|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2-1224 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 881.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 2 PTENAVAVVGMACRLPGADDTAGYWAALTGGVDGISRFTPE-WLLDQGADPDY-VGRENFVPAMGVVTGSRRFDWPYFRY 79
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADrWDADAYYDPDPdAPGKTYVRWGGFLDDVDEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 80 SRAEAAAMDPQQRVFLECATTAVDDAGIDPTRFPG-RIGVYAGAD-----RVGPGADDPLSELALyIGREKDFLATRVAY 153
Cdd:COG3321 81 SPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGsRTGVFVGASsndyaLLLLADPEAIDAYAL-TGNAKSVLAGRISY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 154 KLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGILSPDGRCRPFDERAGGTVPAE 233
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 234 GVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDKmAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGTATRLGDP 313
Cdd:COG3321 240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 314 VEVEALTDVFRDSTDTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASPFRVAAANE 393
Cdd:COG3321 319 IEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 394 PWPDRGT-RLAAVSSFGVGGTNAHVLLQGAPSRAPRKGRP--GFHPLTLSAASPDALGRLAGALADRLEpataGEAAPTL 470
Cdd:COG3321 399 PWPAGGGpRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAarPPQLLVLSAKTEEALRALAARLAAFLE----AHPDLDL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 471 AEVSRTLAERRVH-RHRKALVAAEPAVAARLLRGAAEPGPP-------RRKLGKAAFLFPGQGTLRHGAGTAAYQLLPGF 542
Cdd:COG3321 475 ADVAYTLATGRAHfEHRLAVVASSREELAAKLRALAAGEAApgvvtgaAAAAPKVAFLFPGQGSQYVGMGRELYETEPVF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 543 RAEFDEIRKGVRDAHDIDLTPVVTDPADQDWFTDTVHQQLGLFALGYAFGRQLRAWNIRPAAMLGNSIGEYVAAALAGVW 622
Cdd:COG3321 555 RAALDECDALLRPHLGWSLREVLFPDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 623 SPQDAADLVHRRARAMWDTEP-GLMVSVAARADEVVPRLPGDGEVTVA-VEAPGSVVLSGPEAAMTELLAGDRLAGLGTT 700
Cdd:COG3321 635 SLEDALRLVAARGRLMQALPGgGAMLAVGLSEEEVEALLAGYDGVSIAaVNGPRSTVVSGPAEAVEALAARLEARGIRAR 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 701 LIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGrQAAPQEVTDPAYWAAQLRRPVLLGEAMRTLLGSGCTT 780
Cdd:COG3321 715 RLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTG-TWLTGEALDADYWVRHLRQPVRFADAVEALLADGVRV 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 781 YVELGPGSSMIGGLRRTPGWDSSFAAVPlTARREDPAEAGLLNALATLWELGADRALEDVLgtapgaGEERPSRCSLPGY 860
Cdd:COG3321 794 FLEVGPGPVLTGLVRQCLAAAGDAVVLP-SLRRGEDELAQLLTALAQLWVAGVPVDWSALY------PGRGRRRVPLPTY 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 861 QFRGEDPEQTDAAAPPAPAARRAPAAAPARTADTRAVLAELWCRTLGVPVALDDDSFFALGGESLMAVSLTAQVRELTGC 940
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 941 VLSVTDFSRAPSFGRLVETVERQSPARPAPAATGTLPVPGVATLTEGGTGRPVFLVADATGTALPYRHLAALLAPLAANR 1020
Cdd:COG3321 947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1021 PVLGLEDPGGPRTRTIPAIAADHVTALLRTQPEGPYTLGGWSFGAVVAHEMAYRLTRLGKRVDLLVCLDGFVPDTGGRPV 1100
Cdd:COG3321 1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1101 SFAPEFLRAGLRSQAEALLGIGPVARRLGRATALRRQFVANQATLLRYRPRPVACPVVLFKASSGPAEADRLRGRLSGLY 1180
Cdd:COG3321 1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 753979669 1181 GDGVRVEPVGGDHWSMLTGPYADELALKLAHALPAEDSAEQGER 1224
Cdd:COG3321 1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAA 1230
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
7-419 |
0e+00 |
|
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: 542.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGISRFTPEWLLDQGADPD-YVGRENFVPAMGVVTGSRRFDWPYFRYSRAEAA 85
Cdd:cd00833 3 IAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDpGKPGKTYTRRGGFLDDVDAFDAAFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 86 AMDPQQRVFLECATTAVDDAGIDPTRFPG-RIGVYAGA---DRVGPGADDPLSELALYI-GREKDFLATRVAYKLGLRGP 160
Cdd:cd00833 83 AMDPQQRLLLEVAWEALEDAGYSPESLAGsRTGVFVGAsssDYLELLARDPDEIDAYAAtGTSRAFLANRISYFFDLRGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 161 ALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGILSPDGRCRPFDERAGGTVPAEGVAVVVL 240
Cdd:cd00833 163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 241 KRLADALRDGDRIAGVIAGTAINNDGSDKmAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGTATRLGDPVEVEALT 320
Cdd:cd00833 243 KRLSDALRDGDRIYAVIRGSAVNQDGRTK-GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 321 DVFRDSTDTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASPFRVAAANEPWP-DRG 399
Cdd:cd00833 322 KVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPaPAG 401
|
410 420
....*....|....*....|
gi 753979669 400 TRLAAVSSFGVGGTNAHVLL 419
Cdd:cd00833 402 PRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
7-420 |
3.02e-134 |
|
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: 410.95 E-value: 3.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGISRFtpewlldqgadpdyvgrenfvpamgvvtgsrrfDWPYFRYSRAEAAA 86
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVDLF---------------------------------DAAFFGISPREAEA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 87 MDPQQRVFLECATTAVDDAGIDPTRFPG-RIGVYAGAdrvgpGADDplselalyigrekdflatrvaYklglrgpALTVQ 165
Cdd:smart00825 48 MDPQQRLLLEVAWEALEDAGIDPESLRGsRTGVFVGV-----SSSD---------------------Y-------SVTVD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 166 TACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGILSPDGRCRPFDERAGGTVPAEGVAVVVLKRLAD 245
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 246 ALRDGDRIAGVIAGTAINNDGSDKmAYTAPSVPGQseviraaqriagidpadidyveahgtatrlgdpvevealtdvfrd 325
Cdd:smart00825 175 ALRDGDPILAVIRGSAVNQDGRSN-GITAPSGPAQ--------------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 326 stdttgaCLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASPFRVAAANEPWPDRGT-RLAA 404
Cdd:smart00825 209 -------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPPGRpRRAG 281
|
410
....*....|....*.
gi 753979669 405 VSSFGVGGTNAHVLLQ 420
Cdd:smart00825 282 VSSFGFGGTNAHVILE 297
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
520-813 |
5.58e-69 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 233.83 E-value: 5.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 520 LFPGQGTLRHGAGTAAYQLLPGFRAEFDEIRKGVRDAHDIDLTPVVTDPADQDWFTDTVHQQLGLFALGYAFGRQLRAWN 599
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 600 IRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAMWDT-EPGLMVSVAARADEVVPRL-PGDGEVTVAVE-APGSV 676
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALpGGGAMLAVGLSEEEVEPLLaGVPDRVSVAAVnSPSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 677 VLSGPEAAMTELLAGDRLAGLGTTLIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGRQAAPQEVTDPAYW 756
Cdd:smart00827 161 VLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDADYW 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 753979669 757 AAQLRRPVLLGEAMRTLLGS-GCTTYVELGPGSSMIGGLRRTPGWDSSFAAVPlTARR 813
Cdd:smart00827 241 VRNLREPVRFADAVRALLAEgGVTVFLEVGPHPVLTGPIKQTLAAAGSAVVLP-SLRR 297
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
7-786 |
2.62e-67 |
|
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: 250.69 E-value: 2.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGI-----SRFTPEWLLD---QGADPDYVGRENFVPAMGvvtgsrrFDWPYFR 78
Cdd:TIGR02813 9 IAIVGMASIFANSRYLNKFWDLIFEKIDAItdvpsDHWAKDDYYDsdkSEADKSYCKRGGFLPEVD-------FNPMEFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 79 YSRAEAAAMDPQQRVFLECATTAVDDAGIDPTRFPGRIGVYAG------------ADRVGP---------GADDPLSELA 137
Cdd:TIGR02813 82 LPPNILELTDISQLLSLVVAKEVLNDAGLPDGYDRDKIGITLGvgggqkqssslnARLQYPvlkkvfkasGVEDEDSEML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 138 L------YIGREKD--------FLATRVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVmPRGEW 203
Cdd:TIGR02813 162 IkkfqdqYIHWEENsfpgslgnVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCT-DNSPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 204 GYL-FEQGGILSPDGRCRPFDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDKMAYtAPSVPGQSE 282
Cdd:TIGR02813 241 MYMsFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY-APRPEGQAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 283 VIRAAQRIAGIDPADIDYVEAHGTATRLGDPVEVEALTDVFRDSTDTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLE 362
Cdd:TIGR02813 320 ALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 363 HGQIVPTVHFTSPNPLLELEASPFRVAAANEPWPDR--GT-RLAAVSSFGVGGTNAHVLLQGAPSRAPR----KGRPGFH 435
Cdd:TIGR02813 400 HKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQRedGTpRRAGISSFGFGGTNFHMVLEEYSPKHQRddqyRQRAVAQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 436 PLTLSAASPDAL-GRLAGALADRLEPATAGEAAPTLAEVSRTLAERRVHRHRKALVAAEPAVAARLLRGAAE-------- 506
Cdd:TIGR02813 480 TLLFTAANEKALvSSLKDWKNKLSAKADDQPYAFNALAVENTLRTIAVALARLGFVAKNADELITMLEQAITqleaksce 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 507 -----PGPPRRK------LGKAAFLFPGQGTLRHGAGTAAYQLLPGFRAEFDEIRKGVRDAHDIDLTPVV---------T 566
Cdd:TIGR02813 560 ewqlpSGISYRKsalvveSGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLypipvfndeS 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 567 DPADQDWFTDTVHQQLGLFALGYAFGRQLRAWNIRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAM----WDTE 642
Cdd:TIGR02813 640 RKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMaaptGEAD 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 643 PGLMVSVAARADEVVPRLPGD----GEVTVA-VEAPGSVVLSGPEAAMTelLAGDRLAGLGTTLIH--TRRAFHSKAMDG 715
Cdd:TIGR02813 720 IGFMYAVILAVVGSPTVIANCikdfEGVSIAnYNSPTQLVIAGVSTQIQ--IAAKALKEKGFKAIPlpVSGAFHTPLVAH 797
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753979669 716 AAEEVRAAISSMPVRPPRQPLISGTTGrQAAPQEVTD-PAYWAAQLRRPVLLGEAMRTLLGSGCTTYVELGP 786
Cdd:TIGR02813 798 AQKPFSAAIDKAKFNTPLVPLYSNGTG-KLHSNDAAAiKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGP 868
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
5-246 |
1.20e-64 |
|
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: 219.43 E-value: 1.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 5 NAVAVVGMACRLPGADDTAGYWAALTGGVDGISRFTPE-WLLDQGADPDYVGRENFVPAMGVVTGSRRFDWPYFRYSRAE 83
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrWDPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 84 AAAMDPQQRVFLECATTAVDDAGIDPTRFPG-RIGVYAG-------ADRVGPGADDPLSELALYIGREKDFLATRVAYKL 155
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGsRTGVFIGsgigdyaALLLLDEDGGPRRGSPFAVGTMPSVIAGRISYFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 156 GLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGILSPDGRCRPFDERAGGTVPAEGV 235
Cdd:pfam00109 161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240
|
250
....*....|.
gi 753979669 236 AVVVLKRLADA 246
Cdd:pfam00109 241 GAVVLKRLSDA 251
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
7-419 |
4.69e-64 |
|
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: 223.57 E-value: 4.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGISRFTPEWLLDQGADpdyvgrenfvpamgvVTGSRRFDWPYFRYSRAEAAA 86
Cdd:cd00834 3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSR---------------IAGEVPDFDPEDYLDRKELRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 87 MDPQQRVFLECATTAVDDAGIDPTRF-PGRIGVYAGADRvgPGADDPLSELALYIGREKDFL-------------ATRVA 152
Cdd:cd00834 68 MDRFAQFALAAAEEALADAGLDPEELdPERIGVVIGSGI--GGLATIEEAYRALLEKGPRRVspffvpmalpnmaAGQVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 153 YKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS-----PDGRCRPFDER 225
Cdd:cd00834 146 IRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAeaLITPLTLAG--FAALRALStrnddPEKASRPFDKD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 226 AGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDkMayTAPSV--PGQSEVIRAAQRIAGIDPADIDYVEA 303
Cdd:cd00834 224 RDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYH-I--TAPDPdgEGAARAMRAALADAGLSPEDIDYINA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 304 HGTATRLGDPVEVEALTDVFRDSTDTTgacLLGAVKGNIGHT-GAvSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELE 382
Cdd:cd00834 301 HGTSTPLNDAAESKAIKRVFGEHAKKV---PVSSTKSMTGHLlGA-AGAVEAIATLLALRDGVLPPTINLEEPDPECDLD 376
|
410 420 430
....*....|....*....|....*....|....*...
gi 753979669 383 AspfrVAAANEPWPDRgtrlAAVS-SFGVGGTNAHVLL 419
Cdd:cd00834 377 Y----VPNEAREAPIR----YALSnSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
7-415 |
1.45e-62 |
|
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: 219.20 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGISRFTPEWLLDQGadpdyvgrenfVPAMGVVTGsrrFDWPYFrYSRAEAAA 86
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLP-----------VRIAGEVKD---FDPEEY-LDRKELRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 87 MDPQQRVFLECATTAVDDAGIDPTRF-PGRIGVYAGADRVGPGAddplSELALYIGREKDF---------------LATR 150
Cdd:COG0304 68 MDRFTQYALAAAREALADAGLDLDEVdPDRTGVIIGSGIGGLDT----LEEAYRALLEKGPrrvspffvpmmmpnmAAGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 151 VAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS-----PDGRCRPFD 223
Cdd:COG0304 144 VSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAeaAITPLGLAG--FDALGALStrnddPEKASRPFD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 224 ERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDkMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEA 303
Cdd:COG0304 222 KDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYH-ITAPAPDGEGAARAMRAALKDAGLSPEDIDYINA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 304 HGTATRLGDPVEVEALTDVFRDSTDTTgacLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEA 383
Cdd:COG0304 301 HGTSTPLGDAAETKAIKRVFGDHAYKV---PVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDY 377
|
410 420 430
....*....|....*....|....*....|....
gi 753979669 384 SPfrvaaaNEPwpdRGTRL-AAVS-SFGVGGTNA 415
Cdd:COG0304 378 VP------NEA---REAKIdYALSnSFGFGGHNA 402
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
90-419 |
1.36e-55 |
|
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: 196.70 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 90 QQRVFLECATTAVDDAGIDPTRFPG-RIGVYAGA----DRVGPGADDPLSELALY--IGREKDFLATRVAYKLGLRGPAL 162
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNpIVGVVVGTgggsPRFQVFGADAMRAVGPYvvTKAMFPGASGQIATPLGIHGPAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 163 TVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGILSPDGRCRPFDERAGGTVPAEGVAVVVLKR 242
Cdd:cd00825 91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 243 LADALRDGDRIAGVIAGTAINNDGSDkMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGTATRLGDPVEVEALTDV 322
Cdd:cd00825 171 LEHALARGAHIYAEIVGTAATIDGAG-MGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 323 FRDSTDTtgaclLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASPFRvaaanepwpDRGTRL 402
Cdd:cd00825 250 FGDKSPA-----VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETT---------PRELRT 315
|
330
....*....|....*..
gi 753979669 403 AAVSSFGVGGTNAHVLL 419
Cdd:cd00825 316 ALLNGFGLGGTNATLVL 332
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
515-797 |
8.89e-49 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 176.09 E-value: 8.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 515 GKAAFLFPGQGTLRHGAGTAAYQLLPGFRAEFDEirkgVRDAHDIDLTPVVTDpADQDWFTDTVHQQLGLFALGYAFGRQ 594
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEE----ASEALGYDLSALCFE-GPEEELNLTENTQPAILAASVAAYRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 595 LRAWNIRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAM---WDTEPGLMVSV----AARADEVVPRLPGDGEVT 667
Cdd:COG0331 76 LEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMqeaVPAGPGGMAAVlgldDEEVEALCAEAAQGEVVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 668 VA-VEAPGSVVLSGPEAAMTEllAGDRLAGLG---TTLIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGR 743
Cdd:COG0331 156 IAnYNSPGQIVISGEKEAVEA--AAELAKEAGakrAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 753979669 744 qaapqEVTDPAYW----AAQLRRPVLLGEAMRTLLGSGCTTYVELGPGSSMIGGLRRT 797
Cdd:COG0331 234 -----PVTDPEEIrellVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRI 286
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-419 |
3.28e-44 |
|
"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: 166.08 E-value: 3.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 5 NAVAVVGMACRLP---GADDTAGYWAALTGGVDGISrftpewlldqgadpdyVGRENFVPAMGVVTGSRRFDWPyFRYSR 81
Cdd:cd00828 1 SRVVITGIGVVSPhgeGCDEVEEFWEALREGRSGIA----------------PVARLKSRFDRGVAGQIPTGDI-PGWDA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 82 AEAAAMDPQQRVFLECATTAVDDAGI-DPTRF-PGRIGVYAGADRVGP-----GADDPLSELALYIGREKDFLATRVA-- 152
Cdd:cd00828 64 KRTGIVDRTTLLALVATEEALADAGItDPYEVhPSEVGVVVGSGMGGLrflrrGGKLDARAVNPYVSPKWMLSPNTVAgw 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 153 ---YKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV-TVMPRGEWGYLFEQ---GGILSPDGRCRPFDER 225
Cdd:cd00828 144 vniLLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVeDPLEEGLSGFANMGalsTAEEEPEEMSRPFDET 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 226 AGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDKMAytAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHG 305
Cdd:cd00828 224 RDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSV--PAGGKGIARAIRTALAKAGLSLDDLDVISAHG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 306 TATRLGDPVEVEALTDVFrdsTDTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASP 385
Cdd:cd00828 302 TSTPANDVAESRAIAEVA---GALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVV 378
|
410 420 430
....*....|....*....|....*....|....
gi 753979669 386 FRVAAANEPWpdrgtRLAAVSSFGVGGTNAHVLL 419
Cdd:cd00828 379 GLSRDLNLKV-----RAALVNAFGFGGSNAALVL 407
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
255-373 |
1.82e-43 |
|
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: 153.88 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 255 GVIAGTAINNDGSDkMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGTATRLGDPVEVEALTDVFRDSTDtTGACL 334
Cdd:pfam02801 2 AVIKGSAVNHDGRH-NGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGAR-KQPLA 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 753979669 335 LGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFT 373
Cdd:pfam02801 80 IGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
26-419 |
2.95e-41 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 157.55 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 26 WAALTGGVDGISRFTPEWLLDQGADPDYVGRENFVPAMGVVTGSRrFDWPYFRYSRAEAAAMDPQQRVFLECAT-TAVDD 104
Cdd:PTZ00050 13 WEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMPCQIAAE-VDQSEFDPSDFAPTKRESRATHFAMAAArEALAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 105 AGIDPT--RFPGRIGVYAGadrVGPGADDPLSELALYIgREKDF---------------LATRVAYKLGLRGPALTVQTA 167
Cdd:PTZ00050 92 AKLDILseKDQERIGVNIG---SGIGSLADLTDEMKTL-YEKGHsrvspyfipkilgnmAAGLVAIKHKLKGPSGSAVTA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 168 CSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS------PDGRCRPFDERAGGTVPAEGVAVVV 239
Cdd:PTZ00050 168 CATGAHCIGEAFRWIKYGEADIMICGGTeaSITPVSFAG--FSRMRALCtkynddPQRASRPFDKDRAGFVMGEGAGILV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 240 LKRLADALRDGDRIAGVIAGTAINNDGSDkMAYTAPSVPGQSEVIRAAQR-IAGIDPADIDYVEAHGTATRLGDPVEVEA 318
Cdd:PTZ00050 246 LEELEHALRRGAKIYAEIRGYGSSSDAHH-ITAPHPDGRGARRCMENALKdGANININDVDYVNAHATSTPIGDKIELKA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 319 LTDVFRDSTDTTgaCLLGAVKGNIGHT-GAVSGVAGlIKTVLMLEHGQIVPTVHFTSPNPLLELEASPFRVAAANEpwpd 397
Cdd:PTZ00050 325 IKKVFGDSGAPK--LYVSSTKGGLGHLlGAAGAVES-IVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQ---- 397
|
410 420
....*....|....*....|..
gi 753979669 398 rGTRLAAVSSFGVGGTNAHVLL 419
Cdd:PTZ00050 398 -SIDAVLSTSFGFGGVNTALLF 418
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
519-797 |
2.34e-38 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 146.46 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 519 FLFPGQGTLRHGAGTAAYQLLPGFRAEFDEIRKGVRDAHDIDLTPVVTDPaDQDWFTDTVHQQLGLFALGYAFGRQLRAW 598
Cdd:pfam00698 2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNN-PEGTLDGTQFVQPALFAMQIALAALLQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 599 NIRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAMWD-TEPGLMVSVAARADEVVPRLPgDGEVTVAVEAPGSVV 677
Cdd:pfam00698 81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQlAGPGGMAAVELSAEEVEQRWP-DDVVGAVVNSPRSVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 678 LSGPEAAMTELLAGDRLAGLGTTLIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGRQAAPQEVtDPAYWA 757
Cdd:pfam00698 160 ISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTL-SAEYWV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 753979669 758 AQLRRPVLLGEAMRTLLGSGCTTYVELGPGSSMIGGLRRT 797
Cdd:pfam00698 239 RNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDT 278
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
80-415 |
8.24e-36 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 141.46 E-value: 8.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 80 SRAEAAAMDPQQRVFLECATTAVDDAGIDPTRF-PGRIGVY--------------------AGADRVGPgaddplselaL 138
Cdd:PRK07314 62 SRKEARRMDRFIQYGIAAAKQAVEDAGLEITEEnADRIGVIigsgiggletieeqhitlleKGPRRVSP----------F 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 139 YI-GREKDFLATRVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS- 214
Cdd:PRK07314 132 FVpMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAeaAITPLGIAG--FAAARALSt 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 215 ----PDGRCRPFDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDgsdkmAY--TAPSVPGQSEV--IRA 286
Cdd:PRK07314 210 rnddPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGD-----AYhmTAPAPDGEGAAraMKL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 287 AQRIAGIDPADIDYVEAHGTATRLGDPVEVEALTDVFRDSTDTTgacLLGAVKGNIGHT-GAVSGVAGlIKTVLMLEHGQ 365
Cdd:PRK07314 285 ALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKV---AVSSTKSMTGHLlGAAGAVEA-IFSVLAIRDQV 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 753979669 366 IVPTVHFTSPNPLLELEaspfrvAAANEPwPDRGTRLAAVSSFGVGGTNA 415
Cdd:PRK07314 361 IPPTINLDNPDEECDLD------YVPNEA-RERKIDYALSNSFGFGGTNA 403
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
90-419 |
1.00e-33 |
|
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: 130.64 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 90 QQRVFLECATTAVDDAGIDPTRFPGRIGVYAGADRVGPGAddplselalyigrekdflATRVAYKLGLR-GPALTVQTAC 168
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGA------------------AGQLAYHLGISgGPAYSVNQAC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 169 STSLTAVHLAARALVGGECDAALAGGVTVMPRGewgylfeqggilspdgrcrpfderaggtvpaEGVAVVVLKRLADALR 248
Cdd:cd00327 69 ATGLTALALAVQQVQNGKADIVLAGGSEEFVFG-------------------------------DGAAAAVVESEEHALR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 249 DGDRIAGVIAGTAINNDGSDkmAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGTATRLGDPVEVEALTDVFRDstd 328
Cdd:cd00327 118 RGAHPQAEIVSTAATFDGAS--MVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGV--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 329 ttGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTvhftspnplleleaspfrvaaanepwpDRGTRLAAVSSF 408
Cdd:cd00327 193 --RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------------------PREPRTVLLLGF 243
|
330
....*....|.
gi 753979669 409 GVGGTNAHVLL 419
Cdd:cd00327 244 GLGGTNAAVVL 254
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
92-419 |
1.35e-32 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 131.69 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 92 RVFLECATTAVDDAGIDPTRfPGRIGVYAGADRVGPG---------ADDPLSELALYIGREKD-FLATRVAYKLGLRGPA 161
Cdd:PRK07103 82 QAALAAAREAWRDAALGPVD-PDRIGLVVGGSNLQQReqalvhetyRDRPAFLRPSYGLSFMDtDLVGLCSEQFGIRGEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 162 LTVQTACSTSLTAVHLAARALVGGECDAALAGGvTVMPRGEW--------GYLFEQGGILSPDGRCRPFDERAGGTVPAE 233
Cdd:PRK07103 161 FTVGGASASGQLAVIQAARLVQSGSVDACIAVG-ALMDLSYWecqalrslGAMGSDRFADEPEAACRPFDQDRDGFIYGE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 234 GVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDKmayTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGTATRLGDP 313
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRLDANRG---PDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 314 VEVEALTDVfrdstdTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSP-NPLLEL---EASPFRVa 389
Cdd:PRK07103 317 TELAALFAS------GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFRWvgsTAESARI- 389
|
330 340 350
....*....|....*....|....*....|
gi 753979669 390 aanepwpdrgtRLAAVSSFGVGGTNAHVLL 419
Cdd:PRK07103 390 -----------RYALSLSFGFGGINTALVL 408
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
7-423 |
1.66e-32 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 132.06 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLP---GADDTagyWAALTGGVDG---ISRFTPEWLLDQGAdpdyvGRENFVPAMgvvtgsrrfdwPYFRYS 80
Cdd:PRK06501 13 VAVTGMGVVTSlgqGKADN---WAALTAGESGihtITRFPTEGLRTRIA-----GTVDFLPES-----------PFGASA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 81 RAEAAAMdpqqrvflECATTAVDDAGIDPTRFPGRIGVYAGA-----------DRVGPGADDPLSELALYIGREKDF--- 146
Cdd:PRK06501 74 LSEALAR--------LAAEEALAQAGIGKGDFPGPLFLAAPPvelewparfalAAAVGDNDAPSYDRLLRAARGGRFdal 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 147 --------LATRVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPrgEWGYLFEQGGILS-- 214
Cdd:PRK06501 146 herfqfgsIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATdgSVSA--EALIRFSLLSALStq 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 215 ---PDGRCRPFDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAinnDGSDKMAYTAPSVPGQS--EVIRAAQR 289
Cdd:PRK06501 224 ndpPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCG---EKADSFHRTRSSPDGSPaiGAIRAALA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 290 IAGIDPADIDYVEAHGTATRLGDPVEVEALTDVFRDSTDTTGaclLGAVKGNIGHT----GAVSGVAGLiktvLMLEHGQ 365
Cdd:PRK06501 301 DAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIP---VSSNKSMIGHTltaaGAVEAVFSL----LTIQTGR 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 366 IVPTVHFTSPNPLLELEASPfRVAaanepwpdRGTRLAAV--SSFGVGGTNAHVLLQGAP 423
Cdd:PRK06501 374 LPPTINYDNPDPAIPLDVVP-NVA--------RDARVTAVlsNSFGFGGQNASLVLTAEP 424
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
99-421 |
4.01e-32 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 129.79 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 99 TTAVDDAGIDP-----------TR-FPGRIGVYAGADRVGPGADDPLSELALYIGREKDFLATRVAYKLGLRGPALTVQT 166
Cdd:PRK05952 65 TAALKDAGLTPpltdcgvvigsSRgCQGQWEKLARQMYQGDDSPDEELDLENWLDTLPHQAAIAAARQIGTQGPVLAPMA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 167 ACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILSPDGrCRPFDERAGGTVPAEGVAVVVLKRLA 244
Cdd:PRK05952 145 ACATGLWAIAQGVELIQTGQCQRVIAGAVeaPITPLTLAG--FQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 245 DALRDGDRIAGVIAGTAINNDGsDKMayTAPSVPGQSeVIRAAQRI---AGIDPADIDYVEAHGTATRLGDPVE---VEA 318
Cdd:PRK05952 222 LAQKRGAKIYGQILGFGLTCDA-YHM--SAPEPDGKS-AIAAIQQClarSGLTPEDIDYIHAHGTATRLNDQREanlIQA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 319 L--TDVFRDSTdttgacllgavKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASPfrvaaanepwp 396
Cdd:PRK05952 298 LfpHRVAVSST-----------KGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA----------- 355
|
330 340
....*....|....*....|....*..
gi 753979669 397 dRGTRLAAV--SSFGVGGTNAHVLLQG 421
Cdd:PRK05952 356 -QQSPLQNVlcLSFGFGGQNAAIALGK 381
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
148-423 |
7.69e-31 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 127.22 E-value: 7.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 148 ATRVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS------PDGRC 219
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTesSIDALSIAG--FSRSRALStkfnscPTEAS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 220 RPFDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDkmaYTAPSVPGQSEV--IRAAQRIAGIDPAD 297
Cdd:PLN02836 242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH---ITQPHEDGRGAVlaMTRALQQSGLHPNQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 298 IDYVEAHGTATRLGDPVEVEALTDVFRDSTdTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNP 377
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHA-TSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP 397
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 753979669 378 LLELEASPFRVAAANEpwpdrgTRLAAVSSFGVGGTNAHVLLQGAP 423
Cdd:PLN02836 398 IFDDGFVPLTASKAML------IRAALSNSFGFGGTNASLLFTSPP 437
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
7-419 |
5.26e-28 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 118.56 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGISRFTPEWLLDQGADpdyVGrenfvpamGVVTGSRRFDWPYF---RY-SRA 82
Cdd:PRK06333 6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATK---IG--------GQVPDLAEDAEAGFdpdRYlDPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 83 EAAAMDPQQRVFLECATTAVDDAGIDPTRFPG--RIGVYAGADRVGPGADDPLSELALYIGREK-------DFL----AT 149
Cdd:PRK06333 75 DQRKMDRFILFAMAAAKEALAQAGWDPDTLEDreRTATIIGSGVGGFPAIAEAVRTLDSRGPRRlspftipSFLtnmaAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 150 RVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGYL----FEQGGILSPDGRCRPFD 223
Cdd:PRK06333 155 HVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTeaAIDRVSLAGFAaaraLSTRFNDAPEQASRPFD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 224 ERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDgsdkmAYTAPSVP----GQSEVIRAAQRIAGIDPADID 299
Cdd:PRK06333 235 RDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSAD-----AYHMTAGPedgeGARRAMLIALRQAGIPPEEVQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 300 YVEAHGTATRLGDPVEVEALTDVFrdstDTTGACLLGAVKGNIGHT-GAVSGVAGlIKTVLMLEHGQIVPTVHFTSPNPL 378
Cdd:PRK06333 310 HLNAHATSTPVGDLGEVAAIKKVF----GHVSGLAVSSTKSATGHLlGAAGGVEA-IFTILALRDQIAPPTLNLENPDPA 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 753979669 379 LE-LEAspfrVAAANEPWPdrgTRLAAVSSFGVGGTNAHVLL 419
Cdd:PRK06333 385 AEgLDV----VANKARPMD---MDYALSNGFGFGGVNASILF 419
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
375-1213 |
9.53e-28 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 121.35 E-value: 9.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 375 PNPLLELEASPFRVAAANEPWPDRGTRLAAVSSFGVGGTNAHVLLQGAPSRAPRKGRPGFHPLTLSAASPDALGRLAGAL 454
Cdd:COG3319 3 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 455 ADRLEPATAGEAAPTLAEVSRTLAERRVHRHRKALVAAEPAVAARLLRGAAEPGPPRRKLGKAAFLFPGQGTLRHGAGTA 534
Cdd:COG3319 83 ALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 535 AYQLLPGFRAEFDEIRKGVRDAHDIDLTPVVTDPADQDWFTDTVHQQLGLFALGYAFGRQLRAWNIRPAAMLGNSIGEYV 614
Cdd:COG3319 163 VLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 615 AAALAGVWSPQDAADLVHRRARAMWDTEPGLMVSVAARADEVVPRLPGDGEVTVAVEAPGSVVLSGPEAAMTELLAGDRL 694
Cdd:COG3319 243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 695 AGLGTTLIHTRrafhskamDGAAEEVRAAISSMPVRPPRQPLISGTTGRQAAPQEVTDPAYWAAQLRRPVLLGEAMRTLL 774
Cdd:COG3319 323 GLLVLLVLLVL--------LLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 775 GSGCTTYVELGPGSSMIGGLRRTPGWDSSFAAVPLTARREDPAEAGLLNALATLWELGADRALEDVLGTAPGAGEERPSR 854
Cdd:COG3319 395 LLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 855 CSLPGYQFRGEDPEQTDAAAPPAPAARRAPAAAPARTADTRAVLAELWCRTLGVPVALDDDSFFALGGESLMAVSLTAQV 934
Cdd:COG3319 475 ALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 935 RELTGCVLSVTDFSRAPSFGRLVETVERQSPARPAPAatgtlpvpgVATLTEGGTGRPVFLVADATGTALPYRHLAALLA 1014
Cdd:COG3319 555 LALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSP---------LVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALG 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1015 PlaaNRPVLGLEDPG----GPRTRTIPAIAADHVTALLRTQPEGPYTLGGWSFGAVVAHEMAYRLTRLGKRVDLLVCLDG 1090
Cdd:COG3319 626 P---DRPVYGLQAPGldggEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDS 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1091 FVPDT------------------GGRPVSFAPEFLR-----AGLRSQAEALLGIG-PVARRLGRATALRRQFVANQATLL 1146
Cdd:COG3319 703 YAPGAlarldeaellaallrdlaRGVDLPLDAEELRaldpeERLARLLERLREAGlPAGLDAERLRRLLRVFRANLRALR 782
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 753979669 1147 RYRPRPVACPVVLFKAS-SGPAEADRLRGRLSGLYGDGVRVEPVGGDHWSMLTGPYADELALKLAHAL 1213
Cdd:COG3319 783 RYRPRPYDGPVLLFRAEeDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAAL 850
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
95-418 |
4.06e-27 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 115.60 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 95 LECATTAVDDAGIDPTRF-PGRIGVYAGA---------------DRVGPGADDPL---SELAlyigrekDFLATRVAYKL 155
Cdd:PRK08439 77 LKAAREAMKDAGFLPEELdAERFGVSSASgigglpnieknsiicFEKGPRKISPFfipSALV-------NMLGGFISIEH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 156 GLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS-----PDGRCRPFDERAGG 228
Cdd:PRK08439 150 GLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAesAICPVGIGG--FAAMKALStrnddPKKASRPFDKDRDG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 229 TVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDkmaYTAPSVPGQSEVIRAAQRIAGIDPadIDYVEAHGTAT 308
Cdd:PRK08439 228 FVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANH---ITSPAPEGPLRAMKAALEMAGNPK--IDYINAHGTST 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 309 RLGDPVEVEALTDVFRDSTDTTgacLLGAVKGNIGHtgaVSGVAGLIKTV--LM-LEHGQIVPTVHFTSPNPLLELEASP 385
Cdd:PRK08439 303 PYNDKNETAALKELFGSKEKVP---PVSSTKGQIGH---CLGAAGAIEAVisIMaMRDGILPPTINQETPDPECDLDYIP 376
|
330 340 350
....*....|....*....|....*....|....*
gi 753979669 386 frvaaaNEPwpdRGTRLAAV--SSFGVGGTNAHVL 418
Cdd:PRK08439 377 ------NVA---RKAELNVVmsNSFGFGGTNGVVI 402
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
157-420 |
3.86e-25 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 109.38 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 157 LRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGvtvmprGE---W--GYLFEQGGILS------PDGRCRPFDER 225
Cdd:PRK07967 151 IKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGG------GEeldWemSCLFDAMGALStkyndtPEKASRAYDAN 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 226 AGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDKMAytaPSVPGQSEVIRAAqrIAGIDpADIDYVEAHG 305
Cdd:PRK07967 225 RDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA---PSGEGAVRCMQMA--LATVD-TPIDYINTHG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 306 TATRLGDPVEVEALTDVFRDSTDTtgaclLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPllELEASP 385
Cdd:PRK07967 299 TSTPVGDVKELGAIREVFGDKSPA-----ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP--QAAGMP 371
|
250 260 270
....*....|....*....|....*....|....*
gi 753979669 386 FrvaaANEPWPDRGTRLAAVSSFGVGGTNAHVLLQ 420
Cdd:PRK07967 372 I----VTETTDNAELTTVMSNSFGFGGTNATLVFR 402
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
7-420 |
4.12e-25 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 109.71 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 7 VAVVGMACRLPGADDTAGYWAALTGGVDGISRFtpewlldqgadpDYVGRENFVPAM-GVVTGsrrFDWPYFrYSRAEAA 85
Cdd:PRK08722 6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNI------------EHFDTTNFSTRFaGLVKD---FNCEEY-MSKKDAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 86 AMDPQQRVFLECATTAVDDAGIDPTR-FPGRIGVYAGADRVGPGADDPLSELALYIGREK-----------DFLATRVAY 153
Cdd:PRK08722 70 KMDLFIQYGIAAGIQALDDSGLEVTEeNAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKvspffvpstivNMIAGNLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 154 KLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV--TVMPRGEWGylFEQGGILS-----PDGRCRPFDERA 226
Cdd:PRK08722 150 MRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAekASTPLGMAG--FGAAKALStrndePQKASRPWDKDR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 227 GGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSdKMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAHGT 306
Cdd:PRK08722 228 DGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAY-HMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 307 ATRLGDPVEVEALTDVFrdSTDTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEASPF 386
Cdd:PRK08722 307 STPAGDVAEIKGIKRAL--GEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPH 384
|
410 420 430
....*....|....*....|....*....|....
gi 753979669 387 RVAAAnepwpdRGTRLAAVSSFGVGGTNAHVLLQ 420
Cdd:PRK08722 385 TARKV------ESMEYAICNSFGFGGTNGSLIFK 412
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
484-796 |
1.75e-24 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 106.39 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 484 RHRKALVAAEPAVAARLLRGAAEPGPPRRKLGKAAFLFPGQGTLRHGAGTAAyQLLPGFRAEFDEirkgvrdAHDI---D 560
Cdd:PLN02752 7 AARRASASRVSMSVSVGSQATAADALFADYKPTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDK-------ASEIlgyD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 561 LTPVVTD-PADQdwFTDTVHQQLGLFALGYAFGRQLRAWNIRPAAM------LGNSIGEYVAAALAGVWSPQDAADLVHR 633
Cdd:PLN02752 79 LLDVCVNgPKEK--LDSTVVSQPAIYVASLAAVEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 634 RARAMW---DTEPGLMVSVAARADEVVPRL--------PGDGEVTVA-VEAPGSVVLSGPEAAMTELLAGDRLAG-LGTT 700
Cdd:PLN02752 157 RGEAMQaaaDAGPSGMVSVIGLDSDKVQELcaaaneevGEDDVVQIAnYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 701 LIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGrqaapQEVTDPA----YWAAQLRRPVLLGEAMRTLLGS 776
Cdd:PLN02752 237 RLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVDA-----QPHSDPAtikkILARQVTSPVQWETTVKTLLEK 311
|
330 340
....*....|....*....|
gi 753979669 777 GCTTYVELGPGSSMIGGLRR 796
Cdd:PLN02752 312 GLEKSYELGPGKVIAGIVKR 331
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
145-419 |
1.78e-24 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 107.24 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 145 DFLAtrvAYkLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGV------TVmprgewgYLFEQGGILSPdGR 218
Cdd:PRK09185 141 DFLR---AY-LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVdslcrlTL-------NGFNSLESLSP-QP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 219 CRPFD-ERAGGTVpAEGVAVVVLKRLADalrDGDRIAGViagtainNDGSDKMAYTAPSvP---GQSEVIRAAQRIAGID 294
Cdd:PRK09185 209 CRPFSaNRDGINI-GEAAAFFLLEREDD---AAVALLGV-------GESSDAHHMSAPH-PeglGAILAMQQALADAGLA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 295 PADIDYVEAHGTATRLGDPVEVEALTDVFRDSTDTTGAcllgavKGNIGHT-GAvsgvAGLIKTV---LMLEHGQIVPTV 370
Cdd:PRK09185 277 PADIGYINLHGTATPLNDAMESRAVAAVFGDGVPCSST------KGLTGHTlGA----AGAVEAAicwLALRHGLPPHGW 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 753979669 371 HFTSPNPLLELEAspfRVAAANEpwpdRGTRLAAVSSFGVGGTNAHVLL 419
Cdd:PRK09185 347 NTGQPDPALPPLY---LVENAQA----LAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
71-420 |
1.78e-23 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 103.27 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 71 RFDWPYFRYSRAEAAAMDPQQRvflecaTTAVDDAGIDPtrFPGRIGVYAGADRVGPGADDPLSELALYIgrekDFLATR 150
Cdd:PRK14691 6 RYKWITFHPSLTHADNTEKQER------TATIIGAGIGG--FPAIAHAVRTSDSRGPKRLSPFTVPSFLV----NLAAGH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 151 VAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGILS------PDGRCRPFDE 224
Cdd:PRK14691 74 VSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSthfnstPEKASRPFDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 225 RAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSdKMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEAH 304
Cdd:PRK14691 154 ARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAY-HMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 305 GTATRLGDPVEVEALTDVFRDSTdttgACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHgQIVP-TVHFTSPNPllelEA 383
Cdd:PRK14691 233 ATSTPVGDLGEINAIKHLFGESN----ALAITSTKSATGHLLGAAGGLETIFTVLALRD-QIVPaTLNLENPDP----AA 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 753979669 384 SPFRVAAANEPWPDRGTRLAavSSFGVGGTNAHVLLQ 420
Cdd:PRK14691 304 KGLNIIAGNAQPHDMTYALS--NGFGFAGVNASILLK 338
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
894-1095 |
2.14e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 107.82 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 894 TRAVLAELWCRTLGVPVALDDDSFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVERQSPARPAPAAT 973
Cdd:PRK10252 979 TETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFG 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 974 GTLPvpgvatLTEGgTGRPVFLVADATGTALPYRhlaALLAPLAANRPVLGLEDP--GGP--RTRTIPAIAADHVTALLR 1049
Cdd:PRK10252 1059 TILP------LREG-DGPTLFCFHPASGFAWQFS---VLSRYLDPQWSIYGIQSPrpDGPmqTATSLDEVCEAHLATLLE 1128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 753979669 1050 TQPEGPYTLGGWSFGAVVAHEMAYRLTRLGKRVDLLVCLDGFVPDT 1095
Cdd:PRK10252 1129 QQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPET 1174
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
518-790 |
6.88e-23 |
|
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.
Pssm-ID: 132175 Cd Length: 295 Bit Score: 100.46 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 518 AFLFPGQGTLRHGAgtaayqllpgfraeFDEIRKGVRDAHDIDLTPVVTDPADQDWFTD-----TVHQQLGLFALGYAFG 592
Cdd:TIGR03131 2 ALLFPGQGSQRAGM--------------LAELPDHPAVAAVLAEASDVLGIDPRELDDAealasTRSAQLCILAAGVAAW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 593 RQLRAWNIRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAM---WDTEPGLMVSVAARADEVVPRLPGDGEVTVA 669
Cdd:TIGR03131 68 RALLALLPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMdqaVPGGYGMLAVLGLDLAAVEALIAKHGVYLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 670 VEAPGSVVLSGPEAAMTELLAGDRLAGLG-TTLIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGRQA--A 746
Cdd:TIGR03131 148 INAPDQVVIAGSRAALRAVAELARAAGASrAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVrdA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 753979669 747 PQEVTDpayWAAQLRRPVLLGEAMRTLLGSGCTTYVELGPGSSM 790
Cdd:TIGR03131 228 AQIRDD---LARQIATPVDWHDCMQAAYERGARLVIELGPGDVL 268
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
148-414 |
1.23e-22 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 102.12 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 148 ATRVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEWGYLFEQGGIL------SPDGRCRP 221
Cdd:PRK07910 151 AAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVmstnndDPAGACRP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 222 FDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDkMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYV 301
Cdd:PRK07910 231 FDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFH-MVAPDPNGERAGHAMTRAIELAGLTPGDIDHV 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 302 EAHGTATRLGDPVEVEALTDVFrdstdTTGACLLGAVKGNIGHT-GAVSGVAGLIkTVLMLEHGQIVPTVHFTSPNPLLE 380
Cdd:PRK07910 310 NAHATGTSVGDVAEGKAINNAL-----GGHRPAVYAPKSALGHSvGAVGAVESIL-TVLALRDGVIPPTLNLENLDPEID 383
|
250 260 270
....*....|....*....|....*....|....
gi 753979669 381 LEaspfrvAAANEPWPDRgTRLAAVSSFGVGGTN 414
Cdd:PRK07910 384 LD------VVAGEPRPGN-YRYAINNSFGFGGHN 410
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
516-797 |
2.61e-20 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 92.92 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 516 KAAFLFPGQGTLRHGAGTAAYQLLPGFRAEFDEirkgVRDAHDIDLTPVVTDpADQDWFTDTVHQQLGLFALGYAFGRQL 595
Cdd:TIGR00128 2 KIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQ----ASEALGYDLKKLCQE-GPAEELNKTQYTQPALYVVSAILYLKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 596 R-AWNIRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAMWDTEP---GLMVSVAARADEVVPRLPGDGE---VTV 668
Cdd:TIGR00128 77 KeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPeggGAMAAVIGLDEEQLAQACEEATendVDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 669 A-VEAPGSVVLSGPEAAMTELLAGDRLAGLGTTL-IHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTgrqAA 746
Cdd:TIGR00128 157 AnFNSPGQVVISGTKDGVEAAAALFKEMGAKRAVpLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVD---AK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 753979669 747 PQEVTDPA--YWAAQLRRPVLLGEAMRTLLGSGCTTYVELGPGSSMIGGLRRT 797
Cdd:TIGR00128 234 PYTNGDRIkeKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRI 286
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
79-377 |
3.31e-20 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 94.67 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 79 YSRAEAAAMDPQQRVFLECATTAVDDAGI--DPTRFPGRIGVYAGADrvgPGADDPLSELA--LYIGREKDFLAT----- 149
Cdd:PRK09116 62 YTRKKIRSMGRVSLMATRASELALEDAGLlgDPILTDGRMGIAYGSS---TGSTDPIGAFGtmLLEGSMSGITATtyvrm 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 150 -------RVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEwGYLFEQGGILS-----PDG 217
Cdd:PRK09116 139 mphttavNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTE-AAVFDTLFATStrndaPEL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 218 RCRPFDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSDkmaYTAPSVPGQSEVIRAAQRIAGIDPAD 297
Cdd:PRK09116 218 TPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH---VTQPQAETMQIAMELALKDAGLAPED 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 298 IDYVEAHGTATRLGDPVEVEALTDVFRDSTDTTgacllgAVKGNIGHTgavSGVAGLIK---TVLMLEHGQIVPTVHFTS 374
Cdd:PRK09116 295 IGYVNAHGTATDRGDIAESQATAAVFGARMPIS------SLKSYFGHT---LGACGALEawmSIEMMNEGWFAPTLNLTQ 365
|
...
gi 753979669 375 PNP 377
Cdd:PRK09116 366 VDP 368
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
6-419 |
4.07e-20 |
|
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: 94.35 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 6 AVAVVGMACRLPGADDTAGYWAALTGGVDGI---SRFTPEWLLDQ--GADPDYVGREN----FVPAMGVVTgsrrfdwpy 76
Cdd:cd00832 2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLgpiTRFDPSGYPARlaGEVPDFDAAEHlpgrLLPQTDRMT--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 77 fRYSRAEAAAmdpqqrvflecattAVDDAGIDPTRFPG-RIGVYAGAdrVGPGADDPLSELALYIGREKDFLAT------ 149
Cdd:cd00832 73 -RLALAAADW--------------ALADAGVDPAALPPyDMGVVTAS--AAGGFEFGQRELQKLWSKGPRHVSAyqsfaw 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 150 -------RVAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECdAALAGGVTVmPRGEWGYLFE-QGGILS----PDG 217
Cdd:cd00832 136 fyavntgQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTP-LVVSGGVDS-ALCPWGWVAQlSSGRLStsddPAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 218 RCRPFDERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGsdkmAYTAPSVPGQSEVIRAAQRIAGIDPAD 297
Cdd:cd00832 214 AYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDP----PPGSGRPPGLARAIRLALADAGLTPED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 298 IDYVEAHGTATRLGDPVEVEALTDVFrdstdTTGACLLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNP 377
Cdd:cd00832 290 VDVVFADAAGVPELDRAEAAALAAVF-----GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPP 364
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 753979669 378 LLELEASPFRVAAAnepwpdrGTRLAAVSSFGVGGTNAHVLL 419
Cdd:cd00832 365 AYGLDLVTGRPRPA-------ALRTALVLARGRGGFNSALVV 399
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
151-419 |
8.99e-18 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 88.50 E-value: 8.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 151 VAYKLGLRGPALTVQTACSTSLTAVHLAARALVGGECDAALAGG--VTVMPRGEWGYLFEQGgiLS-----PDGRCRPFD 223
Cdd:PLN02787 274 LAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGsdAAIIPIGLGGFVACRA--LSqrnddPTKASRPWD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 224 ERAGGTVPAEGVAVVVLKRLADALRDGDRIAGVIAGTAINNDGSdKMAYTAPSVPGQSEVIRAAQRIAGIDPADIDYVEA 303
Cdd:PLN02787 352 MNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAY-HMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 304 HGTATRLGDPVEVEALTDVFRDSTDTTgaclLGAVKGNIGHTGAVSGVAGLIKTVLMLEHGQIVPTVHFTSPNPLLELEa 383
Cdd:PLN02787 431 HATSTKAGDLKEYQALMRCFGQNPELR----VNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK- 505
|
250 260 270
....*....|....*....|....*....|....*.
gi 753979669 384 spFRVAAANEpwpDRGTRLAAVSSFGVGGTNAHVLL 419
Cdd:PLN02787 506 --VLVGPKKE---RLDIKVALSNSFGFGGHNSSILF 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
893-1135 |
8.58e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.21 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 893 DTRAVLAELWCRTLGVPVALDDDSFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVE----RQSPARP 968
Cdd:PRK12467 3605 EVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPlgdvPVNLLLD 3684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 969 APAATGTLPVpgvatlteggtgrpVFLVADATGTALPYRhlaALLAPLAANRPVLGLE-----DPGGPRTRtIPAIAADH 1043
Cdd:PRK12467 3685 LNRLETGFPA--------------LFCRHEGLGTVFDYE---PLAVILEGDRHVLGLTcrhllDDGWQDTS-LQAMAVQY 3746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1044 VTALLRTQPEGPYTLGGWSFGAVVAHEMAYRLTRLGKRVDLLVCLDGFVPdtggRPVSFAPEFLRAGLRSQAEALLGIgp 1123
Cdd:PRK12467 3747 ADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTLP----LPDEFVPQAEFLELLRQLGELIGR-- 3820
|
250
....*....|..
gi 753979669 1124 vARRLGRATALR 1135
Cdd:PRK12467 3821 -ANRLLRGLEEG 3831
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
375-461 |
2.21e-14 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 70.27 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 375 PNPLLE-LEASPFRVAAANEPWPDRgtrLAAVSSFGVGGTNAHVLLQGAPS--RAPRKGRPGFHPLTLSAASPDALGRLA 451
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWPGG---IVGVNSFGFGGANAHVILKSNPKpkIPPESPDNLPRLVLLSGRTEEAVKALL 77
|
90
....*....|
gi 753979669 452 GALADRLEPA 461
Cdd:pfam16197 78 EKLENHLDDA 87
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
991-1105 |
5.09e-13 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 69.72 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 991 RPVFLVADATGTALPYRHLAALLAPLAanrPVLGLEDPG----GPRTRTIPAIAADHVTALLRTQPEGPYTLGGWSFGAV 1066
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPPA---EVLAVQYPGrgrgEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGM 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 753979669 1067 VAHEMAYRLTRLGKRVDLLVCLDGFVPDTGGRPVSFAPE 1105
Cdd:pfam00975 78 LAFEVARRLERQGEAVRSLFLSDASAPHTVRYEASRAPD 116
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
892-963 |
2.84e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 57.56 E-value: 2.84e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 753979669 892 ADTRAVLAELWCRTLGVPVAL--DDDSFFA-LGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVERQ 963
Cdd:COG0236 4 EELEERLAEIIAEVLGVDPEEitPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
896-952 |
8.33e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 55.65 E-value: 8.33e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 753979669 896 AVLAELWCRTLGVPVA--LDDDSFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPS 952
Cdd:pfam00550 1 ERLRELLAEVLGVPAEeiDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1027-1206 |
3.25e-09 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 58.39 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1027 DPGGPRTRTIPAIAADHVTALLRTQPEGPYTLGGWSFGAVVAHEMAYRLTRLGKRVDLLVCLDGFVPDTGgrpvsfAPEF 1106
Cdd:smart00824 37 GPGEPLPASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDTYPPGDP------APEG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1107 LRAGLRSQAEALLGiGPVARRLGRATALRRQFVAnqatLLRYRPRPVACPVVLFKASSGPAE--ADRLRGRLSGLYGDGV 1184
Cdd:smart00824 111 WLPELLRGVFERED-SFVPMDDARLTAMGAYLRL----FGGWTPGPVAAPTLLVRASEPLAEwpDEDPDGWRAHWPLPHT 185
|
170 180
....*....|....*....|..
gi 753979669 1185 RVEpVGGDHWSMLTGpYADELA 1206
Cdd:smart00824 186 VVD-VPGDHFTMMEE-HAAATA 205
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
95-232 |
6.85e-08 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 56.12 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 95 LECATTAVDDAGIDPTRfpgrigvyAGADRVGPGADdplselalyiGREKDFLATRVAYKLGLRG-PALTVQTACSTSLT 173
Cdd:cd00829 21 AEAARAALDDAGLEPAD--------IDAVVVGNAAG----------GRFQSFPGALIAEYLGLLGkPATRVEAAGASGSA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 753979669 174 AVHLAARALVGGECDAALAGGVTVMPRGEWGYLFeqGGILSPdgRCRPFDERAGGTVPA 232
Cdd:cd00829 83 AVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEA--GGRASD--LEWEGPEPPGGLTPP 137
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
101-205 |
2.32e-07 |
|
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: 54.69 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 101 AVDDAGIDPtrfpGRIG-VYAGAdrVGPGADDPlselalYIGREkdflatrVAYKLGL--RGPALTVQTACSTSLTAVHL 177
Cdd:COG0183 37 LLERAGLDP----EAVDdVILGC--VLQAGQGQ------NPARQ-------AALLAGLpeSVPAVTVNRVCGSGLQAVAL 97
|
90 100 110
....*....|....*....|....*....|....*
gi 753979669 178 AARALVGGECDAALAGGVTVM-------PRGEWGY 205
Cdd:COG0183 98 AAQAIAAGDADVVIAGGVESMsrapmllPKARWGY 132
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
387-901 |
3.13e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 55.26 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 387 RVAAANEPWPDRGTRLAAVSSFGVGGTNAHVLLQGAPSRAPRKGRPGFHPLTLSAASPDALGRLAGALADRLEPATAGEA 466
Cdd:COG3321 860 RVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 467 APTLAEVSRTLAERRVHRHRKALVAAEPAVAARLLRGAAEPGPPRRKLGKAAFLFPGQGTLRHGAGTAAYQLLPGFRAEF 546
Cdd:COG3321 940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 547 DEIRKGVRDAHDIDLTPVVTDPADQDWFTDTVHQQLGLFALGYAFGRQLRAWNIRPAAMLGNSIGEYVAAALAGVWSPQD 626
Cdd:COG3321 1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 627 AADLVHRRARAMWDTEPGLMVSVAARADEVVPRLPGDGEVTVAVEAPGSVVLSGPEAAMTELLAGDRLAGLGTTLIHTRR 706
Cdd:COG3321 1100 AALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 707 AFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGRQAAPQEVTDPAYWAAQLRRPVLLGEAMRTLLGSGCTTYVELGP 786
Cdd:COG3321 1180 ALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAAL 1259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 787 GSSMIGGLRRTPGWDSSFAAVPLTARREDPAEAGLLNALATLWELGADRALEDVLGTAPGAGEERPSRCSLPGYQFRGED 866
Cdd:COG3321 1260 AALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAA 1339
|
490 500 510
....*....|....*....|....*....|....*
gi 753979669 867 PEQTDAAAPPAPAARRAPAAAPARTADTRAVLAEL 901
Cdd:COG3321 1340 ALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAA 1374
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
160-236 |
5.36e-07 |
|
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: 53.25 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 160 PALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVM-------PRGEWGYLfeqGGILSPDGRCRPFDERAGGTVP- 231
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMsrapyllPKARRGGR---LGLNTLDGMLDDGLTDPFTGLSm 152
|
....*...
gi 753979669 232 ---AEGVA 236
Cdd:cd00751 153 gitAENVA 160
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
893-977 |
3.32e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.71 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 893 DTRAVLAELWCRTLGVPVALDDDSFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVER-QSPARPAPA 971
Cdd:PRK05691 586 ELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARqLAGGGAAQA 665
|
....*.
gi 753979669 972 ATGTLP 977
Cdd:PRK05691 666 AIARLP 671
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
588-1120 |
2.56e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 48.72 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 588 GYAFGRQLRAWNIRPAAMLGNSIGEYVAAALAGVWSPQDAADLVHRRARAmwdtepglmvsVAARADEVVPRLPGDGEVT 667
Cdd:COG3321 865 TYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAA-----------AAAALALAAAALAALLALV 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 668 VAVEAPGSVVLSGPEAAMTELLAGDRLAGLGTTLIHTRRAFHSKAMDGAAEEVRAAISSMPVRPPRQPLISGTTGRQAAP 747
Cdd:COG3321 934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 748 QEVTDPAYWAAQLRRPVLLGEAMRTLLGSGCTTYVELGPGSSMIGGLRRTPGWDSSFAAVPLTARREDPAEAGLLnALAT 827
Cdd:COG3321 1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAA-ALAA 1092
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 828 LWELGADRALEDVLGTAPGAGEERPSRCSLPGYQFRGEDPEQTDAAAPPAPAARRAPAAAPARTADTRAVLAELWCRTLG 907
Cdd:COG3321 1093 AALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAA 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 908 VPVALDDDSFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVERQSPARPAPAATGTLPVPGVATLTEG 987
Cdd:COG3321 1173 LLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAA 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 988 GTGRPVFLVADATGTALPYRHLAALLAPLAANRPVLGLEDPGGPRTRTIPAIAADHVTALLRTQPEGPYTLGGWSFGAVV 1067
Cdd:COG3321 1253 AALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAA 1332
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 753979669 1068 AHEMAYRLTRLGKRVDLLVCLDGFVPDTGGRPVSFAPEFLRAGLRSQAEALLG 1120
Cdd:COG3321 1333 LAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
160-236 |
6.17e-05 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 46.14 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 160 PALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVM---PRGE-----WGYLFEQG---GILSPDGRCRPFDERAGG 228
Cdd:pfam00108 77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMshaPYALptdarSGLKHGDEkkhDLLIPDGLTDAFNGYHMG 156
|
....*...
gi 753979669 229 tVPAEGVA 236
Cdd:pfam00108 157 -LTAENVA 163
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
898-970 |
3.16e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.54 E-value: 3.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 753979669 898 LAELWCRTLGV-PVALDDDsFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVERQSPARPAP 970
Cdd:PRK12467 1035 LAAIWADVLKVeRVGLTDN-FFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPA 1107
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
895-963 |
4.66e-04 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 40.31 E-value: 4.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 753979669 895 RAVLAELWCRTLGVPVALDDD---SFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVERQ 963
Cdd:smart00823 14 LDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1034-1215 |
4.68e-04 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 43.30 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1034 RTIPAIAADHVTALLRtQPEGPYTLGGWSFGAVVAHEMAYRLTRLGKRVDLLVCLDGFVP---DTGGRPVSFAP-EFLRA 1109
Cdd:COG3208 53 TSLEELADDLAEELAP-LLDRPFALFGHSMGALLAFELARRLERRGRPLPAHLFVSGRRAphlPRRRRPLHDLSdAELLA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1110 GLRSQA---EALLGIGPVARRLGRatALRRQFVANQAtlLRYRPR-PVACPVVLFKASSGP-AEADRLRG--RLSglyGD 1182
Cdd:COG3208 132 ELRRLGgtpEEVLADPELLELFLP--ILRADFRLLET--YRYTPGpPLDCPITALGGDDDPlVSPEELAAwrEHT---TG 204
|
170 180 190
....*....|....*....|....*....|...
gi 753979669 1183 GVRVEPVGGDHWSMLTGPyaDELALKLAHALPA 1215
Cdd:COG3208 205 PFRLRVFPGGHFFLRDHP--AELLALIRAALAA 235
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
898-963 |
5.03e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.56 E-value: 5.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 753979669 898 LAELWCRTLGVPVALDDDSFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVERQ 963
Cdd:PRK12316 5077 VAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAA 5142
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
898-962 |
7.20e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 7.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 753979669 898 LAELWCRTLGVP-VALDDDsFFALGGESLMAVSLTAQVRELTGCVLSVTDFSRAPSFGRLVETVER 962
Cdd:PRK05691 1643 IAAIWREVLGLPrVGLRDD-FFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVAR 1707
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
160-200 |
9.75e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 42.83 E-value: 9.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 753979669 160 PALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPR 200
Cdd:PRK05790 80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQ 120
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
891-968 |
1.06e-03 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 42.43 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 891 TADTRAVLAELWCRTLGVPVAL--DDDSFFALGGESLMAVSLTAQVRElTGCVLSVTDFSRAPSFGRLVETVERQSPARP 968
Cdd:COG3433 217 TALTEEELRADVAELLGVDPEEidPDDNLFDLGLDSIRLMQLVERWRK-AGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1031-1200 |
3.91e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 40.37 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1031 PRTRTIPAIAADhVTALLRTQPEGPYTLGGWSFGAVVAHEMAyrlTRLGKRVDLLVCLDGFVpdtggrpvsfapEFLRAG 1110
Cdd:COG0596 67 AGGYTLDDLADD-LAALLDALGLERVVLVGHSMGGMVALELA---ARHPERVAGLVLVDEVL------------AALAEP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753979669 1111 LRsqaeallgigpvaRRLGRATALRRQFVANQATLLRYRPRPVACPVVLFKASSGPAEADRLRGRLSGLYGDGVRVEPVG 1190
Cdd:COG0596 131 LR-------------RPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197
|
170
....*....|
gi 753979669 1191 GDHWSMLTGP 1200
Cdd:COG0596 198 AGHFPPLEQP 207
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
160-203 |
8.14e-03 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 39.94 E-value: 8.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 753979669 160 PALTVQTACSTSLTAVHLAARALVGGECDAALAGGVTVMPRGEW 203
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPF 125
|
|
| |
