|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-895 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1824.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 1 MSHIDSFKCRKTLTVGGKDYVYYSLTEAEKNGLEGVSKLPFSMKVLLENLLRFEDDRSVKKSDIEAVAKWLNDrGSAGAE 80
Cdd:PRK09277 1 MSSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPK-AKPDRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 81 IAYRPARVLMQDFTGVPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYR 160
Cdd:PRK09277 80 IPFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 161 FLKWGQQAFKNFRVVPPGTGICHQVNLEYLAQAVWTKEeDGETVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAML 240
Cdd:PRK09277 160 FLKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTRE-DGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAML 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 241 GQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFP 320
Cdd:PRK09277 239 GQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 321 VDRETLNYMNTTGRDEHRIELVEAYCRAQGMWRDKGAaDPVFTDILELDMSDVVPSMAGPKRPEGRIALENIASGFATSL 400
Cdd:PRK09277 319 IDEETLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLE-EPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 401 ENEYKKTTGQTARyavEGEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVAAY 480
Cdd:PRK09277 398 ELGVQGFGLDEAE---EGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 481 LESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAHA 560
Cdd:PRK09277 475 LEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 561 LAGTVTKDLTKEPLGEDQNGNPVFLRDIWPSSQEIQEFIAKNVTRKIFSEKYADVFKGDENWQAVQVPAGQTYAWDDNST 640
Cdd:PRK09277 555 LAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDST 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 641 YVQNPPYFVGMGKSAGTIGDVKGARILGLFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEVMMR 720
Cdd:PRK09277 635 YIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMR 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 721 GTFANIRIRNHMLgeNGREGGYTIHYPSKEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQ 800
Cdd:PRK09277 715 GTFANIRIRNEMV--PGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 801 SFERIHRSNLVGMGIVPFVFEEGTSWQTLGLKGDEMVTIEGLADVRPRQKVDASITFADGTVKKVPLICRIDTLDELDYM 880
Cdd:PRK09277 793 SFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFPVLCRIDTAVEVDYY 872
|
890
....*....|....*
gi 500733028 881 KNGGILQTVLRDLAA 895
Cdd:PRK09277 873 RNGGILQYVLRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
5-895 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 1750.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 5 DSFKCRKTLTVGGKDYVYYSLTEAEKNGlEGVSKLPFSMKVLLENLLRFEDDRSVKKSDIEAVAKWLNDRGSaGAEIAYR 84
Cdd:COG1048 3 DSFKARKTLTVGGKPYTYYSLPALEEAG-GDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARG-DDEIPFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 85 PARVLMQDFTGVPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYRFLKW 164
Cdd:COG1048 81 PARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 165 GQQAFKNFRVVPPGTGICHQVNLEYLAQAVWTKEEDGETVAYPDTCVGTDSHTTMVNglgvlgwgvggIEAEAAMLGQPV 244
Cdd:COG1048 161 GQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 245 SMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRE 324
Cdd:COG1048 241 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 325 TLNYMNTTGRDEHRIELVEAYCRAQGMWRDKGAADPVFTDILELDMSDVVPSMAGPKRPEGRIALENIASGFATSLENEY 404
Cdd:COG1048 321 TLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 405 KKTTGQTARYAVEGEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVAAYLESA 484
Cdd:COG1048 401 GEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 485 GLQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAHALAGT 564
Cdd:COG1048 481 GLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 565 VTKDLTKEPLGEDQNGNPVFLRDIWPSSQEIQEFIAKNVTRKIFSEKYADVFKGDENWQAVQVPAGQTYAWDDNSTYVQN 644
Cdd:COG1048 561 VDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 645 PPYFVGMGKSAGTIGDVKGARILGLFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEVMMRGTFA 724
Cdd:COG1048 641 PPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 725 NIRIRNHMLGenGREGGYTIHYPSKEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFER 804
Cdd:COG1048 721 NIRIKNLLAP--GTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFER 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 805 IHRSNLVGMGIVPFVFEEGTSWQTLGLKGDEMVTIEGLAD-VRPRQKVDASITFADGTVKKVPLICRIDTLDELDYMKNG 883
Cdd:COG1048 799 IHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHRIDTPVEVEYYRAG 878
|
890
....*....|..
gi 500733028 884 GILQTVLRDLAA 895
Cdd:COG1048 879 GILQYVLRQLLA 890
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-895 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1471.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 1 MSHiDSFKCRKTLTVGGKDYVYYSLTEAEKNGLEGVSKLPFSMKVLLENLLRFEDDRSVKKSDIEAVAKWLnDRGSAGAE 80
Cdd:PRK12881 1 MAH-NLHKTLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWL-PERKSDDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 81 IAYRPARVLMQDFTGVPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYR 160
Cdd:PRK12881 79 IPFVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 161 FLKWGQQAFKNFRVVPPGTGICHQVNLEYLAQAVWTKEEDGETVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAML 240
Cdd:PRK12881 159 FLKWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVML 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 241 GQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFP 320
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 321 VDRETLNYMNTTGRDEHRIELVEAYCRAQGMWRDKGaADPVFTDILELDMSDVVPSMAGPKRPEGRIALENIASGFATSL 400
Cdd:PRK12881 319 VDEQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPK-AEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 401 EneykkTTGQTARYAVEGED---YDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVV 477
Cdd:PRK12881 398 S-----KPVAENGFAKKAQTsngVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 478 AAYLESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVV 557
Cdd:PRK12881 473 TEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 558 AHALAGTVTKDLTKEPLGEDQNGNPVFLRDIWPSSQEIQEFIAKNVTRKIFSEKYADVFKGDENWQAVQVPAGQTYAWDD 637
Cdd:PRK12881 553 AYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 638 NSTYVQNPPYFVGMGKSAGTIGDVKGARILGLFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEV 717
Cdd:PRK12881 633 KSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEV 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 718 MMRGTFANIRIRNHMLGenGREGGYTIHYPSKEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAV 797
Cdd:PRK12881 713 MMRGTFANVRIKNLMIP--GKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAV 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 798 IAQSFERIHRSNLVGMGIVPFVFEEGTSWQTLGLKGDEMVTIEGL-ADVRPRQKVDASITFADGTVKKVPLICRIDTLDE 876
Cdd:PRK12881 791 IAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRIDTPIE 870
|
890
....*....|....*....
gi 500733028 877 LDYMKNGGILQTVLRDLAA 895
Cdd:PRK12881 871 VDYYKAGGILPYVLRQLLA 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
18-893 |
0e+00 |
|
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes. [Energy metabolism, TCA cycle]
Pssm-ID: 273562 [Multi-domain] Cd Length: 876 Bit Score: 1336.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 18 KDYVYYSLTEAEKNGlEGVSKLPFSMKVLLENLLRFEDDRSVKKSDIEAVAKWLNDRgSAGAEIAYRPARVLMQDFTGVP 97
Cdd:TIGR01341 1 KTYYYYSLKALEESG-GKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGE-VADTEIAFKPARVVMQDFTGVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 98 AVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYRFLKWGQQAFKNFRVVPP 177
Cdd:TIGR01341 79 AVVDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 178 GTGICHQVNLEYLAQAVWTKEEDGETVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVVGFRLT 257
Cdd:TIGR01341 159 GTGIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 258 GKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRETLNYMNTTGRDEH 337
Cdd:TIGR01341 239 GKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 338 RIELVEAYCRAQGMWRDkGAADPVFTDILELDMSDVVPSMAGPKRPEGRIALENIASGFATSLE----NEYKKTTGQTAR 413
Cdd:TIGR01341 319 HVELVEKYARAQGLFYD-DSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEknggDKGFTLRKEPLK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 414 YAVEGEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVAAYLESAGLQKDLDAL 493
Cdd:TIGR01341 398 KKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEEL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 494 GFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAHALAGTVTKDLTKEP 573
Cdd:TIGR01341 478 GFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 574 LGEDQNGNPVFLRDIWPSSQEIQEFIAKNVTRKIFSEKYADVFKGDENWQAVQVPAGQTYAWDDNSTYVQNPPYFVGMGK 653
Cdd:TIGR01341 558 IGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 654 SAGTIGDVKGARILGLFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEVMMRGTFANIRIRNHML 733
Cdd:TIGR01341 638 DPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMV 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 734 geNGREGGYTIHYPSKEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGM 813
Cdd:TIGR01341 718 --KGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGM 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 814 GIVPFVFEEGTSWQTLGLKGDEMVTIEGLADVRPRQKVDASITFADGTVKKVPLICRIDTLDELDYMKNGGILQTVLRDL 893
Cdd:TIGR01341 796 GVIPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
8-895 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1316.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 8 KCRKTLTVGGkDYVYYSLTEAEKNGLEgvsKLPFSMKVLLENLLRFEDDRSVKKSDIEAVAKWlNDRGSAGAEIAYRPAR 87
Cdd:PTZ00092 18 KVLKTLKDGG-SYKYYSLNELHDPRLK---KLPYSIRVLLESAVRNCDEFDVTSKDVENILNW-EENSKKQIEIPFKPAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 88 VLMQDFTGVPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYRFLKWGQQ 167
Cdd:PTZ00092 93 VLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 168 AFKNFRVVPPGTGICHQVNLEYLAQAVWtkEEDGetVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSML 247
Cdd:PTZ00092 173 AFKNLLIVPPGSGIVHQVNLEYLARVVF--NKDG--LLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 248 LPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRETLN 327
Cdd:PTZ00092 249 LPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 328 YMNTTGRDEHRIELVEAYCRAQGMWRDkGAADPVFTDILELDMSDVVPSMAGPKRPEGRIALENIASGFATSLENEY--- 404
Cdd:PTZ00092 329 YLKQTGRSEEKVELIEKYLKANGLFRT-YAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVgfk 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 405 -----KKTTGQTARYAVEGEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVAA 479
Cdd:PTZ00092 408 gfgipEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 480 YLESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAH 559
Cdd:PTZ00092 488 YLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAY 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 560 ALAGTVTKDLTKEPLGEDQNGNPVFLRDIWPSSQEIQEFIAKNVTRKIFSEKYADVFKGDENWQAVQVPAGQTYAWDDNS 639
Cdd:PTZ00092 568 ALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 640 TYVQNPPYFVGMGKSAGTIGDVKGARILGLFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEVMM 719
Cdd:PTZ00092 648 TYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMV 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 720 RGTFANIRIRNHMLGEngrEGGYTIHYPSKEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIA 799
Cdd:PTZ00092 728 RGTFANIRLINKLCGK---VGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIA 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 800 QSFERIHRSNLVGMGIVPFVFEEGTSWQTLGLKGDEMVTIEG-LADVRPRQKvdasITFADGTVKKVPLICRIDTLDELD 878
Cdd:PTZ00092 805 ESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLnSGELKPGQD----VTVKTDTGKTFDTILRIDTEVEVE 880
|
890
....*....|....*..
gi 500733028 879 YMKNGGILQTVLRDLAA 895
Cdd:PTZ00092 881 YFKHGGILQYVLRKLVK 897
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
16-895 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1115.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 16 GGKDYVYYSLTEAEKNGLEgvsKLPFSMKVLLENLLRFEDDRSVKKSDIEAVAKWLNDrGSAGAEIAYRPARVLMQDFTG 95
Cdd:PLN00070 57 GGEFGKYYSLPALNDPRID---KLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENT-SPKQVEIPFKPARVLLQDFTG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 96 VPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYRFLKWGQQAFKNFRVV 175
Cdd:PLN00070 133 VPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 176 PPGTGICHQVNLEYLAQAVWTKeeDGetVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVVGFR 255
Cdd:PLN00070 213 PPGSGIVHQVNLEYLGRVVFNT--DG--ILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 256 LTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRETLNYMNTTGRD 335
Cdd:PLN00070 289 LSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 336 EHRIELVEAYCRAQGMWRD--KGAADPVFTDILELDMSDVVPSMAGPKRPEGRIALENIASGFATSLENEY--------K 405
Cdd:PLN00070 369 DETVAMIEAYLRANKMFVDynEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVgfkgfavpK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 406 KTTGQTARYAVEGEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVAAYLESAG 485
Cdd:PLN00070 449 EAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSG 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 486 LQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAHALAGTV 565
Cdd:PLN00070 529 LQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTV 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 566 TKDLTKEPLGEDQNGNPVFLRDIWPSSQEIQEFIAKNVTRKIFSEKYADVFKGDENWQAVQVPAGQTYAWDDNSTYVQNP 645
Cdd:PLN00070 609 DIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEP 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 646 PYFVGMGKSAGTIGDVKGARILGLFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEVMMRGTFAN 725
Cdd:PLN00070 689 PYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFAN 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 726 IRIRNHMLgeNGREGGYTIHYPSKEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERI 805
Cdd:PLN00070 769 IRIVNKLL--KGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERI 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 806 HRSNLVGMGIVPFVFEEGTSWQTLGLKGDEMVTIE---GLADVRPRQkvDASITFADGtvKKVPLICRIDTLDELDYMKN 882
Cdd:PLN00070 847 HRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDlpsNISEIKPGQ--DVTVTTDNG--KSFTCTLRFDTEVELAYFDH 922
|
890
....*....|...
gi 500733028 883 GGILQTVLRDLAA 895
Cdd:PLN00070 923 GGILPYVIRNLIK 935
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
87-565 |
0e+00 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 749.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 87 RVLMQDFTGVPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSVIVDEFGNPSAFKANVDLEYQRNGERYRFLKWGQ 166
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 167 QAFKNFRVVPPGTGICHQVNLEYLAQAVWTKEEDGETVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSM 246
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 247 LLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDretl 326
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 327 nymnttgrdehrielveaycraqgmwrdkgaadpvfTDILELDMSDVVPSMAGPKRPEGRIALeniasgfatsleneykk 406
Cdd:cd01586 237 ------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 407 ttgqtaryavegedydlgHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVAAYLESAGL 486
Cdd:cd01586 264 ------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEASGL 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500733028 487 QKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINEKGLIAAAVLSGNRNFEGRVSPDVQANYLASPPLVVAHALAGTV 565
Cdd:cd01586 326 LPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
80-563 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 647.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 80 EIAYRPARVLMQDFTGVPAVVDLAAMRDGLKALGGDPEKINPLVPVDLVIDHSvivdefgnPSAFKANVDLEYQRNGERY 159
Cdd:pfam00330 15 SLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISRNKEQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 160 RFLKWGQQAFkNFRVVPPGTGICHQVNLEYLaqavwtkeedgetVAYPD-TCVGTDSHTTMVNGLGVLGWGVGGIEAEAA 238
Cdd:pfam00330 87 DFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGGLGALAFGVGGSEAEHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 239 MLGQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGF 318
Cdd:pfam00330 153 LATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 319 FPVDRETLNYMNTTGRDEHRIelVEAYCRAQGMWRDKGAADPVFTDILELDMSDVVPSMAGPKRPEGRIAL-ENIASGFA 397
Cdd:pfam00330 233 FPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLsELVPDPFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 398 TSLENEYKKttgQTARYAVEGEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLArNAVAKGLKTKPWVKTSLAPGSQVV 477
Cdd:pfam00330 311 DAVKRKAAE---RALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLK-KAVEKGLKVAPGVKASVVPGSEVV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 478 AAYLESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPApisktiNEkgliaAAVLSGNRNFEGRVSPDVQAnYLASPPLVV 557
Cdd:pfam00330 387 RAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP------GE-----RCVSSSNRNFEGRQGPGGRT-HLASPALVA 454
|
....*.
gi 500733028 558 AHALAG 563
Cdd:pfam00330 455 AAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
669-841 |
6.34e-103 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 316.53 E-value: 6.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 669 LFGDKITTDHISPAGSIKAQSPAGKYLIDHGVGIADFNQYGTRRGNHEVMMRGTFANIRIRNHMLGenGREGGYTIHYPS 748
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVP--GTEGGTTHHPPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 749 KEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQT 828
Cdd:cd01580 79 GEVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADS 158
|
170
....*....|...
gi 500733028 829 LGLKGDEMVTIEG 841
Cdd:cd01580 159 LGLTGEETYDIIG 171
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
77-895 |
1.94e-86 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 289.35 E-value: 1.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 77 AGAEIAYRPARVLMQDFTGVPAVVDLAAMrdGLkalggdpekinPLVPVDLV---IDHSVIVDEFGNPsafkanvdleyq 153
Cdd:PRK07229 21 PGEEIAIRIDQTLTQDATGTMAYLQFEAM--GL-----------DRVKTELSvqyVDHNLLQADFENA------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 154 rngERYRFLkwgQQAFKNFRVV--PPGTGICHQVNLE-YlaqavwtkeedgetvAYP-DTCVGTDSHTT------MVngl 223
Cdd:PRK07229 76 ---DDHRFL---QSVAAKYGIYfsKPGNGICHQVHLErF---------------AFPgKTLLGSDSHTPtagglgML--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 224 gvlgwgvgGI-----EAEAAMLGQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMT 298
Cdd:PRK07229 132 --------AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 299 LADRATIANMGPEYGATCGFFPVDRETLNYMNTTGRDEHRIELveaycraqgmwrdkgAADP--VFTDILELDMSDVVPS 376
Cdd:PRK07229 204 VPERATITNMGAELGATTSIFPSDERTREFLKAQGREDDWVEL---------------LADPdaEYDEVIEIDLSELEPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 377 MAGPKRPegrialeniasGFATSLENeykkttgqtaryaVEGEdydlghgDVAIAAITSCTNTSNPSVLIAAgllarnAV 456
Cdd:PRK07229 269 IAGPHSP-----------DNVVPVSE-------------VAGI-------KVDQVLIGSCTNSSYEDLMRAA------SI 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 457 AKGLKTKPWVKTSLAPGSQVVAAYLESAGLQKDLDALGFNLVGFGCTTCIGNSGplpAPISKTInekgliaaAVLSGNRN 536
Cdd:PRK07229 312 LKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNV--------SLRTFNRN 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 537 FEGRV-SPDVQAnYLASPPLVVAHALAGTVT--KDLTKEpLGEdqngnpvflrdiWPSSQEIQEFIAKNvtrkifsekyA 613
Cdd:PRK07229 381 FPGRSgTKDAQV-YLASPETAAASALTGVITdpRTLALE-NGE------------YPKLEEPEGFAVDD----------A 436
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 614 DVFKGDENWQAVQVPAGQtyawddNSTYVQ-NPPyfvgmgksagtIGDVKGARILGLFGDKITTDHISPAGSikaqspag 692
Cdd:PRK07229 437 GIIAPAEDGSDVEVVRGP------NIKPLPlLEP-----------LPDLLEGKVLLKVGDNITTDHIMPAGA-------- 491
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 693 KYLidhgvgiadfnqygtrrgnhevMMRGtfaNI-RIRNHMLgengreggytihypskeetSIYDAAMQYKA-EGVPLVV 770
Cdd:PRK07229 492 KWL----------------------PYRS---NIpNISEFVF-------------------EGVDNTFPERAkEQGGGIV 527
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 771 FAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQTLGLkGDEmVTIEGLADVRPRQK 850
Cdd:PRK07229 528 VGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEE-GDV-LEIEDLREFLPGGP 605
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 500733028 851 VDASITFADGTVKkvpliCRID-TLDELDYMKNGGILQTVLRDLAA 895
Cdd:PRK07229 606 LTVVNVTKDEEIE-----VRHTlSERQIEILLAGGALNLIKKKLAA 646
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
87-565 |
1.37e-81 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 268.21 E-value: 1.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 87 RVLMQDFTGVPAVVDLAAMrdglkalgGDPEKINPLVPVDLVIDHSVivdefgnpsafkanvDLEYQRNGERYRFLKWGQ 166
Cdd:cd01351 1 RVMLQDATGPMAMKAFEIL--------AALGKVADPSQIACVHDHAV---------------QLEKPVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 167 QAFKnFRVVPPGTGICHQVNLEYLAQavwtkeedgetvaYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSM 246
Cdd:cd01351 58 ALQG-IAFYRPGVGIIHQIMVENLAL-------------PGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 247 LLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRETL 326
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 327 NYMNTTGrdehrielveaycRAQGMWRDKGAADPVFTD-------ILELDMSDVVPSMAGPKRPEGRIALEniasgfats 399
Cdd:cd01351 204 KWLEATG-------------RPLLKNLWLAFPEELLADegaeydqVIEIDLSELEPDISGPNRPDDAVSVS--------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 400 leneykkttgqtaryavegedyDLGHGDVAIAAITSCTNtSNPSVLIAAGllarnAVAKGLKTKPWVKTSLAPGSQVVAA 479
Cdd:cd01351 262 ----------------------EVEGTKIDQVLIGSCTN-NRYSDMLAAA-----KLLKGAKVAPGVRLIVTPGSRMVYA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 480 YLESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKtinekgliaaAVLSGNRNFEGRVSPDVQANYLASPPLVVAH 559
Cdd:cd01351 314 TLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEV----------GVSSGNRNFPGRLGTYERHVYLASPELAAAT 383
|
....*.
gi 500733028 560 ALAGTV 565
Cdd:cd01351 384 AIAGKI 389
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
89-565 |
2.42e-50 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 182.26 E-value: 2.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 89 LMQDFTGVPAVVDLAAMrdglkalgGDPEkinplVPVDLV---IDHSVIVDEFgnpsafkanvdleyqRNGERYRFLkwg 165
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--------GVDR-----VRTELSvsyVDHNTLQTDF---------------ENADDHRFL--- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 166 QQAFKNFRVV--PPGTGICHQVNLEYLAQAvwtkeedGETVaypdtcVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQP 243
Cdd:cd01585 53 QTVAARYGIYfsRPGNGICHQVHLERFAVP-------GKTL------LGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 244 VSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDR 323
Cdd:cd01585 120 YYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 324 ETLNYMNTTGRDEHRIELveaycraqgmwrdkgAADP--VFTDILELDMSDVVPSMAGPKRPEGRIALENIAsgfatsle 401
Cdd:cd01585 200 RTREFLAAQGREDDWVEL---------------AADAdaEYDEEIEIDLSELEPLIARPHSPDNVVPVREVA-------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 402 neykkttGQtaryavegedydlghgDVAIAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKPWVKTSLAPGSQVVAAYL 481
Cdd:cd01585 257 -------GI----------------KVDQVAIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAPGSKQVLEML 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 482 ESAGLQKDLDALGFNLVGFGCTTCIGNSGplpAPISKTInekgliaaAVLSGNRNFEGRVSPDVQANYLASPPLVVAHAL 561
Cdd:cd01585 308 ARNGALADLLAAGARILESACGPCIGMGQ---APPTGGV--------SVRTFNRNFEGRSGTKDDLVYLASPEVAAAAAL 376
|
....
gi 500733028 562 AGTV 565
Cdd:cd01585 377 TGVI 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
87-566 |
2.59e-48 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 177.14 E-value: 2.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 87 RVLMQDFTGVPAVvdlaamrDGLKALGG----DPEKInplvpVdLVIDHSVivdeFGNPSAFKANVDlEYQRNGERY--R 160
Cdd:COG0065 30 LHLVHDVTSPQAF-------EGLREAGGrkvwDPDRI-----V-AVFDHNV----PTKDPKSAEQVK-TLREFAKEFgiT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 161 FLKWGQQafknfrvvppgtGICHQVnleyLAQAVWTKeedgetvayP-DTCVGTDSHTTM----------VNGLgvlgwg 229
Cdd:COG0065 92 FFDVGDP------------GICHVV----LPEQGLVL---------PgMTIVGGDSHTCThgafgafafgIGTT------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 230 vggiEAEAAMLGQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMG 309
Cdd:COG0065 141 ----DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 310 PEYGATCGFFPVDRETLNYMNttGRDEHRIELVEAycraqgmwrDKGAadpVFTDILELDMSDVVPSMAGPKRPEGRIAL 389
Cdd:COG0065 217 IEAGAKAGIIAPDETTFEYLK--GRPFAPWRTLKS---------DEDA---VYDKEVEIDASDLEPQVAWPHSPDNVVPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 390 ENIAsgfatsleneykkttgqtaryavegedydlghgDVAI--AAITSCTNtsnpSVL----IAAgllarnAVAKGLKTK 463
Cdd:COG0065 283 SELE---------------------------------GIKIdqVFIGSCTN----GRIedlrAAA------EILKGRKVA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 464 PWVKTSLAPGSQVVAAYLESAGLQKDLDALGFNLVGFGCTTCIG-NSGPLPApisktiNEKgliaaAVLSGNRNFEGRV- 541
Cdd:COG0065 320 PGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAP------GER-----CASTSNRNFEGRMg 388
|
490 500
....*....|....*....|....*
gi 500733028 542 SPDVQAnYLASPPLVVAHALAGTVT 566
Cdd:COG0065 389 SPGSRT-YLASPATAAASAIAGRIT 412
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
87-564 |
2.28e-46 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 171.47 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 87 RVLMQDFTGVPAVvdLAAMRDGLKalggdpekiNPLVPVDLVIDHsVIVDEFGNPSAFKANVDLeyqrNGERYRFL---- 162
Cdd:cd01584 1 RVAMQDATAQMAL--LQFMSSGLP---------KVAVPSTIHCDH-LIEAQVGGEKDLKRAKDI----NKEVYDFLasag 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 163 -KWGQQAFKnfrvvpPGTGICHQVNLEylaqavwtkeedgeTVAYPDTC-VGTDSHTTMVNGLGVLGWGVGGIEAEAAML 240
Cdd:cd01584 65 aKYGIGFWK------PGSGIIHQIVLE--------------NYAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 241 GQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFP 320
Cdd:cd01584 125 GIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 321 VDRETLNYMNTTGRDEhrielVEAYcrAQGMWRDKGAADP--VFTDILELDMSDVVPSMAGPKRPEgrialeniasgFAT 398
Cdd:cd01584 205 YNERMKKYLKATGRAE-----IADL--ADEFKDDLLVADEgaEYDQLIEINLSELEPHINGPFTPD-----------LAT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 399 SLeNEYKKTtgqtaryaVEGEDYDLghgDVAIAAITSCTNTSNPSVLIAAGlLARNAVAKGLKTKpwVKTSLAPGSQVVA 478
Cdd:cd01584 267 PV-SKFKEV--------AEKNGWPL---DLRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTITPGSEQIR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 479 AYLESAGLQKDLDALGFNLVGFGCTTCIGNsgplpapISKTINEKGLIAAAVLSGNRNFEGRVSPDVQA-NYLASPPLVV 557
Cdd:cd01584 332 ATIERDGLLQTFRDAGGIVLANACGPCIGQ-------WDRKDIKKGEKNTIVTSYNRNFTGRNDANPAThAFVASPEIVT 404
|
....*..
gi 500733028 558 AHALAGT 564
Cdd:cd01584 405 AMAIAGT 411
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
691-823 |
4.67e-46 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 160.99 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 691 AGKYLIDHGVGIADFNQYGTRRGNHEVMMRGTFANIRIRNHMLgeNGREGGYTIHYPSKEETSIYDAAMQYKAEGVPLVV 770
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINF--EGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 500733028 771 FAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEG 823
Cdd:pfam00694 79 IGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
87-565 |
1.13e-45 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 168.91 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 87 RVLMQDFTGVPAVvdlaamrDGLKALGG----DPEKINplvpvdLVIDHSVIvdefgNPSAFKANVDLEYQRNGERyrfl 162
Cdd:cd01583 1 LHLVHDVTSPQAF-------EGLREAGRekvwDPEKIV------AVFDHNVP-----TPDIKAAEQVKTLRKFAKE---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 163 kwgqQAFKNFRVVppGTGICHQVnleyLAQAVWTKEedGETVaypdtcVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQ 242
Cdd:cd01583 59 ----FGINFFDVG--RQGICHVI----LPEKGLTLP--GMTI------VGGDSHTCTHGAFGAFATGIGTTDVAHVLATG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 243 PVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVD 322
Cdd:cd01583 121 KLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 323 RETLNYMNTTGRDEHRIelveaycraqgmWR-DKGAadpVFTDILELDMSDVVPSMAGPKRPEGRIALENiasgfatsle 401
Cdd:cd01583 201 ETTFEYLKGRGKAYWKE------------LKsDEDA---EYDKVVEIDASELEPQVAWPHSPDNVVPVSE---------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 402 neykkttgqtaryaVEGEDYDlghgdvaIAAITSCTNTSNPSVLIAAgllarnAVAKGLKTKPWVKTSLAPGSQVVAAYL 481
Cdd:cd01583 256 --------------VEGIKID-------QVFIGSCTNGRLEDLRAAA------EILKGRKVADGVRLIVVPASQRVYKQA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 482 ESAGLQKDLDALGFNLVGFGCTTCIG-NSGPLPapisktineKGLIAAAvlSGNRNFEGRVSPDVQANYLASPPLVVAHA 560
Cdd:cd01583 309 EKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLA---------PGERCVS--TSNRNFKGRMGSPGARIYLASPATAAASA 377
|
....*
gi 500733028 561 LAGTV 565
Cdd:cd01583 378 ITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
96-566 |
2.64e-38 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 148.40 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 96 VPAVVDLAAMRDG--------LKALGG----DPEKINplvpvdLVIDHSVivdefgnPSAfkaNVDLEyqrngERYRFL- 162
Cdd:PRK00402 24 VEAKVDLVMAHDItgplaikeFEKIGGdkvfDPSKIV------IVFDHFV-------PAK---DIKSA-----EQQKILr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 163 KWG-QQAFKNFRVVppGTGICHQVNLEylaqavwtkeedgETVAYP-DTCVGTDSHTT----------------Mvnglg 224
Cdd:PRK00402 83 EFAkEQGIPNFFDV--GEGICHQVLPE-------------KGLVRPgDVVVGADSHTCtygalgafatgmgstdM----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 225 vlgwgvggieAEAAMLGQpVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRAT 304
Cdd:PRK00402 143 ----------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 305 IANMGPEYGATCGFFPVDRETLNYMNTTGRDEHRIelveaycraqgMWRDKGAadpVFTDILELDMSDVVPSMAGPKRPe 384
Cdd:PRK00402 212 LANMAIEAGAKAGIFAPDEKTLEYLKERAGRDYKP-----------WKSDEDA---EYEEVYEIDLSKLEPQVAAPHLP- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 385 grialENIasgfatsleneykKTTGQtaryaVEGEDYDlghgdvaIAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKP 464
Cdd:PRK00402 277 -----DNV-------------KPVSE-----VEGTKVD-------QVFIGSCTNGRLEDLRIAAEIL------KGRKVAP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 465 WVKTSLAPGSQVVAAYLESAGLQKDLDALGFNLVGFGCTTCIGNSGplpapisktinekGLIAA---AVLSGNRNFEGRV 541
Cdd:PRK00402 321 GVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHM-------------GVLAPgevCLSTTNRNFKGRM 387
|
490 500
....*....|....*....|....*.
gi 500733028 542 -SPDVQAnYLASPPLVVAHALAGTVT 566
Cdd:PRK00402 388 gSPESEV-YLASPAVAAASAVTGKIT 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
77-566 |
1.96e-35 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273960 Cd Length: 413 Bit Score: 139.90 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 77 AGAEIAYRPARVLMQDFTGVPAvvdLAAMRDGLKALGGDPEKINplvpvdLVIDHSVivdefgNPSAFKANvdlEYQRng 156
Cdd:TIGR02086 18 AGEIVEVEVDLAMTHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNV------PPPTVEAA---EMQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 157 ERYRFLKwgQQAFKNFRVvppGTGICHQVNLEylaqavwtkeedgETVAYP-DTCVGTDSHTTMVNGLGVLGWGVGGIE- 234
Cdd:TIGR02086 78 EIREFAK--RHGIKNFDV---GEGICHQILAE-------------EGYALPgMVVVGGDSHTCTSGAFGAFATGMGATDm 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 235 AEAAMLGQPVSMlLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGA 314
Cdd:TIGR02086 140 AIALATGKTWIK-VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 315 TCGFFPVDRETLNYMNTTGRDEHRIelveaycraqgMWRDKGAadpVFTDILELDMSDVVPSMAGPKRPegrialENIas 394
Cdd:TIGR02086 219 KAGIIEPDEETYEYLKKRRGLEFRI-----------LVPDPGA---NYYKEIEIDLSDLEPQVAVPHSV------DNV-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 395 gfatsleneykKTTGQtaryaVEGEDYDLghgdvaiAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKPWVKTSLAPGS 474
Cdd:TIGR02086 277 -----------KPVSD-----VEGTEIDQ-------VFIGSCTNGRLEDLRIAAEIL------KGRRVHPDVRLIVIPAS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 475 QVVAAYLESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPAPisktiNEkgliaAAVLSGNRNFEGRV-SPDVQAnYLASP 553
Cdd:TIGR02086 328 RKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGD-----GE-----VCLSTTNRNFKGRMgSPNAEI-YLASP 396
|
490
....*....|...
gi 500733028 554 PLVVAHALAGTVT 566
Cdd:TIGR02086 397 ATAAASAVEGYIT 409
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
96-566 |
2.14e-31 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 127.95 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 96 VPAVVDLAAMRDG--------LKALGGD----PEKINplvpvdLVIDHSVivdefgNPSAFKANvdleyQRNGERYRFLK 163
Cdd:TIGR01343 21 IEAEIDLAMVHDItaplaiktLEEYGIDkvwnPEKIV------IVFDHQV------PADTIKAA-----EMQKLAREFVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 164 wgQQAFKNFRvvPPGTGICHQVNLEylaqavwtkeedgETVAYP-DTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQ 242
Cdd:TIGR01343 84 --KQGIKYFY--DVGEGICHQVLPE-------------KGLVKPgDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 243 PVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVD 322
Cdd:TIGR01343 147 KTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 323 RETLNYMNTTGRDEHRIElveaycraqgmwrdKGAADPVFTDILELDMSDVVPSMAGPKRPegrialENIAsgfatslen 402
Cdd:TIGR01343 227 EKTIQYLKERRKEPFRVY--------------KSDEDAEYAKEIEIDASQIEPVVACPHNV------DNVK--------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 403 eykkttgqtaryavegEDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKPWVKTSLAPGSQVVaaYLE 482
Cdd:TIGR01343 278 ----------------PVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKIL------KGRKVAPDVRLIVIPASRAV--YLQ 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 483 SA--GLQKDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINekgliaaavlSGNRNFEGRV-SPDVQAnYLASPPLVVAH 559
Cdd:TIGR01343 334 ALkeGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCIS----------TSNRNFKGRMgHPNAEI-YLASPATAAAS 402
|
....*..
gi 500733028 560 ALAGTVT 566
Cdd:TIGR01343 403 AVKGYIA 409
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
214-566 |
5.95e-24 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 106.14 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 214 DSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEG 293
Cdd:PRK12466 130 DSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 294 LENMTLADRATIANMGPEYGATCGFFPVDRETLNYMNTTGRDEHrielVEAYCRAQGMWRD-KGAADPVFTDILELDMSD 372
Cdd:PRK12466 210 IRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPK----GALWDAALAYWRTlRSDADAVFDREVEIDAAD 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 373 VVPSMAGPKRPEGRIALeniaSGFATSLENEYKKTTGQTARYAVegeDY-DLGHG----DVAI--AAITSCTNtSNPSVL 445
Cdd:PRK12466 286 IAPQVTWGTSPDQAVPI----TGRVPDPAAEADPARRAAMERAL---DYmGLTPGtplaGIPIdrVFIGSCTN-GRIEDL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 446 IAAGllarnAVAKGLKTKPWVKTSLAPGSQVVAAYLESAGLQKDLDALGFNLVGFGCTTCIGNSGPLPAPisktinekGL 525
Cdd:PRK12466 358 RAAA-----AVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAP--------GE 424
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 500733028 526 IAAAvlSGNRNFEGRVSPDVQAnYLASPPLVVAHALAGTVT 566
Cdd:PRK12466 425 RCAS--TTNRNFEGRQGPGART-HLMSPAMVAAAAVAGHIT 462
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
255-566 |
1.02e-23 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 105.59 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 255 RLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRETLNYMNttGR 334
Cdd:PRK05478 169 EVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK--GR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 335 dehriELV---EAYCRAQGMWR----DKGAadpVFTDILELDMSDVVPSMAGPKRPEGRIALeniaSGFATSLENEYKKT 407
Cdd:PRK05478 247 -----PFApkgEDWDKAVAYWKtlksDEDA---VFDKVVTLDAADIEPQVTWGTNPGQVISI----DGKVPDPEDFADPV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 408 TGQTARYAVEgedY-DLGHG----DVAI--AAITSCTNtSNPSVLIAAGllarnAVAKGLKTKPWVKTSLAPGSQVVAAY 480
Cdd:PRK05478 315 KRASAERALA---YmGLKPGtpitDIKIdkVFIGSCTN-SRIEDLRAAA-----AVVKGRKVAPGVRALVVPGSGLVKAQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 481 LESAGLQKDLDALGFNLVGFGCTTCIG-NSGPLPApisktinekGLIAAAvlSGNRNFEGRvspdvQAN----YLASPPL 555
Cdd:PRK05478 386 AEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLPP---------GERCAS--TSNRNFEGR-----QGKggrtHLVSPAM 449
|
330
....*....|.
gi 500733028 556 VVAHALAGTVT 566
Cdd:PRK05478 450 AAAAAITGHFV 460
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
176-565 |
4.73e-23 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 101.92 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 176 PPGTGICHQVNLEylaqavwtkeedgETVAYPDT-CVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVVGF 254
Cdd:cd01582 64 PAGRGIGHQIMIE-------------EGYAFPGTlAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 255 RLTGKIKEGVTATDLVLTVTQMLRKKGVVGKFVEFFGEGLENMTLADRATIANMGPEYGATCGFFPVDRETLNymnttgr 334
Cdd:cd01582 131 ELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLI------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 335 dehrielveaycraqgmwrdkgaadpvftdileLDMSDVVPSMAGPKrpegrialeniASGFATSLEneykkttgqtary 414
Cdd:cd01582 204 ---------------------------------LDLSTLSPYVSGPN-----------SVKVSTPLK------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 415 avegedyDLGHGDVAI--AAITSCTNtSNPSVLIAAGLLARNAVAKGLKTK--PWVKTSLAPGSQVVAAYLESAGLQKDL 490
Cdd:cd01582 227 -------ELEAQNIKInkAYLVSCTN-SRASDIAAAADVVKGKKEKNGKIPvaPGVEFYVAAASSEVQAAAEKNGDWQTL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500733028 491 DALGFNLVGFGCTTCIGNSGPLPAPisktiNEKGLIAAavlsgNRNFEGRV-SPDVQAnYLASPPLVVAHALAGTV 565
Cdd:cd01582 299 LEAGATPLPAGCGPCIGLGQGLLEP-----GEVGISAT-----NRNFKGRMgSTEALA-YLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
673-847 |
7.98e-17 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 78.28 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 673 KITTDHISPAGsikaqsPAGKYlidhgvgiadfnqygtrrgnhevmmRGTFANIRiRNHMLG----ENGrEGGYTIHYPS 748
Cdd:cd01578 5 KCTTDHISAAG------PWLKY-------------------------RGHLDNIS-NNLLIGainaENG-KANSVKNQVT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 749 KEETSIYDAAMQYKAEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQT 828
Cdd:cd01578 52 GEYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDK 131
|
170
....*....|....*....
gi 500733028 829 lgLKGDEMVTIEGLADVRP 847
Cdd:cd01578 132 --IHPDDKVDILGLTDFAP 148
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
671-836 |
1.08e-16 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 77.09 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 671 GDKITTDHISPAGSikaqspagKYLidhgvgiadfnqygTRRGNHEVMMRGTFanirirnHMLGENgreggytihYPSKE 750
Cdd:cd01579 3 GDNITTDHIMPAGA--------KVL--------------PLRSNIPAISEFVF-------HRVDPT---------FAERA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 751 EtsiydaamqykaEGVPLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQTLG 830
Cdd:cd01579 45 K------------AAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFE 112
|
....*.
gi 500733028 831 LkGDEM 836
Cdd:cd01579 113 Q-GDQL 117
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
767-836 |
1.45e-16 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 75.58 E-value: 1.45e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 767 PLVVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQTLGLkGDEM 836
Cdd:cd00404 16 PGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHT-GDEL 84
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
769-822 |
6.82e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 58.66 E-value: 6.82e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 500733028 769 VVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEE 822
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEE 105
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
769-839 |
1.44e-08 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 52.98 E-value: 1.44e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500733028 769 VVFAGVEYGNGSSR---DWAAKGtnlLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQTLGLKGDEmVTI 839
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE-VEV 89
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
207-563 |
6.75e-08 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 55.97 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 207 PDTC-VGTDSHTTMvnGLGVLGWGVGGIEAEAAMLGQ-PVSMllPEVVGFRLTGKIKEGVTATDLV------------LT 272
Cdd:cd01581 106 PDTVgTGGDSHTRF--PIGISFPAGSGLVAFAAATGVmPLDM--PESVLVRFKGKMQPGITLRDLVnaipyyaiqqglLT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 273 VTQMLRKKGVVGKFVEFfgEGLENMTLADRATIANMGPEYGATCGFFPVDRETL-NYMNTT----------GRD-----E 336
Cdd:cd01581 182 VEKKGKKNVFNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLESNvvlmkimianGYDdartlL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 337 HRIELVEAycraqgmWRD-----KGAADPVFTDILELDMSDVV-PSMAGPKRPegrialENIASgfatsleneykkttgq 410
Cdd:cd01581 260 RRIIAMEE-------WLAnppllEPDADAEYAAVIEIDLDDIKePILACPNDP------DDVKL---------------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 411 taRYAVEGEDYDLGHgdvaiaaITSCtnTSNPSVLIAAGLLARNavAKGLKTKPWVktslAPGSQVVAAYLESAGLQKDL 490
Cdd:cd01581 311 --LSEVAGKKIDEVF-------IGSC--MTNIGHFRAAAKILRG--KEFKPTRLWV----APPTRMDWAILQEEGYYSIF 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500733028 491 DALGFNLVGFGCTTCIGNSGPLPapisktineKGliaAAVLS-GNRNFEGRVSPDVQAnYLASPPLVVAHALAG 563
Cdd:cd01581 374 GDAGARTEMPGCSLCMGNQARVA---------DG---ATVFStSTRNFDNRVGKGAEV-YLGSAELAAVCALLG 434
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
175-383 |
8.04e-07 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 53.09 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 175 VPPGTGICHQVNLEYLAQAvwtkeedGETVaypdtcVGTDSHT------TMvnglgvlgwgvgGI-----EAEAAMLGQP 243
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG-------GKMI------LGSDSHTrygalgTM------------AVgegggELVKQLLNDT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 244 VSMLLPEVVGFRLTGKIKEGVTATDLVLTVTQMLRKKGVV-GKFVEFFGEGLENMTLADRATIANMGPEygATC--GFFP 320
Cdd:PRK11413 178 YDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQ 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500733028 321 VDRETLNYMNTTGRdehrielVEAYCRAQgmwrdkgAADPVFTD-ILELDMSDVVPSMAGPKRP 383
Cdd:PRK11413 256 TDEEVHNWLALHGR-------GQDYCELN-------PQPMAYYDgCISVDLSAIKPMIALPFHP 305
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
769-815 |
4.85e-05 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 44.43 E-value: 4.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 500733028 769 VVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGI 815
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGL 97
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
207-563 |
3.81e-04 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 44.14 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 207 PDTcVGT--DSHTTMvnGLGVLGWGVGGIEAEAAMLG-QPVSMllPEVVGFRLTGKIKEGVTATDLV------------L 271
Cdd:PLN00094 552 PDT-VGTggDSHTRF--PIGISFPAGSGLVAFGAATGvIPLDM--PESVLVRFTGTMQPGITLRDLVhaipytaiqdglL 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 272 TVTQMLRKKGVVGKFVEFfgEGLENMTLADRATIANMGPEYGATCGFFPVDRET-----------LNYMNTTGRD----- 335
Cdd:PLN00094 627 TVEKKGKKNVFSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPiieylnsnvvmLKWMIAEGYGdrrtl 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 336 EHRIELVEAYCRAQGMWRdkgaADP--VFTDILELDMSDVV-PSMAGPKRPEgrialeniasgfATSLENEykkttgqta 412
Cdd:PLN00094 705 ERRIARMQQWLADPELLE----ADPdaEYAAVIEIDMDEIKePILCAPNDPD------------DARLLSE--------- 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500733028 413 ryaVEGEDYDlghgDVAIAaitSCtnTSNPSVLIAAGLLArNAVAKGLKTKPWVktslAPGSQVVAAYLESAGLQKDLDA 492
Cdd:PLN00094 760 ---VTGDKID----EVFIG---SC--MTNIGHFRAAGKLL-NDNLSQLPTRLWV----APPTKMDEAQLKAEGYYSTFGT 822
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500733028 493 LGFNLVGFGCTTCIGNSGplpapiskTINEKgliAAAVLSGNRNFEGRVSPDvqAN-YLASPPLVVAHALAG 563
Cdd:PLN00094 823 VGARTEMPGCSLCMGNQA--------RVAEK---STVVSTSTRNFPNRLGKG--ANvYLASAELAAVAAILG 881
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
779-840 |
3.21e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 38.55 E-value: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500733028 779 GSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQTLGLKGDEMVTIE 840
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTVD 64
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
769-840 |
4.14e-03 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 39.84 E-value: 4.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500733028 769 VVFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGIVPFVFEEGTSWQTlgLKGDEMVTIE 840
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGEVYPLESEVRICEE--CKTGDVVTVE 201
|
|
|