|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00070 |
PLN00070 |
aconitate hydratase |
21-700 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1352.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:PLN00070 275 QPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVCMIEFYLRANKMFVDYNEQLEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEDWNSC 180
Cdd:PLN00070 355 DHVTLQYLKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSC 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 LNNRVGFKSFAIPKESQTKVVEFSFHGKPAALRHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:PLN00070 435 LDNKVGFKGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:PLN00070 515 PGSGVVTKYLLK----------------SGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNR 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTVHIDFENEPIGVGKEEKKIFLRDIWPSSVETTRVVESNVLPDTFWEVYEAI 420
Cdd:PLN00070 579 NFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAI 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 421 DKGNSTWNQLTVPSGTLYDWDPSSTYTQEPPFFKDMTMCPPGPHAVKDAYCLLSFEDSITTDHISPSGSIHKDSTAARYL 500
Cdd:PLN00070 659 TKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 501 MDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILAGAEYG 580
Cdd:PLN00070 739 MERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYG 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 581 SGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRERYSVKIPNNIKDLRPCQDITVM 660
Cdd:PLN00070 819 SGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNISEIKPGQDVTVT 898
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1229784350 661 aaAENRKSFQCTLRFDTEVELTYFDHGGILHYVIRNLIST 700
Cdd:PLN00070 899 --TDNGKSFTCTLRFDTEVELAYFDHGGILPYVIRNLIKQ 936
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
21-699 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1142.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:PTZ00092 243 QPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVCMIEFYLRANKMFVDYNEQLEervYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEDWNSC 180
Cdd:PTZ00092 323 DEKTLDYLKQTGRSEEKVELIEKYLKANGLFRTYAEQIE---YSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTAC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 LNNRVGFKSFAIPKESQTKVVEFSFHGKPAALRHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:PTZ00092 400 LSAPVGFKGFGIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLS 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:PTZ00092 480 PGSKVVTKYLEA----------------SGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTVHIDFENEPIGVGKEEKKIFLRDIWPSSVETTRVVESNVLPDTFWEVYEAI 420
Cdd:PTZ00092 544 NFEGRVHPLTRANYLASPPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNI 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 421 DKGNSTWNQLTVPSGTLYDWDPSSTYTQEPPFFKDMTMCPPGPHAVKDAYCLLSFEDSITTDHISPSGSIHKDSTAARYL 500
Cdd:PTZ00092 624 TQGNKQWNELQVPKGKLYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 501 MDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLdGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILAGAEYG 580
Cdd:PTZ00092 704 MERGVERKDFNTYGARRGNDEVMVRGTFANIRLINKLC-GKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYG 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 581 SGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRERYSVKIpnNIKDLRPCQDITVM 660
Cdd:PTZ00092 783 SGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDL--NSGELKPGQDVTVK 860
|
650 660 670
....*....|....*....|....*....|....*....
gi 1229784350 661 aaAENRKSFQCTLRFDTEVELTYFDHGGILHYVIRNLIS 699
Cdd:PTZ00092 861 --TDTGKTFDTILRIDTEVEVEYFKHGGILQYVLRKLVK 897
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
21-698 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1108.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:PRK09277 240 QPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVCMIEFYLRANKMFVDyneQLEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEDWNSc 180
Cdd:PRK09277 320 DEETLDYLRLTGRDEEQVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 lnnrvgfksfAIPKESQTKVVEFSFHGKPAALRHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:PRK09277 396 ----------SAELGVQGFGLDEAEEGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLA 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:PRK09277 466 PGSKVVTDYLEK----------------AGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTVHIDFENEPIGVGKEEKKIFLRDIWPSSVETTRVVESNVLPDTFWEVYEAI 420
Cdd:PRK09277 530 NFEGRIHPLVKANYLASPPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADV 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 421 DKGNSTWNQLTVPSGTLYDWDPSSTYTQEPPFFKDMTMCPPGPHAVKDAYCLLSFEDSITTDHISPSGSIHKDSTAARYL 500
Cdd:PRK09277 610 FEGDERWNAIEVPEGPLYDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 501 MDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILAGAEYG 580
Cdd:PRK09277 690 LEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYG 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 581 SGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRERYSVKIpnnIKDLRPCQDITVM 660
Cdd:PRK09277 770 TGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEG---LEDLKPGATVTVV 846
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1229784350 661 AAAEN--RKSFQCTLRFDTEVELTYFDHGGILHYVIRNLI 698
Cdd:PRK09277 847 ITRADgeVVEFPVLCRIDTAVEVDYYRNGGILQYVLRDLL 886
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
21-699 |
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: 1093.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:COG1048 238 QPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVCMIEFYLRANKMFvdYNEQLEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEDWNSC 180
Cdd:COG1048 318 DEETLDYLRLTGRSEEQIELVEAYAKAQGLW--RDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 LNNRVGfksfaipkESQTKVVEFSFHGKPAALRHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:COG1048 396 LAAPVG--------EELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLA 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:COG1048 468 PGSKVVTDYLER----------------AGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNR 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTVHIDFENEPIGVGKEEKKIFLRDIWPSSVETTRVVESNVLPDTFWEVYEAI 420
Cdd:COG1048 532 NFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADV 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 421 DKGNSTWNQLTVPSGTLYDWDPSSTYTQEPPFFKDMTMCPPGPHAVKDAYCLLSFEDSITTDHISPSGSIHKDSTAARYL 500
Cdd:COG1048 612 FDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 501 MDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILAGAEYG 580
Cdd:COG1048 692 LEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYG 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 581 SGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRERYSvkIPNNIKDLRPCQDITVM 660
Cdd:COG1048 772 TGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFD--IEGLDEGLAPGKTVTVT 849
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1229784350 661 AAAEN--RKSFQCTLRFDTEVELTYFDHGGILHYVIRNLIS 699
Cdd:COG1048 850 ATRADgsTEEFPVLHRIDTPVEVEYYRAGGILQYVLRQLLA 890
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
21-698 |
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: 1080.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:TIGR01341 223 QPYYMNVPEVIGVKLTGKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPI 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVCMIEFYLRANKMFVDYNEqleERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEDWNSC 180
Cdd:TIGR01341 303 DDVTLQYLRLTGRDGDHVELVEKYARAQGLFYDDSE---EPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 LNNRVGFKSFAIPKESQTKVVEfsfhGKPAALRHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:TIGR01341 380 LEKNGGDKGFTLRKEPLKKKVN----GQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLA 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQkrcapldspnallmldENGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:TIGR01341 456 PGSKVVTDYLA----------------ESGLLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNR 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTVHIDFENEPIGVGKEEKKIFLRDIWPSSVETTRVVESNVLPDTFWEVYEAI 420
Cdd:TIGR01341 520 NFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 421 DKGNSTWNQLTVPSGTLYDWDPSSTYTQEPPFFKDMTMCPPGPHAVKDAYCLLSFEDSITTDHISPSGSIHKDSTAARYL 500
Cdd:TIGR01341 600 FEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 501 MDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILAGAEYG 580
Cdd:TIGR01341 680 QERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYG 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 581 SGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRERYSVKipnNIKDLRPCQDITVM 660
Cdd:TIGR01341 760 SGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGVIPLQFPQGEDAETLGLTGDETIDID---GIKDLKPGKEVTVT 836
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1229784350 661 AAAEN--RKSFQCTLRFDTEVELTYFDHGGILHYVIRNLI 698
Cdd:TIGR01341 837 FTNSKgeKITFKCVLRIDTEVELDYYKHGGILQYVLRKFL 876
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
21-699 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 953.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:PRK12881 240 QPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVCMIEFYLRANKMFVDyneQLEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEDWNSC 180
Cdd:PRK12881 320 DEQTLDYLRLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 LNNRVGFKSFAIPKESQTKVvefsfhgkpaALRHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:PRK12881 397 FSKPVAENGFAKKAQTSNGV----------DLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:PRK12881 467 PGSKVVTEYLER----------------AGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTVHIDFENEPIGVGKEEKKIFLRDIWPSSVETTRVVESNVLPDTFWEVYEAI 420
Cdd:PRK12881 531 NFEGRIHPNIKANFLASPPLVVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEV 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 421 DKGNSTWNQLTVPSGTLYDWDPSSTYTQEPPFFKDMTMCPPGPHAVKDAYCLLSFEDSITTDHISPSGSIHKDSTAARYL 500
Cdd:PRK12881 611 FKGSELWAAIEAPDGPLYDWDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 501 MDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILAGAEYG 580
Cdd:PRK12881 691 KENGVPKADFNSYGSRRGNHEVMMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYG 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 581 SGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRERYSVKIPNNikDLRPCQDITVM 660
Cdd:PRK12881 771 TGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPG--EIKPRQDVTLV 848
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1229784350 661 AAAEN--RKSFQCTLRFDTEVELTYFDHGGILHYVIRNLIS 699
Cdd:PRK12881 849 IHRADgsTERVPVLCRIDTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
21-370 |
3.82e-161 |
|
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: 470.25 E-value: 3.82e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:cd01586 156 QPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPV 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DhvtlqylkltgrtdetvcmiefylrankmfvdyneqleervySSHLELNLEDVEPCVSGPKRPHDRVPLremkedwnsc 180
Cdd:cd01586 236 D------------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL---------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 181 lnnrvgfksfaipkesqtkvvefsfhgkpaalrHGDVVIAAITSCTNTSNPSIMLGAALVAKKACELGLEVKPWIKTSLA 260
Cdd:cd01586 264 ---------------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 261 PGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITENDIVAAAVLSGNR 340
Cdd:cd01586 311 PGSRVVTKYLEA----------------SGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNR 374
|
330 340 350
....*....|....*....|....*....|
gi 1229784350 341 NFEGRVHPLTRANYLASPPLVVAYALAGTV 370
Cdd:cd01586 375 NFEGRIHPLVRANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
21-368 |
1.33e-141 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 422.21 E-value: 1.33e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDETVcmIEFYLRANKMFVDYNEqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLRE-MKEDWNS 179
Cdd:pfam00330 236 DETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASD--PGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElVPDPFAD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 180 CLNNRVGFKSfaipkesqtkvVEFSFHGKPAALRHGDVVIAAITSCTNTSNPSIMLGAALVaKKACELGLEVKPWIKTSL 259
Cdd:pfam00330 312 AVKRKAAERA-----------LEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 260 APGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASaitendivaaaVLSGN 339
Cdd:pfam00330 380 VPGSEVVRAYAEA----------------EGLDKILEEAGFEWRGPGCSMCIGNSDRLPPGERC-----------VSSSN 432
|
330 340
....*....|....*....|....*....
gi 1229784350 340 RNFEGRVHPLTRAnYLASPPLVVAYALAG 368
Cdd:pfam00330 433 RNFEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
475-642 |
1.60e-105 |
|
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: 318.45 E-value: 1.60e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 475 FEDSITTDHISPSGSIHKDSTAARYLMDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDK 554
Cdd:cd01580 2 LGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 555 LSVFDAAVRYRSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGL 634
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLGL 161
|
....*...
gi 1229784350 635 TGRERYSV 642
Cdd:cd01580 162 TGEETYDI 169
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
21-693 |
1.83e-61 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 217.32 E-value: 1.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTvtqMLRKHGV---VGKFVEFYGEGMSEISLADRATIANMSPDYGATMGS 97
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILE---LLRRLTVkggVGKIIEYFGPGVATLSVPERATITNMGAELGATTSI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 98 FPVDHVTLQYLKLTGRTDETVcmiefYLRANkmfvdyneqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEdw 177
Cdd:PRK07229 224 FPSDERTREFLKAQGREDDWV-----ELLAD----------PDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAG-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 178 nsclnnrvgfksfaipkesqTKVvefsfhgkpaalrhgDVViaAITSCTNTSNPSIMLGAALVAKKacelglEVKPwiKT 257
Cdd:PRK07229 287 --------------------IKV---------------DQV--LIGSCTNSSYEDLMRAASILKGK------KVHP--KV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 258 SL--APGSKVVtkylqkrcapldspnaLLMLDENGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASaitendivaaaV 335
Cdd:PRK07229 322 SLviNPGSRQV----------------LEMLARDGALADLIAAGARILENACGPCIGMGQAPATGNVS-----------L 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 336 LSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAG--TVHIDFENEPIGVGK-EEKKIFLRD----IWPSsvETTRVVEsn 407
Cdd:PRK07229 375 RTFNRNFPGRSgTKDAQV-YLASPETAAASALTGviTDPRTLALENGEYPKlEEPEGFAVDdagiIAPA--EDGSDVE-- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 408 vlpdtfwevyeaIDKGnstwnqltvpsgtlydwdPSSTYTQEPPFFKDMTMCPpgphavkdayCLLSFEDSITTDHISPS 487
Cdd:PRK07229 450 ------------VVRG------------------PNIKPLPLLEPLPDLLEGK----------VLLKVGDNITTDHIMPA 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 488 GsihkdstaARYLMdhgvnrkdfhsYgsrRGNHEVMIRGTFanIRLVNKlldgevgprtiqFPTgdklsvfdaavRYRSE 567
Cdd:PRK07229 490 G--------AKWLP-----------Y---RSNIPNISEFVF--EGVDNT------------FPE-----------RAKEQ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 568 GHdTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLgltgRERYSVKIPnN 647
Cdd:PRK07229 523 GG-GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKI----EEGDVLEIE-D 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1229784350 648 IKDLRPCQDITVMAAAENRkSFQCTLRFdTEVELTYFDHGGILHYV 693
Cdd:PRK07229 597 LREFLPGGPLTVVNVTKDE-EIEVRHTL-SERQIEILLAGGALNLI 640
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
21-370 |
4.77e-61 |
|
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: 209.66 E-value: 4.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPV 100
Cdd:cd01351 119 GPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 101 DHVTLQYLKLTGRTDEtvcmiefylrANKMFVDYNEQL--EERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEdwn 178
Cdd:cd01351 199 DKTTLKWLEATGRPLL----------KNLWLAFPEELLadEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 179 sclnnrvgfksfaipkesqtkvvefsfhgkpaalrhGDVVIAAITSCTNtSNPSIMLGAALVAKKAcelglEVKPWIKTS 258
Cdd:cd01351 266 ------------------------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 259 LAPGSKVVTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLdeeVASAITendivaaAVLSG 338
Cdd:cd01351 304 VTPGSRMVYATLSR----------------EGYYEILVDSGARILPPGCGPCMGNGARL---VADGEV-------GVSSG 357
|
330 340 350
....*....|....*....|....*....|..
gi 1229784350 339 NRNFEGRVHPLTRANYLASPPLVVAYALAGTV 370
Cdd:cd01351 358 NRNFPGRLGTYERHVYLASPELAAATAIAGKI 389
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
496-626 |
1.35e-43 |
|
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: 153.29 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 496 AARYLMDHGVNRKDFHSYGSRRGNHEVMIRGTFANIRLVNKLLDGEVGPRTIQFPTGDKLSVFDAAVRYRSEGHDTIILA 575
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1229784350 576 GAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQG 626
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
21-370 |
1.05e-37 |
|
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: 144.90 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 21 QPMSMVLPGVVVFKLKGKLKDGVTATDLVLtvtQMLRKHGV---VGKFVEFYGEGMSEISLADRATIANMSPDYGATMGS 97
Cdd:cd01585 118 EPYYIPMPKVVGVRLTGELPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATITNMGAELGATTSI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 98 FPVDHVTLQYLKLTGRTDETVcmiefYLRANkmfvdyneqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMkedw 177
Cdd:cd01585 195 FPSDERTREFLAAQGREDDWV-----ELAAD----------ADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREV---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 178 nsclnnrvgfksfaipkeSQTKVVEfsfhgkpaalrhgdvviAAITSCTNTSNPSIMLGAALVAkkacelGLEVKPWIKT 257
Cdd:cd01585 256 ------------------AGIKVDQ-----------------VAIGSCTNSSYEDLMTVAAILK------GRRVHPHVSM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 258 SLAPGSKVVtkylqkrcapldspnaLLMLDENGLQKYLDQLGFNTVEYGCTTCIGnsgdldeeVASAITENdivAAAVLS 337
Cdd:cd01585 295 VVAPGSKQV----------------LEMLARNGALADLLAAGARILESACGPCIG--------MGQAPPTG---GVSVRT 347
|
330 340 350
....*....|....*....|....*....|...
gi 1229784350 338 GNRNFEGRVHPLTRANYLASPPLVVAYALAGTV 370
Cdd:cd01585 348 FNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
22-369 |
3.72e-32 |
|
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: 129.48 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 22 PMSMVLPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVD 101
Cdd:cd01584 127 PWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 102 HVTLQYLKLTGRTDetvcmIEFYLRANKMFVDYNEqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEdwnscl 181
Cdd:cd01584 207 ERMKKYLKATGRAE-----IADLADEFKDDLLVAD--EGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKE------ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 182 nnrvgfksfaipkesqtkVVEfsFHGKPAALRHGdvviaAITSCTNTSNPSiMLGAALVAKKACELGLEVKpwIKTSLAP 261
Cdd:cd01584 274 ------------------VAE--KNGWPLDLRVG-----LIGSCTNSSYED-MGRAASIAKQALAHGLKCK--SIFTITP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 262 GSKvvtkylQKRCApldspnallmLDENGLQKYLDQLGFNTVEYGCTTCIG--NSGDLDEEvasaiTENDIVAaavlSGN 339
Cdd:cd01584 326 GSE------QIRAT----------IERDGLLQTFRDAGGIVLANACGPCIGqwDRKDIKKG-----EKNTIVT----SYN 380
|
330 340 350
....*....|....*....|....*....|..
gi 1229784350 340 RNFEGR--VHPLTRAnYLASPPLVVAYALAGT 369
Cdd:cd01584 381 RNFTGRndANPATHA-FVASPEIVTAMAIAGT 411
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-370 |
1.72e-31 |
|
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: 126.92 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 28 PGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVDHVTLQY 107
Cdd:cd01583 127 PETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 108 LKLTGRTDETVcmiefyLRANkmfvdyneqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREmkedwnsclnnrvgf 187
Cdd:cd01583 207 LKGRGKAYWKE------LKSD----------EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSE--------------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 188 ksfAIPkesqTKVvefsfhgkpaalrhgDVVIaaITSCTNtSNPSIMLGAALVAKkacelGLEVKPWIKTSLAPGSKVVt 267
Cdd:cd01583 256 ---VEG----IKI---------------DQVF--IGSCTN-GRLEDLRAAAEILK-----GRKVADGVRLIVVPASQRV- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 268 kYLQkrcapldspnallMLDEnGLQKYLDQLGFNTVEYGCTTCIGNSGDLdeevasaITENDIVAAavlSGNRNFEGRVH 347
Cdd:cd01583 305 -YKQ-------------AEKE-GLIEIFIEAGAEVRPPGCGACLGGHMGV-------LAPGERCVS---TSNRNFKGRMG 359
|
330 340
....*....|....*....|...
gi 1229784350 348 PLTRANYLASPPLVVAYALAGTV 370
Cdd:cd01583 360 SPGARIYLASPATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
33-370 |
3.10e-30 |
|
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: 123.60 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 33 FKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVDHVTLQYLKLTG 112
Cdd:COG0065 161 IEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKGRP 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 113 RTDETVcmiefyLRAnkmfvDyneqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEdwnsclnnrvgfksfai 192
Cdd:COG0065 241 FAPWRT------LKS-----D-----EDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEG----------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 193 pkesqTKVvefsfhgkpaalrhgDVVIaaITSCTNtsnpsimlG-------AALVAKkacelGLEVKPWIKTSLAPGSKV 265
Cdd:COG0065 288 -----IKI---------------DQVF--IGSCTN--------GriedlraAAEILK-----GRKVAPGVRAIVVPGSQE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 266 VtkYLQkrcapldspnallMLDEnGLQKYLDQLGFNTVEYGCTTCIGNSGDLdeevasaITENDIVAAavlSGNRNFEGR 345
Cdd:COG0065 333 V--YRQ-------------AEAE-GLDEIFIEAGAEWREPGCGMCLGMNMGV-------LAPGERCAS---TSNRNFEGR 386
|
330 340
....*....|....*....|....*.
gi 1229784350 346 V-HPLTRAnYLASPPLVVAYALAGTV 370
Cdd:COG0065 387 MgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
33-368 |
5.52e-23 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 102.18 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 33 FKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVDHVTLQYLKLTG 112
Cdd:PRK00402 161 VVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKERA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 113 RTDETVcmiefylrankMFVDyneqlEERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREMKEdwnsclnnrvgfksfai 192
Cdd:PRK00402 241 GRDYKP-----------WKSD-----EDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEG----------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 193 pkesqTKVvefsfhgkpaalrhgDVVIaaITSCTNtsnpsimlG-------AALVAKkacelGLEVKPWIKTSLAPGSKV 265
Cdd:PRK00402 288 -----TKV---------------DQVF--IGSCTN--------GrledlriAAEILK-----GRKVAPGVRLIVIPASQK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 266 VtkYLQkrcapldspnALlmldENGLQKYLDQLGFnTVEY-GCTTCIGNSGDL--DEEVASAITendivaaavlsgNRNF 342
Cdd:PRK00402 333 I--YLQ----------AL----KEGLIEIFVDAGA-VVSTpTCGPCLGGHMGVlaPGEVCLSTT------------NRNF 383
|
330 340
....*....|....*....|....*.
gi 1229784350 343 EGRVHPLTRANYLASPPLVVAYALAG 368
Cdd:PRK00402 384 KGRMGSPESEVYLASPAVAAASAVTG 409
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
476-630 |
2.84e-19 |
|
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: 84.03 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 476 EDSITTDHISPSGsihkdstaARYLmdhgvnrkdfhsygSRRGNHEVMIRGTFANIrlvnkllDGEVGPRTiqfptgdkl 555
Cdd:cd01579 3 GDNITTDHIMPAG--------AKVL--------------PLRSNIPAISEFVFHRV-------DPTFAERA--------- 44
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229784350 556 svfdaavryrSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAE 630
Cdd:cd01579 45 ----------KAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYD 109
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
27-370 |
1.27e-18 |
|
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: 88.05 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 27 LPGVVVFKLKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVDhvtlq 106
Cdd:cd01582 124 IPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD----- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 107 ylkltgrtdetvcmiefylrankmfvdyneqleervySSHLELNLEDVEPCVSGPKRPHDRVPLREMKEdwnsclnnrvg 186
Cdd:cd01582 199 -------------------------------------AKHLILDLSTLSPYVSGPNSVKVSTPLKELEA----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 187 fKSFAIPKesqtkvvefsfhgkpaalrhgdvviAAITSCTNTSNPSIMLGAALVAKKACELG-LEVKPWIKTSLAPGSKV 265
Cdd:cd01582 231 -QNIKINK-------------------------AYLVSCTNSRASDIAAAADVVKGKKEKNGkIPVAPGVEFYVAAASSE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 266 VTKYLQKrcapldspnallmldeNGLQKYLDQLGFNTVEYGCTTCIGNSGDLDEEVASAITendivaaavlSGNRNFEGR 345
Cdd:cd01582 285 VQAAAEK----------------NGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGIS----------ATNRNFKGR 338
|
330 340
....*....|....*....|....*
gi 1229784350 346 VHPLTRANYLASPPLVVAYALAGTV 370
Cdd:cd01582 339 MGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
34-370 |
2.13e-17 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 85.56 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 34 KLKGKLKDGVTATDLVLTVtqmLRKHGV---VGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVDHVTLQYLKl 110
Cdd:PRK05478 169 EVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 111 tGRtdetvcmiEFylrANK-----MFVDYNEQL---EERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREmkedwnscln 182
Cdd:PRK05478 245 -GR--------PF---APKgedwdKAVAYWKTLksdEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDG---------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 183 nrvgfkSFAIPKESQTKVVEFSFH----------GKPAALRHGDVVIaaITSCTNtSNPSIMLGAALVAKkacelGLEVK 252
Cdd:PRK05478 303 ------KVPDPEDFADPVKRASAEralaymglkpGTPITDIKIDKVF--IGSCTN-SRIEDLRAAAAVVK-----GRKVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 253 PWIKTSLAPGSKVVtkylqKRCApldspnallmlDENGLQKYLDQLGFNTVEYGCTTCIG-NSGDLDEEVASAITEndiv 331
Cdd:PRK05478 369 PGVRALVVPGSGLV-----KAQA-----------EAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLPPGERCASTS---- 428
|
330 340 350
....*....|....*....|....*....|....*....
gi 1229784350 332 aaavlsgNRNFEGRVHPLTRaNYLASPPLVVAYALAGTV 370
Cdd:PRK05478 429 -------NRNFEGRQGKGGR-THLVSPAMAAAAAITGHF 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
572-642 |
2.43e-17 |
|
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: 77.51 E-value: 2.43e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229784350 572 IILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAesLGLTGRERYSV 642
Cdd:cd00404 18 VVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDY--LKLHTGDELDI 86
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
35-372 |
2.87e-16 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 81.88 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 35 LKGKLKDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSEISLADRATIANMSPDYGATMGSFPVDHVTLQYLKltGRT 114
Cdd:PRK12466 172 VDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLR--GRP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 115 detvcmiefYLRANKMF---VDYNEQL---EERVYSSHLELNLEDVEPCVSGPKRPHDRVPLREmkedwnsclnnRVGF- 187
Cdd:PRK12466 250 ---------RAPKGALWdaaLAYWRTLrsdADAVFDREVEIDAADIAPQVTWGTSPDQAVPITG-----------RVPDp 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 188 KSFAIPKESQTKVVEFSFHGKPAALRHGDVVI--AAITSCTNtSNPSIMLGAALVAKkacelGLEVKPWIKTSLAPGSKV 265
Cdd:PRK12466 310 AAEADPARRAAMERALDYMGLTPGTPLAGIPIdrVFIGSCTN-GRIEDLRAAAAVLR-----GRKVAPGVRAMVVPGSGA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 266 VtkylqKRCApldspnallmlDENGLQKYLDQLGFNTVEYGCTTCIGNSGDL---DEEVASaitendivaaavlSGNRNF 342
Cdd:PRK12466 384 V-----RRQA-----------EAEGLARIFIAAGFEWREPGCSMCLAMNDDVlapGERCAS-------------TTNRNF 434
|
330 340 350
....*....|....*....|....*....|
gi 1229784350 343 EGRVHPLTRAnYLASPPLVVAYALAGtvHI 372
Cdd:PRK12466 435 EGRQGPGART-HLMSPAMVAAAAVAG--HI 461
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
551-628 |
1.46e-11 |
|
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: 62.87 E-value: 1.46e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229784350 551 TGDKLSVFDAAVRYRSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGED 628
Cdd:cd01578 51 TGEYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 128
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
571-638 |
7.12e-10 |
|
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: 56.06 E-value: 7.12e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229784350 571 TIILAGAEYGSGSSR---DWAAKGpmlLGVKAVIAKSFEHTHRSNLVGMGIIPICFKQGEDAESLGLTGRE 638
Cdd:cd01577 19 DIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE 86
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
572-620 |
3.88e-08 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 53.27 E-value: 3.88e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1229784350 572 IILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIP 620
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP 100
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
477-621 |
1.99e-07 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 51.71 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229784350 477 DSITTDHISPsgsihkdstaARYLmdHGVNRKDFHsygsrrgnhevmiRGTFANIRLvNKLLDGEvgprtiqFPTGDKls 556
Cdd:COG0066 16 DNIDTDQIIP----------ARFL--KTIDREGLG-------------KHLFEDWRY-DRSPDPD-------FVLNQP-- 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229784350 557 vfdaavRYRseGHDtIILAGAEYGSGSSRD---WAAKGpmlLGVKAVIAKSFEHTHRSNLVGMGIIPI 621
Cdd:COG0066 61 ------RYQ--GAD-ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPI 116
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
572-621 |
8.08e-06 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 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: 273961 [Multi-domain] Cd Length: 154 Bit Score: 46.26 E-value: 8.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1229784350 572 IILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFEHTHRSNLVGMGIIPI 621
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
572-621 |
3.08e-05 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 44.82 E-value: 3.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1229784350 572 IILAGAEYGSGSSRD---WAAKGpmlLGVKAVIAKSFEHTHRSNLVGMGiIPI 621
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIG-LPV 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
571-632 |
5.29e-05 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 44.73 E-value: 5.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229784350 571 TIILAGAEYGSGSSRD---WAakgpmLL--GVKAVIAKSFEHTHRSNLVGMGIIPICFKQgEDAESL 632
Cdd:PRK01641 69 SILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIVLPE-EDVDEL 129
|
|
| |
