|
Name |
Accession |
Description |
Interval |
E-value |
| FabG2 |
COG4982 |
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and ... |
1-3069 |
0e+00 |
|
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and metabolism];
Pssm-ID: 444006 [Multi-domain] Cd Length: 3088 Bit Score: 3410.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1 MTIHEHDRVSADRGGDSPHT--------THALVDRLMAGEPYAVAFGGQGSAWLETLEELVSATGIETELATLVGEAELL 72
Cdd:COG4982 1 KTATEVDVASADRLLAGAAAldqpatglLVSLGGRLAAGLAAGLATGSRDSLSGGALEALLAPAVAEALLAAEALLVPVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 73 LDPVTDELIVVRPIGFEPLQWVRALAAEDPVPSDKHLTSAAVSVPGVLLTQIAATRALARQGMDLVATPPVAMAGHSQGV 152
Cdd:COG4982 81 AALVVARVAAVAAAALAEAGAVLALAAEAALAAAASAVPAAVIATGAALVAALALKLLGAAGLLLLAVSVSAQAGAPSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 153 LAVEALKAGGARDVELFALAQLIGAAGTLVARRRGISVLGDRPPMVSVTNADPERIGRLLDEFAQDVRTVLPPVLSIRNG 232
Cdd:COG4982 161 VALEAASGAGAQLAELLAALALLAAALLAVAARRAGAVSLGVPALRSLLNALGLSVLAESAERAGAVRTGLLAALGARRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 233 RRAVVITGTPEQLSRFELYCRQISEKEEADRKNKVRGGDVFSPVFEPVQVEVGFHTPRLSDGIDIVAGWAEKAGLDVALA 312
Cdd:COG4982 241 VRSAPILGTAQQLAEGLLAAGARAEALAKEEKRKLAGGVVGGAVVDPVQEEVGAALPDGVPEVDAAADLAAAEALDVGLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 313 RELADAILIRKVDWVDEITRVHAAGARWILDLGPGDILTRLTAPVIRGLGIGIVPAATRGGQRNLFTVGATPEVARAWSS 392
Cdd:COG4982 321 AELRTAILLAAVVVVVDAVAAVAAVTAAGLLLLLGPGLTATRTPVSRVGAVGVAPAAVGLAARELFTTPATPVSARRPSD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 393 YAPTVVRLPDGRVKLSTKFTRLTGRSPILLAGMTPTTVDAKIVAAAANAGHWAELAGGGQVTEEIFGNRIEQMAGLLEPG 472
Cdd:COG4982 401 VAPTTVPLAPGAAAAATGRTALLARLPILGLVMTPTTTAAAAAAKAAAAAAGAGEVGEGGELEELFAGRLAELLGALAEG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 473 RTYQFNALFLDPYLWKLQVGGKRLVQKARQSGAAIDGVVISAGIPDLDEAVELIDELGDIGISHVVFKPGTIEQIRSVIR 552
Cdd:COG4982 481 VDVFAVALALLPALLPLQVGLQRLASEAFQKGVAADGGVVIVGAVAQEAALPLAEVLVDVGIGLVVGGPAGVATIVSIVR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 553 IATEVPTKPVIMHVEGGRAGGHHSWEDLDDLLLATYSELRSRANITVCVGGGIGTPRRAAEYLSGRWAQAYGFPLMPIDG 632
Cdd:COG4982 561 IATAAEVIEVPIIVEEGGGAGGHGSAADLDDLLLTAQALLSRTPPVVIVVGGGIGTAPAAATWAPGGKGVLGDPSGTPVL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 633 ILVGTAAMATKESTTSPSVKRMLVDTQGTDQWISAGKAQGG-MASSRSQLGADIHEIDNSASRCGRLLDEVAGDAEAVAE 711
Cdd:COG4982 641 AADGVAAAAAAAAGTSLLVAKMVLPETGESPGDLGAGGAGGaAASGGSDLLAITHEESSQRRLASRLDDAEAADAAAAEA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 712 RRDEIIAAMAKTAKPYFGDVADMTYLQWLRRYVELAIGeGNSTADTASVGSPWLADTWRDRFEQ----MLQRAEARLHPQ 787
Cdd:COG4982 721 ARARIAAAAEATAKPEFTSDAAAADLEALARADALSAL-DDDDAAQEAIGVIEASARWDDTLEDelqrMTARLEARDAAE 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 788 DFGPIQTLFT-DAGLLDNPQQAIAALLARYPDAETVQLHPADVPFFVTLCKTLGKPVNFVPVIDQDVRRWWRSDSLWQAH 866
Cdd:COG4982 800 LAAPAATLAAdDADLALVHAARPALAAAILPAASAPVLHPADVPFAVVLFKPIGPPPPVVPVIFDDVRRWRRIDSLQAAH 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 867 DARYDADAVCIIPGTASVAGITRMDEPVGELLDRFEQAAIDEVLGAGVEPKDVASRRLGRADVAGPlaVVLDAPDVRWAG 946
Cdd:COG4982 880 AARDDADAVVAIGTVAAAAGETLDDEQADELLDREVARITAAALAAGAPRALVAARGLEGADVAAG--VVLAADDIVWAS 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 947 RTVTNPVHRIADPAEWQVHDGPENPR--ATHSSTGARLQTHGDDVALSVPVSGTWVDIRFTLPANTVDGGTPVIATEDAT 1024
Cdd:COG4982 958 RLDTNPVRRLEIVASTSAGVDPRAVReeVIPELVDGADAGVEDAVVLVIPVLLTRVVTDGTLATDGTATGTPADALVAAA 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1025 SAMRTVLAIAAGVDSPEFLPAVANGTATLTVDWHPERVADHTGVTATFGEPLAPSLTNVPDALVGPCWPAVFAAIGSAVT 1104
Cdd:COG4982 1038 TAGTAVAAGAAGGELAESTPSGAAGIADVGADWAAVPVALVTSATVPDGVPGGPLSTVVPAPLSVLGAATAALGAALAAV 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1105 DTGEPVVEGLLSLVHLDHAARVVGQLPTVPAQLTVTATAANATDTDMGRVVPVSVVVTGADGAVIATLEERFAILGRTGS 1184
Cdd:COG4982 1118 HLGVIVVLDLLLLVLGDAALIHLALSSTLAALVATDLGRVVTADVDVRVVDGVVVTEETRRGAARGTSDEEAAPGRRAGG 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1185 AELADPARAGGAVSANATDTPRRRRRDVTITAPVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVT 1264
Cdd:COG4982 1198 RGRDTEAVPGARRTLARTTVRARRRTTAFAAVAGDYSPIHVSVGAAPRAGLDAAAAAGGWLSAPAAHAAQAAAAAQGSAA 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1265 ATDGQARPPARLVGWTARFLGMVRPGDEVDFRVERVGIDQGAEIVDVAARVGSDLVMSASARLAAPKTVYAFPGQGIQHK 1344
Cdd:COG4982 1278 AARWTGGPAPLLIGWTTRELTVVRAGDEVVVVVVRVGVERGGEVVVVVACVVAAVAVSATAAAAAPPGVAGFPPGSRQAA 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1345 GMGMEVRARSKAARKVWDTADKFTRDTLGFSVLHVVRDNPTSIIASGVHYHHPDGVLYLTQFTQVAMATVAAAQVAEMRE 1424
Cdd:COG4982 1358 GGGGDDARRRKAAARRWDKAARATRDRLGASVLLVVGRDPTHVLALLGHTQHPVGGLLLTQQTQQAAATVAAAAVAEAGE 1437
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1425 QGAFVEGAIACGHSVGEYTALACVTGIYQLEALLEMVFHRGSKMHDIVPRDELGRSNYRLAAIRPSQIDLDDADVPAFVA 1504
Cdd:COG4982 1438 AGGFAGAAAALAGSVAGEAALAAVEGVVLLLELLGEVVHRGSARHRIVRPGDLRRSDDRAAAAHPSVQVAEDVDDVADVA 1517
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1505 GIAESTGEFLEIVNFNLRGSQYAIAGTVRGLEALEAEVERRRELTGGRRSFILVPGIDVPFHSRVLRVGVAEFRRSLDRV 1584
Cdd:COG4982 1518 AIVERTLEFAQEYVNNLLAGQAAAAAGVVALLAALEAERRRREAGGGGRSFFLRVGIVDVPFSSVLLRGGLPEFRSLLRL 1597
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1585 MPRDADPDLIIGRYIPNLVPRLFTLDRDFIQEIRDLVPAEPLDEILADYDTWLRERPREMARTVFIELLAWQFASPVRWI 1664
Cdd:COG4982 1598 LLPDDIDLILRGGKLPPNLPRSFFELEPEFVESILLVVPDEPVEALLDDWTLAAKLLILLLRTLLIELLAWQFASPVRWI 1677
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1665 ETQDLLFIEEAAGGLGVERFVEIGVKSSPTVAGLATNTLKLPEYAHSTVEVLNAERDAAVLFATDTDPEPEPEEDEPVAE 1744
Cdd:COG4982 1678 ETQDLLFIEGLGGGLGVERFVEGGGKSAPTLALTLALTLKLGSAAGTRVVVLNRERDDSLVFATDEDPEPVEDEADAEEA 1757
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1745 SP-----APDVVSEAAPVAPAASSAGPRPDDLVFDAADATLALIALSAKMRIDQIEELDSIESITDGASSRRNQLLVDLG 1819
Cdd:COG4982 1758 AAsaaaaAPAPPAAAAPAAAPAAAGGPRPDDLPFTASDATKALIALSTKIRPDQIGAADTIETLTDGVSSRRNQLLMDLG 1837
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1820 SELNLGAIDGAAESDLAGLRSQVTKLARTYKPYGPVLSDAINDQLRTVLGPSGKRPGAIAERVKKTWELGEGWAKHVTVE 1899
Cdd:COG4982 1838 SELGLGAIDGAAEADVPTLSATVDKLARTYKPFGPVLSDAIRDRLRKLFGPAGKRQSYIADRVTGVWQLGEGWAAHVTAE 1917
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1900 VALGTREGSSVRGGAMGHLHEGALADAASVDKVIDAAVASVAARQGVSVALPSAGSGGGATIDAAALSEFTDQITGREGV 1979
Cdd:COG4982 1918 LALGTREGASVRGGDLATLPTAAPSNAAAVDALIDAAVAAVAARHGVSVALPSAGGGGGATVDSAALGEFTEQITGRDGV 1997
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1980 LASAARLVLGQLGLDDPVNALPAA-PDSELIDLVTAELGADWPRLVAPVFDPKKAVVFDDRWASAREDLVKLWLTDEGDI 2058
Cdd:COG4982 1998 LASAARTLLDKLGLAAPAPVAESAdEDAELVELVEAELGSDWPRLVAPAFDARKAVLLDDRWASAREDLARLWLGDEAAI 2077
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2059 dadwprLAERFEGAGHVVATQATWWQGKSLAAGRQIHASLYGRIAAGAENPEPGRYGGEVAVVTGASKGSIAASVVARLL 2138
Cdd:COG4982 2078 ------EAGSFTGAGEAVADQAAWWAGKALAAGRAVLARRYGQIAADAEDPSAGEYADDVAVVTGASPGSIAAAVVAGLL 2151
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2139 DGGATVIATTSKLDEERLAFYRTLYRDHARYGAALWLVAANMASYSDVDALVEWIGTEQTESLGPQSIHIKDAQTPTLLF 2218
Cdd:COG4982 2152 AGGATVIATTSSLDSDRLAFYKELYRENARGGAALWVVPANMASYRDVDALVEWIGTEQTETVGATTTVTKPALTPTLLF 2231
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2219 PFAAPRVVGDLSEAGSRAEMEMKVLLWAVQRLIGGLSTIGAERDIASRLHVVLPGSPNRGMFGGDGAYGEAKSALDAVVS 2298
Cdd:COG4982 2232 PFAAPRVSGDLADAGPRAESQMRLLLWSVERLIAGLAAIGADTDVDHRLHVVLPGSPNRGMFGGDGAYGEAKAALDAIVN 2311
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2299 RWHAESSWAARVSLAHALIGWTRGTGLMGHNDAIVAAVEEAGVTTYSTDEMAALLLDLCDAESKVAAARSPIKADLTGGL 2378
Cdd:COG4982 2312 RWRAEKSWSSRVTLAHARIGWVRGTGLMGGNDPLVAAVEAAGVRTYSTEEMAAELLDLCTAEAREQAASAPLDADLTGGL 2391
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2379 AEANLDMAELAAKAREQmSAAAAVDEDAEAPGAIAALPSPPRGFTPAPPPQWDDLDVDPADLVVIVGGAEIGPYGSSRTR 2458
Cdd:COG4982 2392 GEVDLDMAALAAEAEAD-AAEEAAAADSAAAGTIAALPSPPRPAQPVALPDWGEVTARPEDLVVIVGAGELGPWGSARTR 2470
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2459 FEMEVENELSAAGVLELAWTTGLIRWEDDPQPGWYDTESGEMVDESELVQRYHDAVVQRVGIREFVDDGAIdPDHASPLL 2538
Cdd:COG4982 2471 FEAEVSVELSAAGVLELAWNTGLITWEDDPKPGWYDTETGELVPESDIAERYHDEVVARCGIRPFVDDGAM-VDGTSPLL 2549
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2539 VSVFLEKDFAFVVSSEADARAFVEFDPEHTVIRPVPDSTDWQVIRKAGTEIRVPRKTKLSRVVGGQIPTGFDPTVWGISA 2618
Cdd:COG4982 2550 ASVFLDKDLTFSVSSEAEARAYVDADPEHTVIAPDEESGEWQVTRKAGTEIRVPRRATMTRTVGGQFPTGFDPTRWGIPA 2629
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2619 DMAGSIDRLAVWNMVATVDAFLSSGFSPAEVMRYVHPSLVANTQGTGMGGGTSMQTMYHGNLLGRNKPNDIFQEVLPNII 2698
Cdd:COG4982 2630 SMVDSVDRIALWNLVTTVDAFLSAGFTPAELLQSVHPSDVASTQGTGMGGMTSMRKLYVDRFLGEPRPNDILQEALPNVV 2709
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2699 AAHVVQSYVGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLEGIIGFGDMAATADTSMMRGRGIHDS 2778
Cdd:COG4982 2710 AAHVMQSYVGGYGNMIHPVAACATAAVSVEEGVDKIRLGKADFVVAGGIDDIGVESITGFGDMNATADSEEMLAKGIDDR 2789
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2779 KFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALGAGRGGKDSPLARALAK 2858
Cdd:COG4982 2790 FFSRANDRRRGGFVEAQGGGTILLARGDVAAKLGLPVLGVVAFAQSFADGAHTSIPAPGLGALAAARGGKDSKLARDLAK 2869
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2859 LGVAADDVAVISKHDTSTLANDPNETELHERLADALGRSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPN 2938
Cdd:COG4982 2870 LGVTADDIAVVSKHDTSTNANDPNESELHERLAHAIGRTDGNPLFVVSQKSLTGHAKGGAAAFQLIGLCQVLRSGVIPPN 2949
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2939 RSLDCVDDELAGSAHFVWVRDTLRLGGKFPLKAGMLTSLGFGHVSGLVALVHPQAFIASLDPAQRADYQRRADARLLAGQ 3018
Cdd:COG4982 2950 RSLDCVDDKLAGDDHLVWLREPLRLGAKGPLKAGLLTSLGFGHVSGLLAVVHHAAFFAALEAEEADAYAAAARARRARGR 3029
|
3050 3060 3070 3080 3090
....*....|....*....|....*....|....*....|....*....|.
gi 622703340 3019 RRLASAIAGGAPMYQRPGDRRFDHHAPERPQEASMLLnPAARLGDGEAYIG 3069
Cdd:COG4982 3030 RRRAAAMAGGGMGYRRPPRRRRDGRRDHEAAAALDLL-ELLRADDGDAGAV 3079
|
|
| COG4981 |
COG4981 |
Enoyl reductase domain of yeast-type fatty acid synthase [Lipid transport and metabolism]; |
20-3067 |
0e+00 |
|
Enoyl reductase domain of yeast-type fatty acid synthase [Lipid transport and metabolism];
Pssm-ID: 444005 [Multi-domain] Cd Length: 3064 Bit Score: 2679.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 20 TTHALVDRLMAGEPYAVAFGGQGSAWLETLEELVSATGIETELATLVGEAELLLDPVTDELIVVRPIGFEPLQWVRALAA 99
Cdd:COG4981 10 ARLANGESSALQFGAQGAQGLDALTALSVLADLEAYAPALAALAAAAAELLAPLLAVARPLLAVPSDGFLPLDLEAAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 100 EDPVPSDKHLTSAAVSVPGVLLTQIAATRALARQGMDLVATPPVAMAGHSQGVLAVEALKAGGARDVELFALAQLIGAAG 179
Cdd:COG4981 90 AAAAAAAALLTLAAASSLPGVLAALGAALAALAAGGLDAAVAPVAAVGGHSGVLLAEAADAAGAADDALLAAAALLGGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 180 TLVARRRGISVLGDRPPMVSVTNADPERIGRLLDEFAQDVRTVL-PPVLSIRNGRRAVVITGTPEQLSRFELYCRQISEK 258
Cdd:COG4981 170 TAVARRRGGLAAGGEAPAMLSVSAVDPELLRALVAEVADLRTPIhGPVLAIRNSRRRVVLSGAPAQLAAERARCARIAAK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 259 EEADRKNKVRGGDVFSPVFEPVQVEVGFHTPRLSDGIDIVAGWAEKAGLDVALARELADAILIRKVDWVDEITRVHAAGA 338
Cdd:COG4981 250 EAAEREAKLRGGAPFAPVFEVLPVEVAFHHPALADAVALVGEWAGRCGLDADLATSLAAAILVDPVDWVEAVDDAVAAGA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 339 RWILDLGPGDILTRLTAPVIRGLGIGIVPAATRGGQRNLFTVGATPEVARAWSSYAPTVVRLPDGRVKLSTKFTRLTGRS 418
Cdd:COG4981 330 RWILDLGPGDLLTRLTGAVVRGTGVGVVPAATRGGRRNLFTPGAAPEVPAAWSRFAPRLVRLPDGRTVVETAFTRLTGRS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 419 PILLAGMTPTTVDAKIVAAAANAGHWAELAGGGQVTEEIFGNRIEQMAGLLEPGRTYQFNALFLDPYLWKLQVGGKRLVQ 498
Cdd:COG4981 410 PILLAGMTPTTVDPKIVAAAANAGHWAELAGGGQVTEEIFAENVAGLKALLEPGRTVQFNAMFLDPYLWNLQVGGKRIVQ 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 499 KARQSGAAIDGVVISAGIPDLDEAVELIDELGDIGISHVVFKPGTIEQIRSVIRIATEVPTKPVIMHVEGGRAGGHHSWE 578
Cdd:COG4981 490 KARAAGAPIDGVVVSAGIPELDEAVALIEELHEAGFSYVAFKPGTVAQIRQVLRIAKEVPDTPIIVHVEGGRAGGHHSWE 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 579 DLDDLLLATYSELRSRANITVCVGGGIGTPRRAAEYLSGRWAQAYGFPLMPIDGILVGTAAMATKESTTSPSVKRMLVDT 658
Cdd:COG4981 570 DLDDLLLATYAELRARPNVVLCVGGGIGTPERAADYLTGQWSLAYGFPAMPVDGVLVGTAAMATLEATTSPEVKQLLVET 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 659 QGTDQWISAGKAQGGMASSRSQLGADIHEIDNSASRCGRLLDEVAGDAEAVAERRDEIIAAMAKTAKPYFGDVADMTYLQ 738
Cdd:COG4981 650 PGTPDWVGAGGASGGMASGRSQLGADIHEIDNAAARCGRLLDEVAGDADAVAARRDEIIEALNKTAKPYFGDVAEMTYAQ 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 739 WLRRYVELAIGEGNSTADTASVGSPWLADTWRDRFEQMLQRAEARLHPQDFGPIQTLFTDAGLLDNPQQAIAALLARYPD 818
Cdd:COG4981 730 WLQRYAELSVGDAASAADTDATRSPWLDITWRDRFHELLQRAEARLHPADRGEIPTLFPDDAAVEDPHAALDALAEAYPD 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 819 AETVQLHPADVPFFVTLCKTLGKPVNFVPVIDQDVRRWWRSDSLWQAHDARYDADAVCIIPGTASVAGITRMDEPVGELL 898
Cdd:COG4981 810 AATTVLHPADVAFFVALCRTPGKPVNFVPVIDKDVRRWWRSDSLWQAHDPRYSADQVCIIPGPVAVAGITRVDEPVGELL 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 899 DRFEQAAIDEVLGAGVEPKDVASRRLGRADVA-GPLAVVLDAPDVRWAGRTVTNPVHRIADPAEWQVHDgpenPRATHSS 977
Cdd:COG4981 890 DRFEAAAVDRLQAAGVAPDAVAARRYSVADGAaGALEFVLAAPDVSWAGRLTDNPVHRLGDGDQWLVVD----PQGADPG 965
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 978 tgarlqthGDDVALSVPVSGT-WVDIRFTLPANTVDGGTPVIATEDATSAMRTVLAIAAGVDSPEFLPAVANGTATLTVD 1056
Cdd:COG4981 966 --------DDRVDLDIPLDGTrELVIPLTLPESVADGGVPVVDAERASAAMYALLAVAAGVGNTTALPEVDDGVAHATFT 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1057 WHPERVADHTGVTAT-FGEPLAPSLTnVPDALVGPCWPAVFAAIGSAVTDTGEPVVEGLLSLVHLDHAARVVGQLPTVPA 1135
Cdd:COG4981 1038 WSPDLGADHAGVTGGaLPSDLSPSAI-VPDALVGPCWPAVFAALGSAKTGDGPPIEEGLLAVVHLDHIALLVGELPLLSY 1116
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1136 QLTVTATAANATDTDMGRVVPVSVVVTGADGAVIATLEERFAILGRTGSAELADPARAGGAVSANATDTPRRRRRDVTIT 1215
Cdd:COG4981 1117 TLTVIATASWAEDTAEGRVVEVVVIVVEHGAEDGTTLARETERFRRRGRVYSRAPPAAAPAAGGAAAGTRRRSRRLTRRA 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1216 APVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQARPPARLVGWTARFLGMVRPGDEVDF 1295
Cdd:COG4981 1197 AVTATDRAAAVGVAHPSHTSDRAAALAAGDAPAVAGMWGSAAAAATASAAAQAVATSAAAPWTTRWLYTVTPADQLDVTV 1276
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1296 RVERVGIDQGAEIVDVAARVGSDLVMSASARLAAPKTVYAFPGQGIQHKGMGMEVRARSKAARKVWDTADKFTRDTLGFS 1375
Cdd:COG4981 1277 ERDREDVGVGRGGVVVGEVVCRVVVEVARAAVARCTPVVAAPGPPGQGPGQGGMTRSKRARARAARRAARRIDKLTRSHL 1356
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1376 VLHVVRDNPTSIIASGVHYHHPDGVLYLTQFTQVAMATVAAAQVAEMREQGAFVEGAIACGHSVGEYTALACVTGIYQLE 1455
Cdd:COG4981 1357 AASLLAVVRDLPRDNTTNGVARGVPLGLPTLVQVLTVATATAAAALMAAQREEGAEAGAAVFGGHSAGASAALSAALAAI 1436
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1456 ALLEMVFHRGSKMHDIVPRDELGRSNYRLAAIRPSQIDLDDADVPAFVAGIAESTGEFLEIVNFNLRGSQYAIAGTVRGL 1535
Cdd:COG4981 1437 ALEVVLELVLSRGSTRGSLMHRLAPRDSNGRMRARRPALDDVDDDHVDAEIEARSGESGEFLQVVLYNVAVNLAAIAGAI 1516
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1536 EALEAEVERRRELTGGRRSFILVPGIDVPFHSRVLRVGVAEFRRSLDRVMPRDADPDLIIGRYIPNLVPRLFTLDRDFIQ 1615
Cdd:COG4981 1517 AGAAAEAERLARAAGRARGAKPFKGVPGLDVGFHSRVARFVLRPGREVLRGRLPELDPEDLDVGPLVPLLVARLDLLPRI 1596
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1616 EIRDLVPAEPLDEILADYDTWLRE------RPREMARTVFIELLAWQFASPVRWIETQDLLFIEEAAGGLGVERFVEIGV 1689
Cdd:COG4981 1597 FARDILEVVPSEVLDADEEEATADadaaakLPVLLALLLLVLLLPWQWASPLRIEETELLLLSQEEEGLGGVGVVVAIEL 1676
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1690 KSSPTVAGLATNTLKLPEYAHSTVEVLNAERDAAVLFATDTDPEPEPEEDEPVAESPAPDvVSEAAPVAPAASSAGPRPD 1769
Cdd:COG4981 1677 GGLATATLLAATVLVLEFVAVQVNVVHVLRRETDVDLTPEDEAAEAPDDEDAAAPAAAPA-AAAAPAPAPAPAAAAPAAP 1755
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1770 DLVFDAADATLALIALSAKMRIDQIEELDSIESITDGASSRRNQLLVDLGSELNLGAIDGAAESDLAGLRSQVTKLARTY 1849
Cdd:COG4981 1756 AAPAPAAPAAAAPAALLSFAAPPALDADDAQTTLAASASVRLLLLLSSLTALLSDAGGGLADGASLADLSASVDAASSEG 1835
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1850 KPYGPVLSDAINDQLRTVLGPSGKRPGAIAERVKKTWELGEGWAKHvTVEVALGTREGSSVRGGAMGHLHEGALADAASV 1929
Cdd:COG4981 1836 MAALAVTSLKQAGKYKALGGVKGGAVSERGPRLTGVSGLGAGAVAD-RVAAARLLGLAGASGGGAAGAGGTLALLSTAAG 1914
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1930 DKVIDAAVASVAArQGVSVALPSAGSGGGATIDAAALSEFTDQITGREGVLASAARLVLGQLGLDDPVNALPAAPDSELI 2009
Cdd:COG4981 1915 DLAAAASAAAGGA-AAVIAAGAATAGGGGAAAVASALAVPAAGLAGGASVLSAALGASAASVAASGEVAAKAAAAAAELV 1993
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2010 DLVTAELGADWPRLVAPVFDPKKAVVFDDRWASAREDLVKLWLT----DEGDIDADWPRLAERFEGAGHVVATQATWWQG 2085
Cdd:COG4981 1994 ELADDALVAAAPADGAPVLVAVDAVVSAARADLDRWSLARAEATarwvLAILPEADAARAAARDAAAAGAAAAAARTSAA 2073
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2086 KSLAAGRQIHASLYGRIAAGAENPEPGRYGGEVAVVTGASKGSIAASVVARLLDGGATVIATTSKLDEERLAFYRTLYRD 2165
Cdd:COG4981 2074 EAASAAAAFAAAKATVAEAGAASADAAAAAASSAVAGAAAAGAAVAAVASAAAGGQAVAVATAAGVLVRASASARALLRL 2153
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2166 HARYGAALWLVAANMASYSDVDALVEWIGTEQTESLGPQSIHIKDAQTPTLLFPFAAPRVVGDLSEAGSRAEMEMKVLLW 2245
Cdd:COG4981 2154 AAALAAYASVVAADAAISTADETLAEAVGVAVGKLAGAALLVFSDALAVARAKAEAAPRVPEAASELAKATTVAIGLLLA 2233
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2246 AVQRLIGGLSTIGAERDIASRLHVVLPGSPNRGMFGGDGAYGEAKSALDAVVSRWHAESSWAARVSLAHALIGWTRGTGL 2325
Cdd:COG4981 2234 PDGRLLGSLSVHGARADSGARLHVLGAGGEVGGVGALAALTATGTAADAVVVASTSALLGTGRVAGLGGGGGGDGLATLV 2313
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2326 MGHNDAIVAAVEEAGVTTYSTDEMAALLLDLCDAESKVAAARSPIKADLTGGLAEANLDMAELAAKAREQMSAAAAVDED 2405
Cdd:COG4981 2314 QGIVARVVAASETSGVTTALCAAGARLLAGEAPGEADLAGLEGESRAVLAGALAEADLDLALLAAAAAQAAAAATAAADA 2393
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2406 AEAPGAIAALPSPPRGFTPAPPPQWDDLDVDPADLVVIVGGAEIGPYGSSRTRFEMEVENELSAAGVLELAWTTGLIRWE 2485
Cdd:COG4981 2394 AATAGAAAAPPAPLPAPSREPAASAPGASAPPATAVSAVGSEPAGEASAAGLAEAEWVAGLAAWTDTAVAGWLTGDEVSE 2473
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2486 DDPQPGWYDTESGEMVDESELVQRYHDAVVQRVGIREFVDDGAIDPDHASPLLVSVFLEKDFAFVVSSEADARAFVEFDP 2565
Cdd:COG4981 2474 DPIEIGALGTDETVAGAEVELNDDAGVDVDGVDERRVESVIALDPTDSVDSVVLADEYAAFDDTVDESAEAAEEVVWEDE 2553
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2566 EHTVIRPVPDSTDWQVIRKAGTEIRVPRKTKLSRVVGGQIPTGFDPTVWGISADMAGSIDRLAVWNMVATVDAFLSSGFS 2645
Cdd:COG4981 2554 VTAIADSPPRADGRTVGARGPEVDRAPRRTGSVVVTVGIGDEAVADLVTTADDADDSEIETAVDLSVAVSAVVGASAAVS 2633
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2646 PAEVMRYVHPSLVANTQGTGMGGGTSMQTMYHGNLLGRNKPNDIFQEVLPNIIAAHVVQSYVGSYGAMIHPVAACATAAV 2725
Cdd:COG4981 2634 TFGGMSFTVGALLDRSGEGAVGSGSLSMIDLVRNALVTNAVGGQGYSSSYPIIAAAVAASVGAEGGVSIGVGAAAVAVVL 2713
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2726 SVEEGVDKIRLGKAQLVVAGGLDDLTLEGIIGFGDMAATADTSMMRGRGIHDSKFSRPNDRRRLGFVEAQGGGTILLARG 2805
Cdd:COG4981 2714 GAVDGGAVIIELGVASGAAGAQDTALAGGGGMGRFAAAADDRAMAATRIGQGALDSRGADGRVLGQGGGDVGGVVLVGGV 2793
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2806 DLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALGAGRGGKDSPLARALAKLGVAADDVAVISKHDTSTLANDPNETE 2885
Cdd:COG4981 2794 GDVAATLGVVAGGAALAAGAFGVAAALPVRGGGLGAGGGGDGALASSRASEGGALDAALDDLAANLAAAGALEAGPAHTL 2873
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2886 LHERLADALGRSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDELAGSAHFVWVRDTLRLGG 2965
Cdd:COG4981 2874 LATSALGSSKAGGAAAEARALGLLAAGGGATAANAPFLGALDALEVGGRNDLHRALLLGDALPLAVGVVSLLRGSTLALG 2953
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2966 KFPLKAGMLTSLGFGHVSGLVALVHPQAFIASLDPAQRADYQRRADARLLAGQRRLASAIAGGAPMYQRPGDRRFDHHAP 3045
Cdd:COG4981 2954 AASGLLALTQVHRGGLLAALALAVAAQAAALGRPRAAARIAQRNALAELRRVRRQRSSRRGGAGEPALQRLDREGALAKP 3033
|
3050 3060
....*....|....*....|..
gi 622703340 3046 ERPQEASMLLNPAARLGDGEAY 3067
Cdd:COG4981 3034 SAIRLGAPLLYTPTARGDGDAV 3055
|
|
| DUF1729 |
pfam08354 |
Domain of unknown function (DUF1729); This domain of unknown function is found in fatty acid ... |
561-898 |
1.62e-126 |
|
Domain of unknown function (DUF1729); This domain of unknown function is found in fatty acid synthase beta subunits together with the MaoC-like domain (pfam01575) and the Acyltransferase domain (pfam00698). The domain has been identified in fungi and bacteria.
Pssm-ID: 369827 Cd Length: 353 Bit Score: 402.99 E-value: 1.62e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 561 PVIMHVEGGRAGGHHSWEDLDDLLLATYSELRSRANITVCVGGGIGTPRRAAEYLSGRWAQAYGFPLMPIDGILVGTAAM 640
Cdd:pfam08354 1 PIILQWTGGRAGGHHSNEDFHAPLLATYARIREQDNVVLVVGSGFGDPEDGAPYLTGEWSQRFGLPPMPVDGILLGSRAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 641 ATKESTTSPSVKRMLVDTQG--TDQWI-SAGKAQGGMASSRSQLGADIHEIDNSASRCGRLLDEVAGDAEAVAER----- 712
Cdd:pfam08354 81 VAKEAHTSDEVKQLIVETPGckDDEWQaTYGKPAGGVVSVRSELGEPIHKIANRAARLWRELDETIFSLAPVEKRgaalr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 713 --RDEIIAAMAKT-AKPYFG--------DVADMTYLQWLRRYVELAigegnstadTASVGSPWLADTWRDRFEQMLQRAE 781
Cdd:pfam08354 161 kkRDEIIERLNKDyQKPWFAvdqhgdpvDLEEMTYSEVVRRFLELM---------YLPHTGRWIDPSWKRLFQDLLQRVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 782 ARLHPQDFGPIQTLFTDAGLLDNPQQAIAALLARYPDAETVQLHPADVPFFVTLCKTLG-KPVNFVPVIDQDVRRWWRSD 860
Cdd:pfam08354 232 ERLHPTDHGPIESLFETVEELEDPAEAINTLTAAYPGAATQLLHPEDCAWFLQLCQRRGqKPVPFVPALDEDFEFWFKKD 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 622703340 861 SLWQAHDARY----DADAVCIIPGTASVAGITRMDEPVGELL 898
Cdd:pfam08354 312 SLWQSEDLDAvvnqDAQRVCILHGPVAVQYSTRANEPVKEIL 353
|
|
| KR_fFAS_SDR_c_like |
cd08950 |
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ... |
2110-2378 |
3.02e-125 |
|
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187653 [Multi-domain] Cd Length: 259 Bit Score: 395.02 E-value: 3.02e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2110 EPGRYGGEVAVVTGASKGSIAASVVARLLDGGATVIATTSKLDEERLAFYRTLYRDHARYGAALWLVAANMASYSDVDAL 2189
Cdd:cd08950 1 SGLSFAGKVALVTGAGPGSIGAEVVAGLLAGGATVIVTTSRFSHERTAFFQKLYRKHGAKGSKLWVVPFNQASKQDVEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2190 VEWIGTEQTeslgpqsihiKDAQTPTLLFPFAAPRVVGDLSEAGSRAEMEMKVLLWAVQRLIGGLSTIGAERDIASR-LH 2268
Cdd:cd08950 81 VEYIYDEQT----------KLAWDLDFLFPFAAISENGRLIDIDSKSELAHRLMLTNVLRLLGCVKKQKRARGIVTRpTH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2269 VVLPGSPNRGMFGGDGAYGEAKSALDAVVSRWHAEsSWAARVSLAHALIGWTRGTGLMGHNDAIVAAVEEAGVTTYSTDE 2348
Cdd:cd08950 151 VVLPLSPNHGTFGGDGLYSESKLALEALFNRWHSE-SWSDYLSICGAVIGWTRGTGLMGGNDVLAEAVEKLGVRTFSTEE 229
|
250 260 270
....*....|....*....|....*....|
gi 622703340 2349 MAALLLDLCDAESKVAAARSPIKADLTGGL 2378
Cdd:cd08950 230 MAFNLLGLLSPEVVELAQEAPVYADLTGGL 259
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2564-2988 |
5.64e-72 |
|
"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: 248.12 E-value: 5.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2564 DPEHTVIRPVPDStdWQVIRKAGTEIRVPR--KTKLSRVVGGQIPTGFDPtVWGISAdmAGSIDRLAVWNMVATVDAFLS 2641
Cdd:cd00828 12 SPHGEGCDEVEEF--WEALREGRSGIAPVArlKSRFDRGVAGQIPTGDIP-GWDAKR--TGIVDRTTLLALVATEEALAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2642 SGFSPAEVmryVHPSLVANTQGTGMGGGTSMQTMYHgnLLGRNKPNDIFQ--EVLPNIIAAHVVQSYVGSYGAMIHPVAA 2719
Cdd:cd00828 87 AGITDPYE---VHPSEVGVVVGSGMGGLRFLRRGGK--LDARAVNPYVSPkwMLSPNTVAGWVNILLLSSHGPIKTPVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2720 CATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLEGIIGFGDMAATADTsmmrgrGIHDSKFSRPNDRRRLGFVEAQGGGT 2799
Cdd:cd00828 162 CATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTA------EEEPEEMSRPFDETRDGFVEAEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2800 ILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALgagrggkdSPLARALAKLGVAADDVAVISKHDTSTLAN 2879
Cdd:cd00828 236 LVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIA--------RAIRTALAKAGLSLDDLDVISAHGTSTPAN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2880 DPNETELHERLADALgrseGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDELAGSAhfvwVRD 2959
Cdd:cd00828 308 DVAESRAIAEVAGAL----GAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLS----VVG 379
|
410 420 430
....*....|....*....|....*....|
gi 622703340 2960 TLR-LGGKfpLKAGMLTSLGFGHVSGLVAL 2988
Cdd:cd00828 380 LSRdLNLK--VRAALVNAFGFGGSNAALVL 407
|
|
| FAS_MaoC |
cd03447 |
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ... |
1211-1330 |
6.69e-47 |
|
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).
Pssm-ID: 239531 [Multi-domain] Cd Length: 126 Bit Score: 165.15 E-value: 6.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1211 DVTITAPVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQaRPPARLVGWTARFLGMVRPG 1290
Cdd:cd03447 6 SLTITAPASNEPYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAAD-NDRSRVRSFTASFVGMVLPN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 622703340 1291 DEVDFRVERVGIDQGAEIVDVAARVG--SDLVMSASARLAAP 1330
Cdd:cd03447 85 DELEVRLEHVGMVDGRKVIKVEARNEetGELVLRGEAEVEQP 126
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
1331-1704 |
1.55e-35 |
|
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: 139.11 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1331 KTVYAFPGQGIQHKGMGMEVRARSKAARKVWDTADkftrDTLGFSVLHVVRDNptsiiasgvhyhhPDGVLYLTQFTQVA 1410
Cdd:COG0331 2 KLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEAS----EALGYDLSALCFEG-------------PEEELNLTENTQPA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1411 MATVAAAQVAEMREQGafVEGAIACGHSVGEYTALACvTGIYQLEALLEMVFHRGSKMHDIVPRDELGrsnyrLAAIrps 1490
Cdd:COG0331 65 ILAASVAAYRALEEEG--IRPDAVAGHSLGEYSALVA-AGALSFEDALRLVRLRGRLMQEAVPAGPGG-----MAAV--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1491 qIDLDDADVPAFVAGIAEstGEFLEIVNFNLRGsQYAIAGTVRGLEALEAEVERRreltGGRRsFILVPgIDVPFHSRVL 1570
Cdd:COG0331 134 -LGLDDEEVEALCAEAAQ--GEVVEIANYNSPG-QIVISGEKEAVEAAAELAKEA----GAKR-AVPLP-VSGPFHTPLM 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1571 RVGVAEFRRSLDRVMPRDADPdliigRYIPNlvprlftldrdfiqeirdlVPAEPLDEiladydtwlrerPREMArtvfi 1650
Cdd:COG0331 204 APAAEKLAEALAAVTFADPKI-----PVVSN-------------------VDAAPVTD------------PEEIR----- 242
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 622703340 1651 ELLAWQFASPVRWIETQdllfieEAAGGLGVERFVEIGVKSspTVAGLATNTLK 1704
Cdd:COG0331 243 ELLVRQLTSPVRWDESV------EALAEAGVTTFVELGPGK--VLSGLVKRIDP 288
|
|
| KR_fFAS_like_SDR_c_like |
cd08928 |
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ... |
2119-2378 |
8.02e-34 |
|
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187633 [Multi-domain] Cd Length: 248 Bit Score: 132.03 E-value: 8.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2119 AVVTGASKGSIAASVVARLLDGGATVIATTSKLDEERLAFYRTLYrdhARYGAA---LWLVAANMASYSDVDALVEWIgT 2195
Cdd:cd08928 1 VLITGAGDGSIGAEVLQGLLNGGAKVYVTTSRFSRQVTKYYQDIY---AACGAAgsvLIVVPFNQGSKQDVEALAIGI-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2196 EQTESLGpqsihikdaQTPTLLFPFAA-PRVVGDLSEAGSRAEMEMKVLLWAVQRLIGGLSTIGAERDIASR-LHVVLPG 2273
Cdd:cd08928 77 DTVNGLG---------WDLDLYGPFAAiPETGIEIPAIDSKSEVAHRIMLTNLLRPKGLVKIQKQLRGQETRpAQVILPF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2274 SPNRGMFGGDGAYGEAKSALDAVVSRWHAEsSWAARVSLAHALIGWTRGTGLMghnDAIVAAVEEAGVTTYSTDEMAALL 2353
Cdd:cd08928 148 SPNHGTFGDDGAYSESKLHLETLFNRWASE-SWGNDLTVCGAHIGWTRGTLGG---EAAPEGLEKGGVRTFSQAEMAFNL 223
|
250 260
....*....|....*....|....*
gi 622703340 2354 LDLCDAESKVAAARSPIKADLTGGL 2378
Cdd:cd08928 224 LGLYFPPKVVLCQPLPVSADLNGGL 248
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2601-2980 |
1.87e-33 |
|
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: 135.61 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2601 VGGQIPtGFDPTVWgISADMAGSIDRLAVWNMVATVDAFLSSGFSPAEVMRY---VhpsLVANTQGTGMGGGTSMQTMYH 2677
Cdd:COG0304 47 IAGEVK-DFDPEEY-LDRKELRRMDRFTQYALAAAREALADAGLDLDEVDPDrtgV---IIGSGIGGLDTLEEAYRALLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2678 GNLLGRNkPNDIFQeVLPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLD-DLTLEGII 2756
Cdd:COG0304 122 KGPRRVS-PFFVPM-MMPNMAAGHVSIRF-GLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2757 GFGDMAATAdtsmmrGRGIHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA-VVAFAQSfGDGVHTSIPA 2835
Cdd:COG0304 199 GFDALGALS------TRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAeVVGYGAS-SDAYHITAPA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2836 PGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNETELherLADALGRSEGAPLfVVSQKSLTGHAK 2915
Cdd:COG0304 272 PDGEGAARA-------MRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKA---IKRVFGDHAYKVP-VSSTKSMTGHLL 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 622703340 2916 GGAAVFQMMGLCQILRDGVIPPNRSLDCVDDELAgsahFVWVRDTLRlggKFPLKAGMLTSLGFG 2980
Cdd:COG0304 341 GAAGAIEAIASVLALRDGVIPPTINLENPDPECD----LDYVPNEAR---EAKIDYALSNSFGFG 398
|
|
| MaoC_dehydratas |
pfam01575 |
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ... |
1197-1321 |
7.35e-33 |
|
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.
Pssm-ID: 396243 [Multi-domain] Cd Length: 123 Bit Score: 124.76 E-value: 7.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1197 VSANATDTPRRRRRDVTITaPVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMwLSAAAQHAVTATDGQARPPARL 1276
Cdd:pfam01575 1 DFQNAPGEPPDTEKPRTVT-EADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGM-LTLAIVAGLVEEWGGDNVIARF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 622703340 1277 VGWTARFLGMVRPGDEVDFRVERVGIDQGAEIVDVAARVGSDLVM 1321
Cdd:pfam01575 79 GEIKVRFTKPVFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2601-2980 |
3.42e-32 |
|
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: 131.89 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2601 VGGQIPtGFDPTVWGISADMAgSIDRLAVWNMVATVDAFLSSGFSPAEVMRY----VHPSLVANTQGTGmgggtSMQTMY 2676
Cdd:cd00834 47 IAGEVP-DFDPEDYLDRKELR-RMDRFAQFALAAAEEALADAGLDPEELDPErigvVIGSGIGGLATIE-----EAYRAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2677 HGNLLGRNKPNDIFQeVLPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLD-DLTLEGI 2755
Cdd:cd00834 120 LEKGPRRVSPFFVPM-ALPNMAAGQVAIRL-GLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2756 IGFGDMAATADtsmmrgRGIHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA-VVAFAQSfGDGVHTSIP 2834
Cdd:cd00834 198 AGFAALRALST------RNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAeILGYGAS-SDAYHITAP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2835 APGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNETELherLADALGRSEGAPLfVVSQKSLTGHA 2914
Cdd:cd00834 271 DPDGEGAARA-------MRAALADAGLSPEDIDYINAHGTSTPLNDAAESKA---IKRVFGEHAKKVP-VSSTKSMTGHL 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622703340 2915 KGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDElagsAHFVWVRDTLRlggKFPLKAGMLTSLGFG 2980
Cdd:cd00834 340 LGAAGAVEAIATLLALRDGVLPPTINLEEPDPE----CDLDYVPNEAR---EAPIRYALSNSFGFG 398
|
|
| DNA_pol_B_N |
pfam18094 |
DNA polymerase beta N-terminal domain; This is the N-terminal domain of DNA polymerase beta ... |
935-1037 |
1.34e-26 |
|
DNA polymerase beta N-terminal domain; This is the N-terminal domain of DNA polymerase beta present in Homo sapiens. DNA polymerase beta is a repair enzyme that has a key role in the base excision repair of simple DNA lesions.
Pssm-ID: 436268 Cd Length: 104 Bit Score: 106.34 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 935 VVLDAPDVRWAGRTVTNPVHRIADPAEWQVHDGpenPRATHSSTGARL----QTHGDDVALSVPVSGTWVDIRFTLPANT 1010
Cdd:pfam18094 1 FVLAAPDVSWAGRLTDNPVRRLGDPSAWELTED---DRAAHAPTGATLlihtDTGWDHAGLSVPHAVRHLVIPLTLPASA 77
|
90 100
....*....|....*....|....*..
gi 622703340 1011 VDGGTPVIATEDATSAMRTVLAIAAGV 1037
Cdd:pfam18094 78 ATGGVPVVTRERASAAMRELLAGAAGG 104
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
1331-1688 |
1.93e-25 |
|
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: 109.09 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1331 KTVYAFPGQGIQHKGMGMEVRARSKAARKVWDTADkftrDTLGFSVLHVVRDNPTSIiasgvhyhhpdgvLYLTQFTQVA 1410
Cdd:TIGR00128 2 KIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQAS----EALGYDLKKLCQEGPAEE-------------LNKTQYTQPA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1411 MATVAAAQVAEMREQGAFvEGAIACGHSVGEYTALACvTGIYQLEALLEMVFHRGSKMHDIVPRDELGrsnyrLAAIrps 1490
Cdd:TIGR00128 65 LYVVSAILYLKLKEQGGL-KPDFAAGHSLGEYSALVA-AGALDFETALKLVKKRGELMQEAVPEGGGA-----MAAV--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1491 qIDLDDADVpafVAGIAESTGEFLEIVNFNlRGSQYAIAGTVRGLEALEAEVErrrelTGGRRSFILVPgIDVPFHSRVL 1570
Cdd:TIGR00128 135 -IGLDEEQL---AQACEEATENDVDLANFN-SPGQVVISGTKDGVEAAAALFK-----EMGAKRAVPLE-VSGAFHSRFM 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1571 RVGVAEFRRSLDRVMPRDADpdliigryipnlVPRLFTLDRDFIQEIRDLVpaepldeiladydtwlrerpremartvfi 1650
Cdd:TIGR00128 204 KPAAEKFAETLEACQFNDPT------------VPVISNVDAKPYTNGDRIK----------------------------- 242
|
330 340 350
....*....|....*....|....*....|....*...
gi 622703340 1651 ELLAWQFASPVRWIETQDLLfieeaaGGLGVERFVEIG 1688
Cdd:TIGR00128 243 EKLSEQLTSPVRWTDSVEKL------MARGVTEFAEVG 274
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1310-2178 |
8.45e-25 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 114.20 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1310 DVAARVGSDLVMSASARlAAPKTVYAFPGQGIQHKGMGMEVRARSKAARKVWDTADKFTRDTLGFSVLHVVRDNPtsiia 1389
Cdd:COG3321 508 ALAAGEAAPGVVTGAAA-AAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDE----- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1390 sgvhyhhPDGVLYLTQFTQVAMATVAAAQVAEMREQGafVEGAIACGHSVGEYTAlACVTGIYQLEALLEMVFHRGSKMH 1469
Cdd:COG3321 582 -------EESRLDRTEVAQPALFAVEYALARLWRSWG--VRPDAVIGHSVGEYAA-ACVAGVLSLEDALRLVAARGRLMQ 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1470 DIVPRDelgrsnyRLAAIRpsqidLDDADVPAFVAGIAEstgefLEIVNFNLRgSQYAIAGTVRGLEALEAEVERRrelt 1549
Cdd:COG3321 652 ALPGGG-------AMLAVG-----LSEEEVEALLAGYDG-----VSIAAVNGP-RSTVVSGPAEAVEALAARLEAR---- 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1550 gGRRSFILvpGIDVPFHSRVLRVGVAEFRRSLDRVMPRDADPDLIIGryipnlvprlftldrdfiqeirdlVPAEPLDEI 1629
Cdd:COG3321 710 -GIRARRL--PVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISN------------------------VTGTWLTGE 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1630 LADYDTWLR------------ERPREMARTVFIE------LLAW-----QFASPVRWIETQ-----DLLFIEEAAGGL-- 1679
Cdd:COG3321 763 ALDADYWVRhlrqpvrfadavEALLADGVRVFLEvgpgpvLTGLvrqclAAAGDAVVLPSLrrgedELAQLLTALAQLwv 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1680 -GVErfveigVKSSPTVAGLATNTLKLPEYA--HSTVEVLNAERDAAVLFATDTDPEPEPEEDEPVAESPAPDVVSEAAP 1756
Cdd:COG3321 843 aGVP------VDWSALYPGRGRRRVPLPTYPfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1757 VAPAASSAGPRPDDLVFDAADATLALIALSAKMR-IDQIEELDSIESITDGASSRRNQLLVDLGSELNLGAIDGAAESDL 1835
Cdd:COG3321 917 AALALAAAALAALLALVALAAAAAALLALAAAAAaAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL 996
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1836 AGLRSQVTKLARTYKPYGPVLSDAINDQLRTVLGPSGKRPGAIAERVKKTWELGEGWAKHVTVEVALGTREGSSVRGGAM 1915
Cdd:COG3321 997 AAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAE 1076
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1916 GHLHEGALADAASVDKVIDAAVASVAARQGVSVALPSAGSGGGATIDAAALSEFTDQITGREGVLASAARLVLGQLGLDD 1995
Cdd:COG3321 1077 LALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAA 1156
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1996 PVNALPAAPDSELIDLVTAELGADWPRLVAPVFDPKKAVVFDDRWASAREDLVKLWLTDEGDIDADWPRLAERFEGAGHV 2075
Cdd:COG3321 1157 AALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALL 1236
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2076 VATQATWWQGKSLAAGRQIHASLYGRIAAGAENPEPGRYGGEVAVVTGASKGSIAASVVARLLDGGATVIATTSKLDEER 2155
Cdd:COG3321 1237 ALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAA 1316
|
890 900
....*....|....*....|...
gi 622703340 2156 LAFYRTLYRDHARYGAALWLVAA 2178
Cdd:COG3321 1317 AAAALAAALLAAALAALAAAVAA 1339
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
1333-1602 |
1.85e-24 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 107.17 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1333 VYAFPGQGIQHKGMGMEVRARSKAARKVWDTADKFTRDTLGFSVLHVVRDNPTSIIASgvhyhhpdgvlylTQFTQVAMA 1412
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNNPEGTLDG-------------TQFVQPALF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1413 TVAAAQVAEMREQGafVEGAIACGHSVGEYTALACVTGIYQLEALLEMVFHRGSKMHDIVPRDELGRSN----------- 1481
Cdd:pfam00698 68 AMQIALAALLQSYG--VRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELsaeeveqrwpd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1482 --YRLAAIRPSQIDLD--DADVPAFVAGI-AESTGEFLEIVNFNLRGSQYAIAGTVRGLE-------------------- 1536
Cdd:pfam00698 146 dvVGAVVNSPRSVVISgpQEAVRELVERVsKEGVGALVENVNYAVHSPQMDAIAPALLSAladiaprtprvpfisstsid 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 622703340 1537 -----ALEAEVERR--------RELTGGRRSFILVPGIDVPFHSRVLRVGVAEFRRSLdrvmprDADPDLIIGRYIPNL 1602
Cdd:pfam00698 226 psdqrTLSAEYWVRnlrspvrfAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSAS------DGKVATLVGTLIRDQ 298
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2816-2942 |
1.49e-22 |
|
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: 95.33 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2816 LAVVAFAQSFGDGVHTSIPAPGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNETELherLADALG 2895
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARA-------IRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEA---LKRVFG 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 622703340 2896 RSE-GAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLD 2942
Cdd:pfam02801 71 SGArKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
2693-2988 |
1.83e-22 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 103.23 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2693 VLPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDD-LTLEGIIGFGDMAATADtsmmr 2771
Cdd:PTZ00050 142 ILGNMAAGLVAIKH-KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEAsITPVSFAGFSRMRALCT----- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2772 grGIHD--SKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA-VVAFAQSfGDGVHTSIPAPGLGALGAGrggk 2848
Cdd:PTZ00050 216 --KYNDdpQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAeIRGYGSS-SDAHHITAPHPDGRGARRC---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2849 dspLARALAKLG-VAADDVAVISKHDTSTLANDpnETELHErLADALGRSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLC 2927
Cdd:PTZ00050 289 ---MENALKDGAnININDVDYVNAHATSTPIGD--KIELKA-IKKVFGDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTI 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 622703340 2928 QILRDGVIPPNRSLDCVDDELAGSAHFVWVRDTLRlggkfPLKAGMLTSLGFGHVSglVAL 2988
Cdd:PTZ00050 363 LSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQ-----SIDAVLSTSFGFGGVN--TAL 416
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
2692-2990 |
5.96e-22 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 100.90 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2692 EVLPNIIAAHVVQSyVGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDD----LTLegiIGFGDMAATADT 2767
Cdd:PRK05952 119 DTLPHQAAIAAARQ-IGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEApitpLTL---AGFQQMGALAKT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2768 SmmrgrgihdskfSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVAfaqSFG---DGVHTSIPAPGLGALGAG 2844
Cdd:PRK05952 195 G------------AYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQIL---GFGltcDAYHMSAPEPDGKSAIAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2845 rggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNETELHERLAdalgrseGAPLFVVSQKSLTGHAKGGAAVFQMM 2924
Cdd:PRK05952 260 -------IQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF-------PHRVAVSSTKGATGHTLGASGALGVA 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622703340 2925 GLCQILRDGVIPPNRSLDCVDDELagsahfvwvrDTLRLGGKFPLKAGMLTSLGFGHVSGLVALVH 2990
Cdd:PRK05952 326 FSLLALRHQQLPPCVGLQEPEFDL----------NFVRQAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| R_hydratase_like |
cd03441 |
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ... |
1212-1329 |
1.78e-21 |
|
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.
Pssm-ID: 239525 [Multi-domain] Cd Length: 127 Bit Score: 92.33 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1212 VTITaPVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQArPPARLVGWTARFLGMVRPGD 1291
Cdd:cd03441 8 RTVT-EADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGT-DGANLGSQSVRFLAPVFPGD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 622703340 1292 EVDFRVERVGI----DQGAEIVDVAARVGSDLVMSASARLAA 1329
Cdd:cd03441 86 TLRVEVEVLGKrpskGRGVVTVRTEARNQGGEVVLSGEATVL 127
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
2717-2986 |
5.70e-21 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 98.27 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2717 VAACATAAVSVEEGVDKIRLGKA-QLVVAGGLDDLTLEGIIGFGDMAATADtsmmrgRGIHDSKFSRPNDRRRLGFVEAQ 2795
Cdd:PRK08439 159 VTACAAGTHAIIEAVKTIMLGGAdKMLVVGAESAICPVGIGGFAAMKALST------RNDDPKKASRPFDKDRDGFVMGE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2796 GGGTILLARGDLALRMGLPVLA-VVAFAQSfGDGVHTSIPAPglgalgagrggkDSPLaRALAKLGVAADDVAV--ISKH 2872
Cdd:PRK08439 233 GAGALVLEEYESAKKRGAKIYAeIIGFGES-GDANHITSPAP------------EGPL-RAMKAALEMAGNPKIdyINAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2873 DTSTLANDPNETelhERLADALGRSEGAPLfVVSQKSLTGHAKGGA----AVFQMMGlcqiLRDGVIPPNRSLDCVDDEl 2948
Cdd:PRK08439 299 GTSTPYNDKNET---AALKELFGSKEKVPP-VSSTKGQIGHCLGAAgaieAVISIMA----MRDGILPPTINQETPDPE- 369
|
250 260 270
....*....|....*....|....*....|....*...
gi 622703340 2949 agsAHFVWVRDTLRlggKFPLKAGMLTSLGFGHVSGLV 2986
Cdd:PRK08439 370 ---CDLDYIPNVAR---KAELNVVMSNSFGFGGTNGVV 401
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
2601-2982 |
7.52e-20 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 95.06 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2601 VGGQIPT-------GFDPTVWgISADMAGSIDRLAVWNMVATVDAFLSSGFSPAEVM-RYVHPSLVANTQGTGMGGGTSM 2672
Cdd:PRK06333 50 IGGQVPDlaedaeaGFDPDRY-LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEdRERTATIIGSGVGGFPAIAEAV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2673 QTMyhgNLLGRNKPNDIF-QEVLPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGG----L 2747
Cdd:PRK06333 129 RTL---DSRGPRRLSPFTiPSFLTNMAAGHVSIRY-GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGteaaI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2748 DDLTLEGII-------GFGDMAATAdtsmmrgrgihdskfSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA-VV 2819
Cdd:PRK06333 205 DRVSLAGFAaaralstRFNDAPEQA---------------SRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAeLV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2820 AFAQSfGDGVHTSIPAPGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNETelhERLADALGRSEG 2899
Cdd:PRK06333 270 GYGTS-ADAYHMTAGPEDGEGARRA-------MLIALRQAGIPPEEVQHLNAHATSTPVGDLGEV---AAIKKVFGHVSG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2900 apLFVVSQKSLTGHAKGGA----AVFQMMGlcqiLRDGVIPPNRSLDCVDDELAGsahFVWVRDTLRlggKFPLKAGMLT 2975
Cdd:PRK06333 339 --LAVSSTKSATGHLLGAAggveAIFTILA----LRDQIAPPTLNLENPDPAAEG---LDVVANKAR---PMDMDYALSN 406
|
....*..
gi 622703340 2976 SLGFGHV 2982
Cdd:PRK06333 407 GFGFGGV 413
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2576-2808 |
7.72e-20 |
|
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: 91.54 E-value: 7.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2576 STDWQVIRKAGTEIR-VPRKT-------KLSRVVGGQIPTG---------FDPTVWGISADMAGSIDRLAVWNMVATVDA 2638
Cdd:pfam00109 19 EEFWENLLEGRDGISeIPADRwdpdklyDPPSRIAGKIYTKwgglddifdFDPLFFGISPREAERMDPQQRLLLEAAWEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2639 FLSSGFSPAEVmryvHPSLVANTQGTGMGGGTSMQTMYHGNllGRNKPNDIFQEVLPNIIAAHVVQSYvGSYGAMIHPVA 2718
Cdd:pfam00109 99 LEDAGITPDSL----DGSRTGVFIGSGIGDYAALLLLDEDG--GPRRGSPFAVGTMPSVIAGRISYFL-GLRGPSVTVDT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2719 ACATAAVSVEEGVDKIRLGKAQLVVAGGLD-DLTLEGIIGFGDMAATADTsmmrGRgihdSKFSRPNDrrrLGFVEAQGG 2797
Cdd:pfam00109 172 ACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPD----GP----CKAFDPFA---DGFVRGEGV 240
|
250
....*....|.
gi 622703340 2798 GTILLARGDLA 2808
Cdd:pfam00109 241 GAVVLKRLSDA 251
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2694-2947 |
1.74e-19 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 94.09 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2694 LPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDD-LTLEGIIGFGdmAATAdtsmMRG 2772
Cdd:PRK07314 137 IINMAAGHVSIRY-GAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAaITPLGIAGFA--AARA----LST 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2773 RGIHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA-VVAFAQSfGDGVHTSIPAPGLGALGAGrggkdsp 2851
Cdd:PRK07314 210 RNDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAeVVGYGMT-GDAYHMTAPAPDGEGAARA------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2852 LARALAKLGVAADDVAVISKHDTSTLANDPNETELHERladALGrsEGAP-LFVVSQKSLTGHAKGGA----AVFQMMGl 2926
Cdd:PRK07314 282 MKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKR---VFG--EHAYkVAVSSTKSMTGHLLGAAgaveAIFSVLA- 355
|
250 260
....*....|....*....|.
gi 622703340 2927 cqiLRDGVIPPNRSLDCVDDE 2947
Cdd:PRK07314 356 ---IRDQVIPPTINLDNPDEE 373
|
|
| MaoC |
COG2030 |
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism]; |
1212-1331 |
1.06e-18 |
|
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
Pssm-ID: 441633 [Multi-domain] Cd Length: 140 Bit Score: 84.94 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1212 VTITApVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQARpPARLVGWTARFLGMVRPGD 1291
Cdd:COG2030 16 RTVTE-EDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTA-VANLGLQEVRFLRPVRVGD 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 622703340 1292 EVDFRVERVGIDQ--GAEIVDVAARV---GSDLVMSASARLAAPK 1331
Cdd:COG2030 94 TLRARVEVLEKREskSRGIVTLRTTVtnqDGEVVLTGEATVLVPR 138
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
2718-2938 |
4.18e-17 |
|
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: 86.84 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2718 AACATAAVSVEEGVDKIRLGKAQLVVAGGLD-DLTLEGIIGFGdmaatadtsmmRGRGIHDSKFSRPNDRRRLGFVEAQG 2796
Cdd:cd00833 168 TACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFS-----------KAGMLSPDGRCRPFDADADGYVRGEG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2797 GGTILLARGDLALRMGLPVLAVV-AFAQSFgDGVHTSIPAPglgalgagrggkdSP------LARALAKLGVAADDVAVI 2869
Cdd:cd00833 237 VGVVVLKRLSDALRDGDRIYAVIrGSAVNQ-DGRTKGITAP-------------SGeaqaalIRRAYARAGVDPSDIDYV 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 622703340 2870 SKHDTSTLANDPNETElheRLADALG--RSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPN 2938
Cdd:cd00833 303 EAHGTGTPLGDPIEVE---ALAKVFGgsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPN 370
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2719-2980 |
1.28e-16 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 86.19 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2719 ACATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLEgiIGFGDMAATADTSMmrgRGIHDSKFSRPNDRRRLGFVEAQGGG 2798
Cdd:PLN02787 290 ACATSNFCILNAANHIIRGEADVMLCGGSDAAIIP--IGLGGFVACRALSQ---RNDDPTKASRPWDMNRDGFVMGEGAG 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2799 TILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLA 2878
Cdd:PLN02787 365 VLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILC-------IEKALAQSGVSKEDVNYINAHATSTKA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2879 NDPNEtelHERLADALGRSEGapLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDElagsahfvwVR 2958
Cdd:PLN02787 438 GDLKE---YQALMRCFGQNPE--LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESG---------VD 503
|
250 260
....*....|....*....|....*
gi 622703340 2959 DTLRLGGK---FPLKAGMLTSLGFG 2980
Cdd:PLN02787 504 TKVLVGPKkerLDIKVALSNSFGFG 528
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2696-2942 |
1.03e-15 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 82.36 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2696 NIIAAHVvQSYVGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLE-GIIGFGdmAATAdtsmMRGRG 2774
Cdd:PRK08722 141 NMIAGNL-SIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPlGMAGFG--AAKA----LSTRN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2775 IHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA-VVAFAQSfGDGVHTSIPAPGLGALGAGrggkdspLA 2853
Cdd:PRK08722 214 DEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAeLVGFGMS-GDAYHMTSPSEDGSGGALA-------ME 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2854 RALAKLGVAADDVAVISKHDTSTLANDPNETELHERladALGRSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDG 2933
Cdd:PRK08722 286 AAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKR---ALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQ 362
|
....*....
gi 622703340 2934 VIPPNRSLD 2942
Cdd:PRK08722 363 IVPPTINLD 371
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2693-2980 |
5.67e-15 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 80.22 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2693 VLPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGG----LDDLTLEGI-------IGFGDM 2761
Cdd:PLN02836 158 ILINMAAGHVSIRY-GFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGtessIDALSIAGFsrsralsTKFNSC 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2762 AATAdtsmmrgrgihdskfSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGAL 2841
Cdd:PLN02836 237 PTEA---------------SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2842 GAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNE-TELHERLADalgRSEGAPLFVVSQKSLTGHAKGGA-- 2918
Cdd:PLN02836 302 VLA-------MTRALQQSGLHPNQVDYVNAHATSTPLGDAVEaRAIKTVFSE---HATSGGLAFSSTKGATGHLLGAAga 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 622703340 2919 --AVFQMMGlcqiLRDGVIPPNRSLDCVDDELAGsaHFVwvrdTLRLGGKFPLKAGMLTSLGFG 2980
Cdd:PLN02836 372 veAIFSVLA----IHHGIAPPTLNLERPDPIFDD--GFV----PLTASKAMLIRAALSNSFGFG 425
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
1330-1540 |
5.52e-14 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 76.34 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1330 PKTVYAFPGQGIQHKGMGMEVrARSKAARKVWDTAdkftRDTLGFSVLHVVRDNPTSIIASgvhyhhpdgvlylTQFTQV 1409
Cdd:PLN02752 38 PTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDKA----SEILGYDLLDVCVNGPKEKLDS-------------TVVSQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1410 A--MATVAAAQVAEMREQGAFVEGAI--ACGHSVGEYTALaCVTGIYQLEALLEMVFHRGSKMHDIVPRDELGRSnyrla 1485
Cdd:PLN02752 100 AiyVASLAAVEKLRARDGGQAVIDSVdvCAGLSLGEYTAL-VFAGALSFEDGLKLVKLRGEAMQAAADAGPSGMV----- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 622703340 1486 airpSQIDLDDADVPAFVAGIAESTGEF--LEIVNFNLRGSqYAIAGTVRGLEALEA 1540
Cdd:PLN02752 174 ----SVIGLDSDKVQELCAAANEEVGEDdvVQIANYLCPGN-YAVSGGKKGIDAVEA 225
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
1336-1594 |
1.48e-13 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 73.98 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1336 FPGQGIQHKGMGMEVRARSKAARKVWDTADKFTRDTLGFSVLHVVRDNPtsiiasgvhyhhPDGVLYLTQFTQVAMATVA 1415
Cdd:smart00827 2 FTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGED------------GAASLLDTEVAQPALFAVQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1416 AAQVAEMREQGafVEGAIACGHSVGEYTAlACVTGIYQLEALLEMVFHRGSKMHDIVPRDelgrsnyRLAAIRpsqidLD 1495
Cdd:smart00827 70 VALARLLRSWG--VRPDAVVGHSSGEIAA-AYVAGVLSLEDAARLVAARGRLMQALPGGG-------AMLAVG-----LS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1496 DADVPAFVAGIAEStgefLEIVNFNlrG-SQYAIAGTVRGLEALEAEVERRreltgGRRSFILvpGIDVPFHSRVLRVGV 1574
Cdd:smart00827 135 EEEVEPLLAGVPDR----VSVAAVN--SpSSVVLSGDEDAVDELAARLEAE-----GIFARRL--KVDHAFHSPHMEPIL 201
|
250 260
....*....|....*....|
gi 622703340 1575 AEFRRSLDRVMPRDADPDLI 1594
Cdd:smart00827 202 DEFRAALAGLTPRPPRIPFV 221
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
94-361 |
1.97e-13 |
|
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: 74.01 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 94 VRALAAEDPvpsDKHLTSAAVSVPGVLLTQIAATRALARQGMDlvatpPVAMAGHSQGVLAveALKAGGARDVE-LFALA 172
Cdd:COG0331 43 LSALCFEGP---EEELNLTENTQPAILAASVAAYRALEEEGIR-----PDAVAGHSLGEYS--ALVAAGALSFEdALRLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 173 QLIGAA-GTLVARRRGisvlgdrpPMVSVTNADPERIGRLLDEFAQDVrtVLppVLSIRNGRRAVVITGTPEQLSRFELY 251
Cdd:COG0331 113 RLRGRLmQEAVPAGPG--------GMAAVLGLDDEEVEALCAEAAQGE--VV--EIANYNSPGQIVISGEKEAVEAAAEL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 252 CrqiseKEEADRKnkvrggdvfspvFEPVQVEVGFHTPRLSDGIDIVAgwAEKAGLDVA----------LARELADAILI 321
Cdd:COG0331 181 A-----KEAGAKR------------AVPLPVSGPFHTPLMAPAAEKLA--EALAAVTFAdpkipvvsnvDAAPVTDPEEI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 622703340 322 RK---------VDWVDEITRVHAAGARWILDLGPGDILTRLTAPVIRGL 361
Cdd:COG0331 242 REllvrqltspVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGV 290
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
2691-2948 |
2.33e-13 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 75.15 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2691 QEVLPNIIAAhVVQSYVGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLDD-LTLEGIIGFGDMAATADTSM 2769
Cdd:PRK07910 143 QMYMPNGPAA-AVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETrIEAVPIAGFAQMRIVMSTNN 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2770 MRGRGIhdskfSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALGAGrggkd 2849
Cdd:PRK07910 222 DDPAGA-----CRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHA----- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2850 spLARALAKLGVAADDVAVISKHDTSTLANDPNETElheRLADALGRSEGAplfVVSQKSLTGHAKGGAAVFQMMGLCQI 2929
Cdd:PRK07910 292 --MTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK---AINNALGGHRPA---VYAPKSALGHSVGAVGAVESILTVLA 363
|
250
....*....|....*....
gi 622703340 2930 LRDGVIPPNRSLDCVDDEL 2948
Cdd:PRK07910 364 LRDGVIPPTLNLENLDPEI 382
|
|
| SAV4209_like |
cd03453 |
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ... |
1214-1315 |
9.54e-13 |
|
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.
Pssm-ID: 239537 [Multi-domain] Cd Length: 127 Bit Score: 67.35 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1214 ITAPV---DMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTatdGQARPPARLVGWTARFLGMVRPG 1290
Cdd:cd03453 8 LTPPVsraDLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVT---DWVGDPGRVVSFGVRFTKPVPVP 84
|
90 100
....*....|....*....|....*
gi 622703340 1291 DEVDFRVERVGIDQGAEIVDVAARV 1315
Cdd:cd03453 85 DTLTCTGIVVEKTVADGEDALTVTV 109
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
2694-2950 |
1.45e-12 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 71.68 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2694 LPNIIAAHVV--QSYVGSYGAmihPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLddltlEGIIgfgDMAATADTSMMR 2771
Cdd:PRK14691 66 LVNLAAGHVSikHHFKGPIGA---PVTACAAGVQAIGDAVRMIRNNEADVALCGGA-----EAVI---DTVSLAGFAAAR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2772 GRGIH----DSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALGAGrgg 2847
Cdd:PRK14691 135 ALSTHfnstPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2848 kdspLARALAKLGVAADDVAVISKHDTSTLANDPNETELHERLAdalgrSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLC 2927
Cdd:PRK14691 212 ----MKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLF-----GESNALAITSTKSATGHLLGAAGGLETIFTV 282
|
250 260
....*....|....*....|...
gi 622703340 2928 QILRDGVIPPNRSLDCVDDELAG 2950
Cdd:PRK14691 283 LALRDQIVPATLNLENPDPAAKG 305
|
|
| HDE_HSD |
cd03448 |
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ... |
1227-1329 |
3.13e-12 |
|
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.
Pssm-ID: 239532 [Multi-domain] Cd Length: 122 Bit Score: 65.70 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1227 SGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQARpPARLVGWTARFLGMVRPGDEVDFRVERVGidqga 1306
Cdd:cd03448 24 SGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGD-PARFKAIKVRFSSPVFPGETLRTEMWKEG----- 97
|
90 100
....*....|....*....|....*
gi 622703340 1307 EIVDVAARV--GSDLVMSASARLAA 1329
Cdd:cd03448 98 NRVIFQTKVveRDVVVLSNGAALLA 122
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
38-931 |
3.76e-12 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 72.60 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 38 FGGQGSAWLETLEELVSAtgiETELATLVGEAELLLDPVTdelivvrpiGFEPLQWVRalaaedPVPSDKHLTSAAVSVP 117
Cdd:COG3321 533 FPGQGSQYVGMGRELYET---EPVFRAALDECDALLRPHL---------GWSLREVLF------PDEEESRLDRTEVAQP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 118 GVLLTQIAATRALARQGMDlvatpPVAMAGHSQGVLAveALKAGGARDVElfalaqligAAGTLVARR-RGISVLGDRPP 196
Cdd:COG3321 595 ALFAVEYALARLWRSWGVR-----PDAVIGHSVGEYA--AACVAGVLSLE---------DALRLVAARgRLMQALPGGGA 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 197 MVSVtNADPERIGRLLDEFAQdvrtvlpPVLSIRNGRRAVVITGTPEQLSRFElycRQISEKEEADRKNKVRGGdvF-SP 275
Cdd:COG3321 659 MLAV-GLSEEEVEALLAGYDG-------VSIAAVNGPRSTVVSGPAEAVEALA---ARLEARGIRARRLPVSHA--FhSP 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 276 VFEPVQVE-------VGFHTPRLSDGIDIVAGWAEKAGLDVA-LARELADAilirkVDWVDEITRVHAAGARWILDLGPG 347
Cdd:COG3321 726 LMEPALEEfraalagVTPRAPRIPLISNVTGTWLTGEALDADyWVRHLRQP-----VRFADAVEALLADGVRVFLEVGPG 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 348 DILTRLTAPVIRGLGIGIVPAATRGGQR----------NLFTVGATPEVARAWSSYAPTVVRLPdgrvklSTKFTRLTGR 417
Cdd:COG3321 801 PVLTGLVRQCLAAAGDAVVLPSLRRGEDelaqlltalaQLWVAGVPVDWSALYPGRGRRRVPLP------TYPFQREDAA 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 418 SPILLAGMTPTTVDAKIVAAAANAGHWAELAGGGQVTEEIFGNRIEQMAGLLEPGRTYQfnALFLDPYLWKLQVGGKRLV 497
Cdd:COG3321 875 AALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV--ALAAAAAALLALAAAAAAA 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 498 QKARQSGAAIDGVVISAGIPDLDEAVELIDELGDIGISHVVFKPGTIEQIRSVIRIATEVPTKPVIMHVEGGRAGGHHSW 577
Cdd:COG3321 953 AAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAA 1032
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 578 EDLDDLLLATYSELRSRANITVCVGGGIGTPRRAAEYLSGRWAQAYGFPLMPIDGILVGTAAMATKESTTSPSVKRMLVD 657
Cdd:COG3321 1033 AALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALL 1112
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 658 TQGTDQWISAGKAQGGMASSRSQLGADIHEIDNSASRCGRLLDEVAGDAEAVAERRDEIIAAMAKTAKPYFGDVADMTYL 737
Cdd:COG3321 1113 AALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGL 1192
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 738 QWLRRYVELAIGEGNSTADTASVGSPWLADTWRDRFEQMLQRAEARLHPQDFGPIQTLFTDAGLLDNPQQAIAALLARYP 817
Cdd:COG3321 1193 AALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLA 1272
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 818 DAETVQLHPADVPFFVTLCKTLGKPVNFVPVIDQDVRRWWRSDSLWQAHDARYDADAVCIIPGTASVAGITRMDEPVGEL 897
Cdd:COG3321 1273 ALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAA 1352
|
890 900 910
....*....|....*....|....*....|....
gi 622703340 898 LDRFEQAAIDEVLGAGVEPKDVASRRLGRADVAG 931
Cdd:COG3321 1353 AAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
2742-2990 |
5.53e-12 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 70.83 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2742 VVAGGLDDLT---LEGIIGFGDMAATADTSmmrgrgiHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAV 2818
Cdd:PRK07103 190 IAVGALMDLSyweCQALRSLGAMGSDRFAD-------EPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2819 VAFAQSFGDGvhTSIPAPGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDpnETELherlaDALGRSE 2898
Cdd:PRK07103 263 LLGWSMRLDA--NRGPDPSLEGEMRV-------IRAALRRAGLGPEDIDYVNPHGTGSPLGD--ETEL-----AALFASG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2899 GAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLD-CVDDELAgsahfvWVRDTLRLGGkfpLKAGMLTSL 2977
Cdd:PRK07103 327 LAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDePIDERFR------WVGSTAESAR---IRYALSLSF 397
|
250
....*....|...
gi 622703340 2978 GFGHVSGLVALVH 2990
Cdd:PRK07103 398 GFGGINTALVLER 410
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
2682-2937 |
7.42e-12 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 70.43 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2682 GRNKPNDIFQEVLPNIIAAHVVQSYvGSYGAMIHPVAACATAAVSVEEGVDKIRLGKAQLVVAGGLD-DLTLEGIIGFGD 2760
Cdd:PRK06501 138 RGGRFDALHERFQFGSIADRLADRF-GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgSVSAEALIRFSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2761 MAA--TADTSmmrgrgihDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGL 2838
Cdd:PRK06501 217 LSAlsTQNDP--------PEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2839 galgagrggkdSP----LARALAKLGVAADDVAVISKHDTSTLANDPNEtelHERLADALG-RSEGAPlfVVSQKSLTGH 2913
Cdd:PRK06501 289 -----------SPaigaIRAALADAGLTPEQIDYINAHGTSTPENDKME---YLGLSAVFGeRLASIP--VSSNKSMIGH 352
|
250 260
....*....|....*....|....*...
gi 622703340 2914 --AKGGA--AVFQMmglcQILRDGVIPP 2937
Cdd:PRK06501 353 tlTAAGAveAVFSL----LTIQTGRLPP 376
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
2718-2948 |
5.03e-11 |
|
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: 66.89 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2718 AACATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLEGIIGFgdmaatadtsMMRGRGIHDSKFSRPNDRRRLGFVEAQGG 2797
Cdd:cd00825 94 AACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEF----------DAMGALSTPEKASRTFDAAADGFVFGDGA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2798 GTILLARGDLALRMGLPVLAVVAFAQSFGDGVHTSIPAPGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTL 2877
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARA-------AKEALAVAGLTVWDIDYLVAHGTGTP 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 622703340 2878 ANDPNETELherLADALGrseGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDEL 2948
Cdd:cd00825 237 IGDVKELKL---LRSEFG---DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG 301
|
|
| R_hydratase |
cd03449 |
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ... |
1212-1329 |
4.90e-10 |
|
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.
Pssm-ID: 239533 [Multi-domain] Cd Length: 128 Bit Score: 59.87 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1212 VTITAPvDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAaaqhAVTATDGQARPP--ARLVGWTARFLGMVRP 1289
Cdd:cd03449 11 RTITEE-DVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTAS----LISAVLGTLLPGpgTIYLSQSLRFLRPVFI 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 622703340 1290 GDEVDFRVERVGIDQGAEIVDVAARV---GSDLVMSASARLAA 1329
Cdd:cd03449 86 GDTVTATVTVTEKREDKKRVTLETVCtnqNGEVVIEGEAVVLA 128
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
2714-2949 |
5.22e-10 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 64.62 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2714 IHPVA-ACATAAVSVEEGVDKIRLGKAQLVVAGGLDDLTLEGIIGFGDMAATAdtsmmrGRGIHDSKFSRPNDRRRLGFV 2792
Cdd:PRK09116 157 VIPTSsACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATS------TRNDAPELTPRPFDANRDGLV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2793 EAQGGGTILLARGDLALRMGLPVLA-VVAFAqSFGDGVHTSIPAPGLGALGagrggkdspLARALAKLGVAADDVAVISK 2871
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAeIVGFG-TNSDGAHVTQPQAETMQIA---------MELALKDAGLAPEDIGYVNA 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 622703340 2872 HDTSTLANDPNETElherladALGRSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDELA 2949
Cdd:PRK09116 301 HGTATDRGDIAESQ-------ATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACG 371
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
2608-2980 |
1.60e-09 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 62.77 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2608 GFDPTVWG-ISADMAGSIDR--------LAVWNMVATVDAFLSSGFSPAEVmryvhpslvANTQGtgmgggtsmqtmyhG 2678
Cdd:PRK07967 43 GMRSQVWGnVKLDPTGLIDRkvmrfmgdASAYAYLAMEQAIADAGLSEEQV---------SNPRT--------------G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2679 NLLGRNKPNDIFQEVLPNIIAAHVVQSYVGSYG---AM-------------IHPV-----AACATAAVSVEEGVDKIRLG 2737
Cdd:PRK07967 100 LIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAvtkAMastvsaclatpfkIKGVnysisSACATSAHCIGNAVEQIQLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2738 KAQLVVAGGLDDLTLEGIIGFGDMAAtadtsMMRGRGIHDSKFSRPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLA 2817
Cdd:PRK07967 180 KQDIVFAGGGEELDWEMSCLFDAMGA-----LSTKYNDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2818 VVAFAQSFGDGVHTSIPAPGLGALGagrggkdspLARALAKLGVAADdvaVISKHDTSTLANDPNETE-LHERLADAlgr 2896
Cdd:PRK07967 255 EIVGYGATSDGYDMVAPSGEGAVRC---------MQMALATVDTPID---YINTHGTSTPVGDVKELGaIREVFGDK--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2897 segAPlFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNRSLDCVDDELAGSAHFVWVRDTLRLGgkfplkAGMLTS 2976
Cdd:PRK07967 320 ---SP-AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELT------TVMSNS 389
|
....
gi 622703340 2977 LGFG 2980
Cdd:PRK07967 390 FGFG 393
|
|
| PRK08190 |
PRK08190 |
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated |
1219-1332 |
8.97e-09 |
|
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
Pssm-ID: 236180 [Multi-domain] Cd Length: 466 Bit Score: 60.66 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1219 DMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWlSAAAQHAV--TATDGqarPPARLVGWTARFLGMVRPGDEVDFR 1296
Cdd:PRK08190 30 DIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMW-GGALISAVlgTRLPG---PGTIYLGQSLRFRRPVRIGDTLTVT 105
|
90 100 110
....*....|....*....|....*....|....*....
gi 622703340 1297 VERVGIDQGAEIVDVAARV---GSDLVMSASARLAAPKT 1332
Cdd:PRK08190 106 VTVREKDPEKRIVVLDCRCtnqDGEVVITGTAEVIAPTE 144
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
507-662 |
2.41e-08 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 57.49 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 507 IDGVVISAGIPDldeavELIDELGDIGIShVVFKPGTIEQIRSVIRIATEVptkpVImhVEGGRAGGHHSWEDLDDLLLa 586
Cdd:cd04730 81 VPVVSFSFGPPA-----EVVERLKAAGIK-VIPTVTSVEEARKAEAAGADA----LV--AQGAEAGGHRGTFDIGTFAL- 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622703340 587 tYSELRSRANITVCVGGGIGTPRRAAEylsgrwAQAYGFplmpiDGILVGTAAMATKESTTSPSVKRMLVDTQGTD 662
Cdd:cd04730 148 -VPEVRDAVDIPVIAAGGIADGRGIAA------ALALGA-----DGVQMGTRFLATEESGASPAYKQALLAATAED 211
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
507-662 |
1.62e-07 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 55.89 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 507 IDGVVISAGIPDldeavELIDELGDIGIsHVVFKPGTIEQIRSVIRI---AtevptkpVImhVEGGRAGGHHSWEDLDDL 583
Cdd:COG2070 83 VPVVSTSAGLPA-----DLIERLKEAGI-KVIPIVTSVREARKAEKAgadA-------VV--AEGAEAGGHRGADEVSTF 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 622703340 584 LLAtySELRSRANITVCVGGGIGTPRRAAEylsgrwAQAYGfplmpIDGILVGTAAMATKESTTSPSVKRMLVDTQGTD 662
Cdd:COG2070 148 ALV--PEVRDAVDIPVIAAGGIADGRGIAA------ALALG-----ADGVQMGTRFLATEESPAHEAYKQALVDAKEED 213
|
|
| SDR |
cd02266 |
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ... |
2217-2361 |
7.58e-07 |
|
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187535 [Multi-domain] Cd Length: 186 Bit Score: 52.13 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2217 LFPFAAPRVVG---DLSEAGSRAEMEMKVLlwAVQRLIGGLSTIGAERDIASrlhVVLPGSPNRGMF-GGDGAYGEAKSA 2292
Cdd:cd02266 35 VVHNAAILDDGrliDLTGSRIERAIRANVV--GTRRLLEAARELMKAKRLGR---FILISSVAGLFGaPGLGGYAASKAA 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 622703340 2293 LDAVVSRWHAEsSWAARVSLAHALIGWTRGTGLM--GHNDAIVAAVEEAGVTTYSTDEMAALLLDLCDAES 2361
Cdd:cd02266 110 LDGLAQQWASE-GWGNGLPATAVACGTWAGSGMAkgPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPK 179
|
|
| SAV4209 |
cd03455 |
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ... |
1217-1328 |
4.30e-06 |
|
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The alpha- and gamma-proteobacterial members of this CD have, in addition to a hot dog fold, an N-terminal extension.
Pssm-ID: 239539 [Multi-domain] Cd Length: 123 Bit Score: 48.47 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1217 PVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTatdGQARPPARLVGWTARFLGMVRPGDEVDFR 1296
Cdd:cd03455 13 PTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVT---DWAGPDARVKSFAFRLGAPLYAGDTLRFG 89
|
90 100 110
....*....|....*....|....*....|....
gi 622703340 1297 VERVGIDQGAEI-VDVAARVGS-DLVMSASARLA 1328
Cdd:cd03455 90 GRVTAKRDDEVVtVELWARNSEgDHVMAGTATVA 123
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2718-2938 |
1.72e-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: 51.03 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2718 AACATAAVSVEEGVDKIRLGKAQLVVAGGLD-DLTLEGIIGFGDMAATADTsmmrGRgihdskfSRPNDRRRLGFVEAQG 2796
Cdd:COG3321 172 TACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLSPD----GR-------CRAFDADADGYVRGEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2797 GGTILLARGDLALRMGLPVLAVV---AFAQsfgDGVHTSIPAPglgalgagrggkdSP------LARALAKLGVAADDVA 2867
Cdd:COG3321 241 VGVVVLKRLSDALRDGDRIYAVIrgsAVNQ---DGRSNGLTAP-------------NGpaqaavIRRALADAGVDPATVD 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 622703340 2868 VISKHDTSTLANDPneTELhERLADALG--RSEGAPLFVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPN 2938
Cdd:COG3321 305 YVEAHGTGTPLGDP--IEA-AALTAAFGqgRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPT 374
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
38-248 |
2.75e-05 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
Pssm-ID: 465005 Cd Length: 239 Bit Score: 48.37 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 38 FGGQGSAWLETLEELVSATGiETELATLVGEA-ELLLDPVTDELIVVRPIgFEPLQWVRALAAEDPVPSDKHltsAAVSV 116
Cdd:pfam16073 3 FGDQTLDFLPGLRQLLRAKD-NPLLASFLERAaDALRAEISRLPRAERDS-LPRFTSLQELLERYYASGDKN---PALES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 117 PGVLLTQIAA-TRALARQGMDLVATPPVAMAGHSQGVLAVEALKAggARDV-ELFALA-QLIGAA---GTLVARRRGI-- 188
Cdd:pfam16073 78 ALLCIAQLGHfIDYLEENGEDYPSPSSTYLVGLCTGLLAAAAVSC--SRSLsELVPLAvEAVRIAfrlGLLVQRVADRle 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 622703340 189 -SVLGDRPPMVSVTNADPERIGRLLDEFAQDVRtvLPPV----LSIRNGrRAVVITGTPEQLSRF 248
Cdd:pfam16073 156 gSSSSPGSWSLVVPGLSEEEAEKALEQFNESKG--IPPAsrpyISAVSP-SSVTISGPPSTLELL 217
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
1248-1328 |
5.00e-05 |
|
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.
Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 44.77 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1248 PIVHGMWLSAAAQHAVTAT---DGQARPPARLVGWTARFLGMVRPGDEVDFRVERVGIDQGAEIVDVAARVGSD-LVMSA 1323
Cdd:cd03440 16 GIVHGGLLLALADEAAGAAaarLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGkLVATA 95
|
....*
gi 622703340 1324 SARLA 1328
Cdd:cd03440 96 TATFV 100
|
|
| Tryptophan_synthase_alpha |
cd04724 |
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ... |
489-638 |
6.81e-05 |
|
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.
Pssm-ID: 240075 Cd Length: 242 Bit Score: 47.09 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 489 LQVGGKRLVQKARQSGaaIDGVVIsagiPDL--DEAVELIDELGDIGISHVVFKPGT--IEQIRSVIRIATE----VPTK 560
Cdd:cd04724 89 LQYGLERFLRDAKEAG--VDGLII----PDLppEEAEEFREAAKEYGLDLIFLVAPTtpDERIKKIAELASGfiyyVSRT 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 622703340 561 PVImhveGGRAgghhsweDLDDLLLATYSELRSRANITVCVGGGIGTPRRAAEylSGRWAqaygfplmpiDGILVGTA 638
Cdd:cd04724 163 GVT----GART-------ELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAE--VAKYA----------DGVIVGSA 217
|
|
| PRK13693 |
PRK13693 |
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional |
1219-1328 |
8.24e-05 |
|
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
Pssm-ID: 184249 [Multi-domain] Cd Length: 142 Bit Score: 45.21 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1219 DMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQarpPARLVGWTARFLGMVR-PGD----EV 1293
Cdd:PRK13693 26 DLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGD---PGAVTEYNVRFTAVVPvPNDgkgaEL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 622703340 1294 DF--RVERVGIDQGAEIVDVAARVGSDLVMS---ASARLA 1328
Cdd:PRK13693 103 VFngRVKSVDPESKSVTIALTATTGGKKIFGraiASAKLA 142
|
|
| FAS_I_H |
pfam18314 |
Fatty acid synthase type I helical domain; This domain is found in the fatty acid synthase ... |
1998-2068 |
1.55e-04 |
|
Fatty acid synthase type I helical domain; This domain is found in the fatty acid synthase (FAS) complex present in species such as Mycobacterium smegmatis and Thermomyces lanuginosus. FAS is a homo-hexameric enzyme that catalyzes synthesis of fatty acid precursors of mycolic acids. This domain is composed of dimerization module 1 (DM1) and four-helix bundle (4HB), both of which are conserved parts of the acetyl transferase.
Pssm-ID: 465705 Cd Length: 203 Bit Score: 45.45 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 622703340 1998 NALPAAPDSELiDLVTAELGADWPRLVAPVFDPKKAVVFDDRWASAREDLVKLWL--------TDEGDIDADWPRLAER 2068
Cdd:pfam18314 34 SALVAELQAEL-DLWIAEHGDEYANGIKPIFDAKKARRYDSWWNWARQDILKLYYdllqgrlkDVDREITSRLQRILNR 111
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
2718-2939 |
1.75e-04 |
|
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: 45.90 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2718 AACATAAVSVEEGVDKIRLGKAQLVVAGGLDdltlegIIGFGDmaatadtsmmrgrgihdskfsrpndrrrlgfveaqGG 2797
Cdd:cd00327 66 QACATGLTALALAVQQVQNGKADIVLAGGSE------EFVFGD-----------------------------------GA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2798 GTILLARGDLALRMGLPVLAVVAFAQSFGDGVhTSIPAPGLGALGAGRGgkdsplaRALAKLGVAADDVAVISKHDTSTL 2877
Cdd:cd00327 105 AAAVVESEEHALRRGAHPQAEIVSTAATFDGA-SMVPAVSGEGLARAAR-------KALEGAGLTPSDIDYVEAHGTGTP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 622703340 2878 ANDPNETELherLADALGRSEGAplfVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIPPNR 2939
Cdd:cd00327 177 IGDAVELAL---GLDPDGVRSPA---VSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP 232
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
2734-2949 |
1.79e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 46.76 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2734 IRLGKAQLVVAGGLDDLTLEGIIGFGDMAATADTSmmrgrgihdskfSRPNDRRRLGFVEAQGGGTILLARGDLAlrmgl 2813
Cdd:PRK09185 174 LEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQP------------CRPFSANRDGINIGEAAAFFLLEREDDA----- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2814 pVLAVVAFAQSfGDGVHTSIPAPGLGALGAGrggkdspLARALAKLGVAADDVAVISKHDTSTLANDPNEtelherlADA 2893
Cdd:PRK09185 237 -AVALLGVGES-SDAHHMSAPHPEGLGAILA-------MQQALADAGLAPADIGYINLHGTATPLNDAME-------SRA 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2894 LGRSEGAPLFVVSQKSLTGHAKGGA----AVFQMmglcQILRDGVIPPNRSLDCVDDELA 2949
Cdd:PRK09185 301 VAAVFGDGVPCSSTKGLTGHTLGAAgaveAAICW----LALRHGLPPHGWNTGQPDPALP 356
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2782-2949 |
5.12e-04 |
|
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: 45.43 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2782 RPNDRRRLGFVEAQGGGTILLARGDLALRMGLPVLAVVA-FAQSFGDGVHTSIPAPglgalgagrggkdspLAR----AL 2856
Cdd:cd00832 216 LPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAgYAATFDPPPGSGRPPG---------------LARairlAL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2857 AKLGVAADDVAVISKHDTSTLANDPNETElheRLADALGRsEGAPlfVVSQKSLTGHAKGGAAVFQMMGLCQILRDGVIP 2936
Cdd:cd00832 281 ADAGLTPEDVDVVFADAAGVPELDRAEAA---ALAAVFGP-RGVP--VTAPKTMTGRLYAGGAPLDVATALLALRDGVIP 354
|
170
....*....|...
gi 622703340 2937 PNRSLDCVDDELA 2949
Cdd:cd00832 355 PTVNVTDVPPAYG 367
|
|
| YqjQ |
COG0300 |
Short-chain dehydrogenase [General function prediction only]; |
2116-2196 |
5.73e-04 |
|
Short-chain dehydrogenase [General function prediction only];
Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 44.48 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2116 GEVAVVTGASKGsIAASVVARLLDGGATVIATTskLDEERLAfyrTLYRDHARYGAALWLVAANMASYSDVDALVEWIGT 2195
Cdd:COG0300 5 GKTVLITGASSG-IGRALARALAARGARVVLVA--RDAERLE---ALAAELRAAGARVEVVALDVTDPDAVAALAEAVLA 78
|
.
gi 622703340 2196 E 2196
Cdd:COG0300 79 R 79
|
|
| FabA |
COG0764 |
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ... |
1281-1329 |
6.41e-04 |
|
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440527 Cd Length: 141 Bit Score: 42.49 E-value: 6.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 622703340 1281 ARFLGMVRPGDEVDFRVERVGIDQGAEIVDVAARVGSDLVmsASARLAA 1329
Cdd:COG0764 90 VKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLV--AEAELTF 136
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1116-1662 |
7.14e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 45.63 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1116 SLVHLDHAARVVgQLPTVPAQLTVTATAANATDTdmGRVVPVSVVVTGADGAVIATLEERFAILGRTGSAELADPARAGG 1195
Cdd:COG3321 850 SALYPGRGRRRV-PLPTYPFQREDAAAALLAAAL--AAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAAL 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1196 AVSANATDTPRRRRRDVTITAPVDMRPFAVVSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTATDGQARPPAR 1275
Cdd:COG3321 927 AALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLA 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1276 LVGWTARFLGMVRPGDEVDFRVERVGIDQGAEIVDVAARVGSDLVMSASARLAAPKTVYAFPGQGIQhkgmgmeVRARSK 1355
Cdd:COG3321 1007 AAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAA-------LAELAL 1079
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1356 AARKVWDTADKFTRDTLGFSVLHVVRDNPTSIIASGVHYHHPDGVLYLTQFTQVAMATVAAAQVAEMREQGAFVEGAIAC 1435
Cdd:COG3321 1080 AAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAAL 1159
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1436 GHSVGEYTALACVTGIYQLEALLEMVFHRGSKMHDIVPRDELGRSNYRLAAIRPSQIDLDDADVPAFVAGIAESTGEFLE 1515
Cdd:COG3321 1160 AAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALA 1239
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 1516 IVNFNLRGSQYAIAGTVRGLEALEAEVERRRELTGGRRSFILVPGIDVPFHSRVLRVGVAEFRRSLDRVMPRDADPDLII 1595
Cdd:COG3321 1240 AAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAA 1319
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 622703340 1596 GRYIPNLVPRLFTLDRDFIQEIRDLVPAEPLDEILADYDTWLRERPREMARTVFIELLAWQFASPVR 1662
Cdd:COG3321 1320 ALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PLN02864 |
PLN02864 |
enoyl-CoA hydratase |
1226-1291 |
8.49e-04 |
|
enoyl-CoA hydratase
Pssm-ID: 178455 [Multi-domain] Cd Length: 310 Bit Score: 44.39 E-value: 8.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 622703340 1226 VSGDHNPIHTDRAAALLAGLESPIVHGMWLSAAAQHAVTAT--DGQarpPARLVGWTARFLGMVRPGD 1291
Cdd:PLN02864 206 LSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCfcNGD---PTAVKTISGRFLLHVYPGE 270
|
|
| fused_HadA_HadB |
NF040620 |
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB; |
1223-1253 |
1.18e-03 |
|
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
Pssm-ID: 468592 [Multi-domain] Cd Length: 329 Bit Score: 44.06 E-value: 1.18e-03
10 20 30
....*....|....*....|....*....|.
gi 622703340 1223 FAVVSGDHNPIHTDRAAALLAGLESPIVHGM 1253
Cdd:NF040620 220 YAGVSGDPNPIHWSDEVARLAGLPTVVAHGM 250
|
|
| FabG |
COG1028 |
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ... |
2116-2193 |
1.26e-03 |
|
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 43.24 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 622703340 2116 GEVAVVTGASKGsIAASVVARLLDGGATVIATTskLDEERLAfyrTLYRDHARYGAALWLVAANMASYSDVDALVEWI 2193
Cdd:COG1028 6 GKVALVTGGSSG-IGRAIARALAAEGARVVITD--RDAEALE---AAAAELRAAGGRALAVAADVTDEAAVEALVAAA 77
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
105-357 |
2.30e-03 |
|
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: 42.68 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 105 SDKHLTSAAVSVPGVLLTQIAATRALARQGmdlvaTPPVAMAGHSQGVLAVeALKAGGARDVELFAL----AQLIGAAgt 180
Cdd:TIGR03131 45 DAEALASTRSAQLCILAAGVAAWRALLALL-----PRPSAVAGYSVGEYAA-AVVAGVLTFDDALRLvalrAALMDQA-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 181 lVARRRGisvlgdrppMVSVTNADPERIGRLLDEfaqdVRTVLppvlSIRNGRRAVVITGTPEQLSRFELYCRQisekee 260
Cdd:TIGR03131 117 -VPGGYG---------MLAVLGLDLAAVEALIAK----HGVYL----AIINAPDQVVIAGSRAALRAVAELARA------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 261 adrknkvRGGDVFspvfEPVQVEVGFHTPRLSD-----------------------GIDIVAGWAEKAGLDvALARELAd 317
Cdd:TIGR03131 173 -------AGASRA----KRLAVRVPSHTPLLAKaaeqfaealaeiplaaprlpylsGIDARLVRDAAQIRD-DLARQIA- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 622703340 318 ailiRKVDWVDEITRVHAAGARWILDLGPGDILTRLTAPV 357
Cdd:TIGR03131 240 ----TPVDWHDCMQAAYERGARLVIELGPGDVLTKLANEA 275
|
|
| adh_short |
pfam00106 |
short chain dehydrogenase; This family contains a wide variety of dehydrogenases. |
2117-2193 |
4.27e-03 |
|
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 41.06 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 622703340 2117 EVAVVTGASKGsIAASVVARLLDGGATVIATTSklDEERLAfyrTLYRDHARYGAALWLVAANMASYSDVDALVEWI 2193
Cdd:pfam00106 1 KVALVTGASSG-IGRAIAKRLAKEGAKVVLVDR--SEEKLE---AVAKELGALGGKALFIQGDVTDRAQVKALVEQA 71
|
|
| fabG |
PRK05565 |
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional |
2112-2191 |
4.57e-03 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
Pssm-ID: 235506 [Multi-domain] Cd Length: 247 Bit Score: 41.75 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622703340 2112 GRYGGEVAVVTGASKGsIAASVVARLLDGGATVIATTSKlDEERLAfyRTLYRDHARYGAALwLVAANMASYSDVDALVE 2191
Cdd:PRK05565 1 MKLMGKVAIVTGASGG-IGRAIAELLAKEGAKVVIAYDI-NEEAAQ--ELLEEIKEEGGDAI-AVKADVSSEEDVENLVE 75
|
|
| BKR_like_SDR_like |
cd05344 |
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ... |
2116-2191 |
6.45e-03 |
|
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187602 [Multi-domain] Cd Length: 253 Bit Score: 41.10 E-value: 6.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622703340 2116 GEVAVVTGASKGsIAASVVARLLDGGATViATTSKlDEERLAfyrTLYRDHARYGAALWLVAANMASYSDVDALVE 2191
Cdd:cd05344 1 GKVALVTAASSG-IGLAIARALAREGARV-AICAR-NRENLE---RAASELRAGGAGVLAVVADLTDPEDIDRLVE 70
|
|
| PRK06523 |
PRK06523 |
short chain dehydrogenase; Provisional |
2116-2147 |
8.08e-03 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 180604 [Multi-domain] Cd Length: 260 Bit Score: 41.04 E-value: 8.08e-03
10 20 30
....*....|....*....|....*....|..
gi 622703340 2116 GEVAVVTGASKGsIAASVVARLLDGGATVIAT 2147
Cdd:PRK06523 9 GKRALVTGGTKG-IGAATVARLLEAGARVVTT 39
|
|
| |
