 ASRPWDKDrdGFVLGEGAGVMVLEEYEHAKARGAKIYAEVSG 260
Cdd:PRK06519 230 SRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARISG 269
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
163-236 3.96e-05

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: 45.44  E-value: 3.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738072904 163 ACTTGLHCIGEAARLIEYGDADLMIAGGAEA-TVSPLGIGGFAAARALSQRNDDPATASRPWDkDRDGFVLGEGA 236
Cdd:COG0183   87 VCGSGLQAVALAAQAIAAGDADVVIAGGVESmSRAPMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGETA 160
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
164-192 6.09e-04

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 41.86  E-value: 6.09e-04
                         10        20
                 ....*....|....*....|....*....
gi 738072904 164 CTTGLHCIGEAARLIEYGDADLMIAGGAE 192
Cdd:PRK09050  90 CGSGMDAVGTAARAIKAGEAELMIAGGVE 118
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
163-192 4.74e-03

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: 39.00  E-value: 4.74e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 738072904 163 ACTTGLHCIGEAARLIEYGDADLMIAGGAE 192
Cdd:cd00751   83 VCGSGLQAVALAAQSIAAGEADVVVAGGVE 112
 
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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