|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-901 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1750.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 1 MAANFKEQSKKHFDLNGQSYTYYDLKAVEEQGITKVLKLPYSIRVLLESLLRQEDDFVITDDHIKALSQFGKDG-NEGEV 79
Cdd:PRK09277 1 MSSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAkPDREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 80 PFKPSRVILQDFTGVPAVVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQF 159
Cdd:PRK09277 81 PFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 160 LNWATKAFDNYNAVPPATGIVHQVNLEYLASVVHVRDvDGEKTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLG 239
Cdd:PRK09277 161 LKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTRE-DGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 240 QPSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPV 319
Cdd:PRK09277 240 QPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 320 DDESLKYMKLTGRSDEHIALVKEYLKQNHMFFDvEKEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFENSvt 399
Cdd:PRK09277 320 DEETLDYLRLTGRDEEQVALVEAYAKAQGLWRD-PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKS-- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 400 APAGNQGHGLDKSEFdkkaeinfkdGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAP 479
Cdd:PRK09277 397 AELGVQGFGLDEAEE----------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 480 GSKVVTGYLRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLAS 559
Cdd:PRK09277 467 GSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLAS 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 560 PQLVVAYALAGTVDIDLQNEPIGKGNDGEDVYLKDIWPSIKEVSDTVDSVVTPELFIEEYNNVYNNNELWNEIDVTDQPL 639
Cdd:PRK09277 547 PPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPL 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 640 YDFDPNSTYIQNPSFFQGLSKEPGTIVPLNGLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRR 719
Cdd:PRK09277 627 YDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRR 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 720 GNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGV 799
Cdd:PRK09277 707 GNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGV 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 800 KTVIAQSYERIHRSNLVMMGVLPLEFKKGESADSLGLDGTEEISVNIDENVQPHDYVKVTAKKQDGDLVEFDAMVRFDSL 879
Cdd:PRK09277 787 KAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFPVLCRIDTA 866
|
890 900
....*....|....*....|..
gi 612907865 880 VEMDYYRHGGILQMVLRNKLAQ 901
Cdd:PRK09277 867 VEVDYYRNGGILQYVLRDLLAS 888
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
8-901 |
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: 1682.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 8 QSKKHFDLNGQSYTYYDLKAVEEQGItKVLKLPYSIRVLLESLLRQEDDFVITDDHIKALSQFGKDG-NEGEVPFKPSRV 86
Cdd:COG1048 6 KARKTLTVGGKPYTYYSLPALEEAGG-DISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKArGDDEIPFRPARV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 87 ILQDFTGVPAVVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQFLNWATKA 166
Cdd:COG1048 85 LMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 167 FDNYNAVPPATGIVHQVNLEYLASVVHVRDVDGEKTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPI 246
Cdd:COG1048 165 FDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 247 PEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKY 326
Cdd:COG1048 245 PEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 327 MKLTGRSDEHIALVKEYLKQNHMFFDVEKEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFENSVTAPAGNqg 406
Cdd:COG1048 325 LRLTGRSEEQIELVEAYAKAQGLWRDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVGE-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 407 hgldksEFDKKAEINFkDGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAPGSKVVTG 486
Cdd:COG1048 403 ------ELDKPVRVEV-DGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 487 YLRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAY 566
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAY 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 567 ALAGTVDIDLQNEPIGKGNDGEDVYLKDIWPSIKEVSDTVDSVVTPELFIEEYNNVYNNNELWNEIDVTDQPLYDFDPNS 646
Cdd:COG1048 556 ALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDS 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 647 TYIQNPSFFQGLSKEPGTIVPLNGLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRRGNHEVMV 726
Cdd:COG1048 636 TYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMM 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 727 RGTFANIRIKNQLAPGTEGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQS 806
Cdd:COG1048 716 RGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAES 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 807 YERIHRSNLVMMGVLPLEFKKGESADSLGLDGTEEISV-NIDENVQPHDYVKVTAKKQDGDLVEFDAMVRFDSLVEMDYY 885
Cdd:COG1048 796 FERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIeGLDEGLAPGKTVTVTATRADGSTEEFPVLHRIDTPVEVEYY 875
|
890
....*....|....*.
gi 612907865 886 RHGGILQMVLRNKLAQ 901
Cdd:COG1048 876 RAGGILQYVLRQLLAA 891
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
18-899 |
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: 1408.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 18 QSYTYYDLKAVEEQGiTKVLKLPYSIRVLLESLLRQEDDFVITDDHIKALSQFGKDG-NEGEVPFKPSRVILQDFTGVPA 96
Cdd:TIGR01341 1 KTYYYYSLKALEESG-GKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEvADTEIAFKPARVVMQDFTGVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 97 VVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQFLNWATKAFDNYNAVPPA 176
Cdd:TIGR01341 80 VVDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 177 TGIVHQVNLEYLASVVHVRDVDGEKTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLVN 256
Cdd:TIGR01341 160 TGIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 257 SLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKYMKLTGRSDEH 336
Cdd:TIGR01341 240 KLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 337 IALVKEYLKQNHMFFDvEKEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFENSVTAPAGNQGHGLDKSEFDK 416
Cdd:TIGR01341 320 VELVEKYARAQGLFYD-DSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 417 KAEinfkdGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAPGSKVVTGYLRDAGLQPY 496
Cdd:TIGR01341 399 KVN-----GQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 497 LDELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTVDIDL 576
Cdd:TIGR01341 474 LEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 577 QNEPIGKGNDGEDVYLKDIWPSIKEVSDTVDSVVTPELFIEEYNNVYNNNELWNEIDVTDQPLYDFDPNSTYIQNPSFFQ 656
Cdd:TIGR01341 554 YTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 657 GLSKEPGTIVPLNGLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRRGNHEVMVRGTFANIRIK 736
Cdd:TIGR01341 634 EMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 737 NQLAPGTEGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLV 816
Cdd:TIGR01341 714 NLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLV 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 817 MMGVLPLEFKKGESADSLGLDGTEEISVNIDENVQPHDYVKVTAKKQDGDLVEFDAMVRFDSLVEMDYYRHGGILQMVLR 896
Cdd:TIGR01341 794 GMGVIPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLR 873
|
...
gi 612907865 897 NKL 899
Cdd:TIGR01341 874 KFL 876
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
9-900 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1403.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 9 SKKHFDLNGQSYTYYDLKAVEEQGITKVLKLPYSIRVLLESLLRQEDDFVITDDHIKALSQFGKDG-NEGEVPFKPSRVI 87
Cdd:PRK12881 8 TLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERkSDDEIPFVPARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 88 LQDFTGVPAVVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQFLNWATKAF 167
Cdd:PRK12881 88 MQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 168 DNYNAVPPATGIVHQVNLEYLASVVHVRDVDGEKTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIP 247
Cdd:PRK12881 168 DNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 248 EVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKYM 327
Cdd:PRK12881 248 DVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 328 KLTGRSDEHIALVKEYLKQNHMFFDvEKEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFENSVTAPAGNQGh 407
Cdd:PRK12881 328 RLTGRTEAQIALVEAYAKAQGLWGD-PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENG- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 408 gldkseFDKKAEinfkDGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAPGSKVVTGY 487
Cdd:PRK12881 406 ------FAKKAQ----TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 488 LRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAYA 567
Cdd:PRK12881 476 LERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAYA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 568 LAGTVDIDLQNEPIGKGNDGEDVYLKDIWPSIKEVSDTVDSVVTPELFIEEYNNVYNNNELWNEIDVTDQPLYDFDPNST 647
Cdd:PRK12881 556 LAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKST 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 648 YIQNPSFFQGLSKEPGTIVPLNGLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRRGNHEVMVR 727
Cdd:PRK12881 636 YIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMMR 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 728 GTFANIRIKNQLAPGTEGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSY 807
Cdd:PRK12881 716 GTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESF 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 808 ERIHRSNLVMMGVLPLEFKKGESADSLGLDGTEEISVN-IDENVQPHDYVKVTAKKQDGDLVEFDAMVRFDSLVEMDYYR 886
Cdd:PRK12881 796 ERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRQDVTLVIHRADGSTERVPVLCRIDTPIEVDYYK 875
|
890
....*....|....
gi 612907865 887 HGGILQMVLRNKLA 900
Cdd:PRK12881 876 AGGILPYVLRQLLA 889
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
16-901 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1347.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 16 NGQSYTYYDLKAVEEqgiTKVLKLPYSIRVLLESLLRQEDDFVITDDHIKALSQFGKDGNEG-EVPFKPSRVILQDFTGV 94
Cdd:PTZ00092 25 DGGSYKYYSLNELHD---PRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQiEIPFKPARVLLQDFTGV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 95 PAVVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQFLNWATKAFDNYNAVP 174
Cdd:PTZ00092 102 PAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSKAFKNLLIVP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 175 PATGIVHQVNLEYLASVVhvrdVDGEKTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRL 254
Cdd:PTZ00092 182 PGSGIVHQVNLEYLARVV----FNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 255 VNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKYMKLTGRSD 334
Cdd:PTZ00092 258 TGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 335 EHIALVKEYLKQNHMFFDvEKEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFENSVTAPAGNQGHGLDKSEF 414
Cdd:PTZ00092 338 EKVELIEKYLKANGLFRT-YAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGFGIPEEKH 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 415 DKKAEINFKdGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAPGSKVVTGYLRDAGLQ 494
Cdd:PTZ00092 417 EKKVKFTYK-GKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 495 PYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTVDI 574
Cdd:PTZ00092 496 KYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGRVNI 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 575 DLQNEPIGKGNDGEDVYLKDIWPSIKEVSDTVDSVVTPELFIEEYNNVYNNNELWNEIDVTDQPLYDFDPNSTYIQNPSF 654
Cdd:PTZ00092 576 DFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTYIHNPPF 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 655 FQGLSKEPGTIVPLNGLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRRGNHEVMVRGTFANIR 734
Cdd:PTZ00092 656 FQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRGTFANIR 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 735 IKNQLAPGTeGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSN 814
Cdd:PTZ00092 736 LINKLCGKV-GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSN 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 815 LVMMGVLPLEFKKGESADSLGLDGTEEISVNIDE-NVQPHDYVKVtaKKQDGDlvEFDAMVRFDSLVEMDYYRHGGILQM 893
Cdd:PTZ00092 815 LVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTV--KTDTGK--TFDTILRIDTEVEVEYFKHGGILQY 890
|
....*...
gi 612907865 894 VLRNKLAQ 901
Cdd:PTZ00092 891 VLRKLVKG 898
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
22-901 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1136.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 22 YYDLKAVEEqgiTKVLKLPYSIRVLLESLLRQEDDFVITDDHIKALSQFGKDG-NEGEVPFKPSRVILQDFTGVPAVVDL 100
Cdd:PLN00070 63 YYSLPALND---PRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSpKQVEIPFKPARVLLQDFTGVPAVVDL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 101 ASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQFLNWATKAFDNYNAVPPATGIV 180
Cdd:PLN00070 140 ACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 181 HQVNLEYLASVVHvrDVDGekTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLVNSLPQ 260
Cdd:PLN00070 220 HQVNLEYLGRVVF--NTDG--ILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 261 GATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKYMKLTGRSDEHIALV 340
Cdd:PLN00070 296 GVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 341 KEYLKQNHMFFDVEKEDPN--YTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFENSVTAPAGNQGHGLDKSEFDKKA 418
Cdd:PLN00070 376 EAYLRANKMFVDYNEPQQErvYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 419 EINFkDGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAPGSKVVTGYLRDAGLQPYLD 498
Cdd:PLN00070 456 KFSF-HGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLN 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 499 ELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTVDIDLQN 578
Cdd:PLN00070 535 QQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEK 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 579 EPIGKGNDGEDVYLKDIWPSIKEVSDTVDSVVTPELFIEEYNNVYNNNELWNEIDVTDQPLYDFDPNSTYIQNPSFFQGL 658
Cdd:PLN00070 615 EPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNM 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 659 SKEPGTIVPLNGLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRRGNHEVMVRGTFANIRIKNQ 738
Cdd:PLN00070 695 TMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNK 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 739 LAPGTEGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMM 818
Cdd:PLN00070 775 LLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGM 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 819 GVLPLEFKKGESADSLGLDGTEEISVNIDENV---QPHDYVKVTAKKQDgdlvEFDAMVRFDSLVEMDYYRHGGILQMVL 895
Cdd:PLN00070 855 GIIPLCFKSGEDADTLGLTGHERYTIDLPSNIseiKPGQDVTVTTDNGK----SFTCTLRFDTEVELAYFDHGGILPYVI 930
|
....*.
gi 612907865 896 RNKLAQ 901
Cdd:PLN00070 931 RNLIKQ 936
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
85-572 |
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: 767.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 85 RVILQDFTGVPAVVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSVQVDSYANPEALERNMKLEFERNYERYQFLNWAT 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 165 KAFDNYNAVPPATGIVHQVNLEYLASVVHVRDVDGEKTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYF 244
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 245 PIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDdesl 324
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 325 kymkltgrsdehialvkeylkqnhmffdvekedpnyTDVIELDLSTVEASLSGPKRPQDLIFLsdmkssfensvtapagn 404
Cdd:cd01586 237 ------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 405 qghgldksefdkkaeinfkdgskatmkTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEYVKTSLAPGSKVV 484
Cdd:cd01586 264 ---------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 485 TGYLRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIADEDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVV 564
Cdd:cd01586 317 TKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVV 396
|
....*...
gi 612907865 565 AYALAGTV 572
Cdd:cd01586 397 AYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
73-570 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 655.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 73 DGNEGEVPFKPSRVILQDFTGVPAVVDLASLRKAMDDVGGDITKINPEVPVDLVIDHSvqvdsyanPEALERNMKLEFER 152
Cdd:pfam00330 10 EELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 153 NYERYQFLNWATKAFdNYNAVPPATGIVHQVNLEYLasvvhvrdvdgekTAFPD-TLVGTDSHTTMINGIGVLGWGVGGI 231
Cdd:pfam00330 82 NKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGGLGALAFGVGGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 232 EAEAGMLGQPSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYG 311
Cdd:pfam00330 148 EAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 312 ATCGFFPVDDESLKYMKLTGRSDEHIalVKEYLKQNHMFFDVEKEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSD-M 390
Cdd:pfam00330 228 ATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 391 KSSFENSVTAPAGnqghgldksefdKKAEINFKDGSKATMKTGDIAIAAITSCTNTSNPYVMLGAGLVaKKAVEKGLKVP 470
Cdd:pfam00330 306 PDPFADAVKRKAA------------ERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 471 EYVKTSLAPGSKVVTGYLRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEiekaiadedllVTSVLSGNRNFEGRIHP 550
Cdd:pfam00330 373 PGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPG-----------ERCVSSSNRNFEGRQGP 441
|
490 500
....*....|....*....|
gi 612907865 551 LVKAnYLASPQLVVAYALAG 570
Cdd:pfam00330 442 GGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
676-844 |
1.31e-111 |
|
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: 339.25 E-value: 1.31e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 676 KFGDSVTTDHISPAGAIGKDTPAGKYLQDHQVPIREFNSYGSRRGNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTNE 755
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 756 VMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEFKKGESADSLG 835
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
....*....
gi 612907865 836 LDGTEEISV 844
Cdd:cd01580 161 LTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-572 |
8.72e-94 |
|
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: 300.95 E-value: 8.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 85 RVILQDFTGVPAVVDLASLRKAmddvggdiTKINPEVPVDLVIDHSVQvdsyanpealernmkLEFERNYERYQFLNWAT 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAAL--------GKVADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 165 KAFDNYNaVPPATGIVHQVNLEYLASvvhvrdvdgektaFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYF 244
Cdd:cd01351 58 ALQGIAF-YRPGVGIIHQIMVENLAL-------------PGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 245 PIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESL 324
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 325 KYMKLTGRSDehiALVKEYLKQNHMFFDvekEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSsfensvtapagn 404
Cdd:cd01351 204 KWLEATGRPL---LKNLWLAFPEELLAD---EGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG------------ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 405 qghgldksefdkkaeinfkdgskatmktGDIAIAAITSCTNtSNPYVMLGAGLVAKKAvekglKVPEYVKTSLAPGSKVV 484
Cdd:cd01351 266 ----------------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLIVTPGSRMV 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 485 TGYLRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEkaiadedllvTSVLSGNRNFEGRIHPLVKANYLASPQLVV 564
Cdd:cd01351 312 YATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGE----------VGVSSGNRNFPGRLGTYERHVYLASPELAA 381
|
....*...
gi 612907865 565 AYALAGTV 572
Cdd:cd01351 382 ATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
78-901 |
1.71e-83 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 281.65 E-value: 1.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 78 EVPFKPSRVILQDFTGVPAVVDLASLRKamddvggditkinPEVPVDLvidhSVQ-VDsyanpealeRNMKLEFERNYER 156
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMGL-------------DRVKTEL----SVQyVD---------HNLLQADFENADD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 157 YQFLNWATKafdNYNAV--PPATGIVHQVNLEylasvvhvrdvdgeKTAFP-DTLVGTDSHTTMINGIGVLGWGVGGIEA 233
Cdd:PRK07229 78 HRFLQSVAA---KYGIYfsKPGNGICHQVHLE--------------RFAFPgKTLLGSDSHTPTAGGLGMLAIGAGGLDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 234 EAGMLGQPSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGAT 313
Cdd:PRK07229 141 ALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 314 CGFFPVDDESLKYMKLTGRSDEHIALVKEylkqnhmffdvekEDPNYTDVIELDLSTVEASLSGPkrpqdliflsdmkSS 393
Cdd:PRK07229 221 TSIFPSDERTREFLKAQGREDDWVELLAD-------------PDAEYDEVIEIDLSELEPLIAGP-------------HS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 394 FENSVTApagnqghgldkSEFDKKAeinfkdgskatmktgdIAIAAITSCTNTSnpYVMLGAglVAKKAveKGLKVPEYV 473
Cdd:PRK07229 275 PDNVVPV-----------SEVAGIK----------------VDQVLIGSCTNSS--YEDLMR--AASIL--KGKKVHPKV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 474 KTSLAPGSKVVTGYL-RDAGLQPYLDeLGFNLVGYGCTTCIGNSGpllpeiEKAIADedllvTSVLSGNRNFEGRI-HPL 551
Cdd:PRK07229 322 SLVINPGSRQVLEMLaRDGALADLIA-AGARILENACGPCIGMGQ------APATGN-----VSLRTFNRNFPGRSgTKD 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 552 VKAnYLASPQLVVAYALAGTV----DIDLQNEPIGKGNDGEDVYLKD--IWPSIKEVSDtVDSVVTPelfieeynnvynn 625
Cdd:PRK07229 390 AQV-YLASPETAAASALTGVItdprTLALENGEYPKLEEPEGFAVDDagIIAPAEDGSD-VEVVRGP------------- 454
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 626 nelwneidvTDQPLYDFDPnstyiqnpsFfqglskePGTIvplnGLRVMGKFGDSVTTDHISPAGAigkdtpagKYLqdh 705
Cdd:PRK07229 455 ---------NIKPLPLLEP---------L-------PDLL----EGKVLLKVGDNITTDHIMPAGA--------KWL--- 494
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 706 qvpirefnSYgsrRGNHEVMVRGTFanIRIKNqlapgteggfttywptnevmpifDAAMKYKEDGTGLVVlAGNDYGMGS 785
Cdd:PRK07229 495 --------PY---RSNIPNISEFVF--EGVDN-----------------------TFPERAKEQGGGIVV-GGENYGQGS 537
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 786 SRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEFKKGESADSLGLDGTEEIsVNIDENVQPHDyVKVTAKKQDg 865
Cdd:PRK07229 538 SREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEGDVLEI-EDLREFLPGGP-LTVVNVTKD- 614
|
810 820 830
....*....|....*....|....*....|....*..
gi 612907865 866 dlveFDAMVRFD-SLVEMDYYRHGGILQMVlRNKLAQ 901
Cdd:PRK07229 615 ----EEIEVRHTlSERQIEILLAGGALNLI-KKKLAA 646
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
152-572 |
7.95e-52 |
|
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: 186.50 E-value: 7.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 152 RNYERYQFLNWATKAFDNYNAvPPATGIVHQVNLEYLAsvvhvrdVDGEktafpdTLVGTDSHTTMINGIGVLGWGVGGI 231
Cdd:cd01585 44 ENADDHRFLQTVAARYGIYFS-RPGNGICHQVHLERFA-------VPGK------TLLGSDSHTPTAGGLGMLAIGAGGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 232 EAEAGMLGQPSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYG 311
Cdd:cd01585 110 DVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 312 ATCGFFPVDDESLKYMKLTGRSDEHIALVKEylkqnhmffdvekEDPNYTDVIELDLSTVEASLSGPKRPQDLIflsdmk 391
Cdd:cd01585 190 ATTSIFPSDERTREFLAAQGREDDWVELAAD-------------ADAEYDEEIEIDLSELEPLIARPHSPDNVV------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 392 ssfenSVTAPAGNQghgldksefdkkaeinfkdgskatmktgdIAIAAITSCTNTSNPYVMLGAGLVakkaveKGLKVPE 471
Cdd:cd01585 251 -----PVREVAGIK-----------------------------VDQVAIGSCTNSSYEDLMTVAAIL------KGRRVHP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 472 YVKTSLAPGSKVVTGYLRDAGLQPYLDELGFNLVGYGCTTCIGnsgpllpeIEKAIADEDLlvtSVLSGNRNFEGRIHPL 551
Cdd:cd01585 291 HVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIG--------MGQAPPTGGV---SVRTFNRNFEGRSGTK 359
|
410 420
....*....|....*....|.
gi 612907865 552 VKANYLASPQLVVAYALAGTV 572
Cdd:cd01585 360 DDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
119-571 |
2.73e-51 |
|
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: 185.72 E-value: 2.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 119 PEVPVDLVIDHSVQVDsyanpEALERNMKLEFERNYERYQFLNWATKAFdNYNAVPPATGIVHQVNLEylasvvhvrdvd 198
Cdd:cd01584 24 VAVPSTIHCDHLIEAQ-----VGGEKDLKRAKDINKEVYDFLASAGAKY-GIGFWKPGSGIIHQIVLE------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 199 geKTAFPDTL-VGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRK 277
Cdd:cd01584 86 --NYAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 278 KGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKYMKLTGRSDehialVKEYLKQNHMFFDVEKED 357
Cdd:cd01584 164 KGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAE-----IADLADEFKDDLLVADEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 358 PNYTDVIELDLSTVEASLSGPKRPQDLIFLSDMKSSFEnsvtapagnqghgldksefdkkaeinfKDGSKAtmktgDIAI 437
Cdd:cd01584 239 AEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAE---------------------------KNGWPL-----DLRV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 438 AAITSCTNTSnpYV-MLGAGLVAKKAVEKGLKVPeyVKTSLAPGSKVVTGYLRDAGLQPYLDELGFNLVGYGCTTCIGNS 516
Cdd:cd01584 287 GLIGSCTNSS--YEdMGRAASIAKQALAHGLKCK--SIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQW 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 612907865 517 GPllPEIEKaiADEDLLVTSVlsgNRNFEGR--IHPLVKAnYLASPQLVVAYALAGT 571
Cdd:cd01584 363 DR--KDIKK--GEKNTIVTSY---NRNFTGRndANPATHA-FVASPEIVTAMAIAGT 411
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
71-572 |
5.60e-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: 176.37 E-value: 5.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 71 GKDGNEGEVPF-KPSRVILQDFTGVPAVvdlaslrKAMDDVGGDitKI-NPEVPVdLVIDHSVqvdsYANPEALERNMKl 148
Cdd:COG0065 15 GREVEPGEIVLlYIDLHLVHDVTSPQAF-------EGLREAGGR--KVwDPDRIV-AVFDHNV----PTKDPKSAEQVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 149 EFERNYERYQFlnwatKAFDNYNAvppatGIVHQVNLEylasvvhvrdvdgEKTAFP-DTLVGTDSHTTMINGIGVLGWG 227
Cdd:COG0065 80 TLREFAKEFGI-----TFFDVGDP-----GICHVVLPE-------------QGLVLPgMTIVGGDSHTCTHGAFGAFAFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 228 VGGIEAEAGMLGQPSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMA 307
Cdd:COG0065 137 IGTTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 308 PEYGATCGFFPVDDESLKYMKltGRSDEHIALVKEylkqnhmffDvekEDPNYTDVIELDLSTVEaslsgpkrPQdlifl 387
Cdd:COG0065 217 IEAGAKAGIIAPDETTFEYLK--GRPFAPWRTLKS---------D---EDAVYDKEVEIDASDLE--------PQ----- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 388 sdmkssfensVTAPaGNQGHGLDKSEFdkkaeinfkdgskatmktGDIAI--AAITSCTNtsnpyvmlgaG----LVAKK 461
Cdd:COG0065 270 ----------VAWP-HSPDNVVPVSEL------------------EGIKIdqVFIGSCTN----------GriedLRAAA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 462 AVEKGLKVPEYVKTSLAPGSKVVTGYLRDAGLQPYLDELGFNLVGYGCTTCIG-NSGPLLPEiEKAIAdedllvTSvlsg 540
Cdd:COG0065 311 EILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAPG-ERCAS------TS---- 379
|
490 500 510
....*....|....*....|....*....|...
gi 612907865 541 NRNFEGRI-HPLVKAnYLASPQLVVAYALAGTV 572
Cdd:COG0065 380 NRNFEGRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
698-828 |
7.73e-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: 160.61 E-value: 7.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 698 AGKYLQDHQVPIREFNSYGSRRGNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTNEVMPIFDAAMKYKEDGTGLVVLA 777
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 612907865 778 GNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEFKKG 828
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
85-572 |
1.68e-43 |
|
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: 162.36 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 85 RVILQDFTGVPAVvdlASLRKAMDDVGGDITKINpevpvdLVIDHSVQVDSyanPEALERNMKLEfeRNYERyqflnWAT 164
Cdd:cd01583 1 LHLVHDVTSPQAF---EGLREAGREKVWDPEKIV------AVFDHNVPTPD---IKAAEQVKTLR--KFAKE-----FGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 165 KAFDNYNavppaTGIVHQVnleyLASVVHVRdvdgektafP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSY 243
Cdd:cd01583 62 NFFDVGR-----QGICHVI----LPEKGLTL---------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLW 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 244 FPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDES 323
Cdd:cd01583 124 FRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 324 LKYMKLTGRSDEhialvkEYLKQNhmffdvekEDPNYTDVIELDLSTVEASLSGPKRPQDLIFLSDmkssfensvtapag 403
Cdd:cd01583 204 FEYLKGRGKAYW------KELKSD--------EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSE-------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 404 NQGHGLDksefdkKAEInfkdGSKATMKTGDIAIAAitsctntsnpyvmlgaglvakkAVEKGLKVPEYVKTSLAPGSKV 483
Cdd:cd01583 256 VEGIKID------QVFI----GSCTNGRLEDLRAAA----------------------EILKGRKVADGVRLIVVPASQR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 484 VTGYLRDAGLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIAdedllvTSvlsgNRNFEGRIHPLVKANYLASPQLV 563
Cdd:cd01583 304 VYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS------TS----NRNFKGRMGSPGARIYLASPATA 373
|
....*....
gi 612907865 564 VAYALAGTV 572
Cdd:cd01583 374 AASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
71-570 |
4.10e-38 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 147.63 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 71 GKDGNEGE-VPFKPSRVILQDFTGVPAVvdlaslrKAMDDVGGDitKI-NPEvPVDLVIDHSVQvdsyANPEALERNMKL 148
Cdd:PRK00402 15 GRDVSPGDiVEAKVDLVMAHDITGPLAI-------KEFEKIGGD--KVfDPS-KIVIVFDHFVP----AKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 149 --EFERnyeRYQFLNWatkaFDNYNavppatGIVHQVNLEYlasvVHVRdvdgektafP-DTLVGTDSHTTMINGIGVLG 225
Cdd:PRK00402 81 lrEFAK---EQGIPNF----FDVGE------GICHQVLPEK----GLVR---------PgDVVVGADSHTCTYGALGAFA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 226 WGVGGIEAEAGM-LGQpSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIA 304
Cdd:PRK00402 135 TGMGSTDMAAAMaTGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 305 NMAPEYGATCGFFPVDDESLKYMKltGRSDEHIALVKEYlkqnhmffdvekEDPNYTDVIELDLSTVEaslsgpkrPQdl 384
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLK--ERAGRDYKPWKSD------------EDAEYEEVYEIDLSKLE--------PQ-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 385 iflsdmkssfensVTAPagnqgHGLDksefdkkaeiNFKDGSKAtmktGDIAI--AAITSCTNtsnpyvmlgaG----LV 458
Cdd:PRK00402 270 -------------VAAP-----HLPD----------NVKPVSEV----EGTKVdqVFIGSCTN----------GrledLR 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 459 AKKAVEKGLKVPEYVKTSLAPGSKVVtgYLR--DAGLQPYLDELGFnLVGY-GCTTCIGNSGPLLPEIEKAIAdedllvT 535
Cdd:PRK00402 308 IAAEILKGRKVAPGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHMGVLAPGEVCLS------T 378
|
490 500 510
....*....|....*....|....*....|....*..
gi 612907865 536 SvlsgNRNFEGRI-HPlvKAN-YLASPQLVVAYALAG 570
Cdd:PRK00402 379 T----NRNFKGRMgSP--ESEvYLASPAVAAASAVTG 409
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
86-572 |
1.07e-33 |
|
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: 134.50 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 86 VILQDFTGVPAVvdlaslrKAMDDVGGDITKiNPEvPVDLVIDHSVQVDSYANPEAlernmklefernyerYQFLNWATK 165
Cdd:TIGR01343 28 AMVHDITAPLAI-------KTLEEYGIDKVW-NPE-KIVIVFDHQVPADTIKAAEM---------------QKLAREFVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 166 AFDNYNAVPPATGIVHQVNLEylasvvhvrdvdgEKTAFP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYF 244
Cdd:TIGR01343 84 KQGIKYFYDVGEGICHQVLPE-------------KGLVKPgDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 245 PIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESL 324
Cdd:TIGR01343 151 KVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 325 KYMKLTGRSDEhialvKEYlkqnhmffdVEKEDPNYTDVIELDLSTVEASLSGPKRPQdliflsdmkssfensvtapagn 404
Cdd:TIGR01343 231 QYLKERRKEPF-----RVY---------KSDEDAEYAKEIEIDASQIEPVVACPHNVD---------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 405 qghgldksefdkkaeiNFKDGSKATMKTgdIAIAAITSCTNtsnpyvmlG--AGLVAKKAVEKGLKVPEYVKTSLAPGSK 482
Cdd:TIGR01343 275 ----------------NVKPVSEVEGTE--IDQVFIGSCTN--------GrlEDLRVAAKILKGRKVAPDVRLIVIPASR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 483 VVTGYLRDAGLQPYLDELGFNLVGYGCTTCIG-NSGPLLPeiekaiaDEDLLVTSvlsgNRNFEGRIHPLVKANYLASPQ 561
Cdd:TIGR01343 329 AVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGsHQGVLAP-------GEVCISTS----NRNFKGRMGHPNAEIYLASPA 397
|
490
....*....|.
gi 612907865 562 LVVAYALAGTV 572
Cdd:TIGR01343 398 TAAASAVKGYI 408
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
115-572 |
8.83e-30 |
|
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: 121.95 E-value: 8.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 115 TKINPEVPVDLVIDHSVQVDSYANpeaLERNMKLEfernyeryqflNWATK-AFDNYnavPPATGIVHQVNLEylasvvh 193
Cdd:cd01582 21 TKIHNPDQIVMTLDHDVQNKSEKN---LKKYKNIE-----------SFAKKhGIDFY---PAGRGIGHQIMIE------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 194 vrdvdgEKTAFPDTL-VGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLVNSLPQGATATDLALRVT 272
Cdd:cd01582 77 ------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 273 QELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKymkltgrsdehialvkeylkqnhmffd 352
Cdd:cd01582 151 GLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLI--------------------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 353 vekedpnytdvieLDLSTVEASLSGPkrpqdliflsdmkssfeNSVTAPAgnqghgldksefdkkaeinfkdgSKATMKT 432
Cdd:cd01582 204 -------------LDLSTLSPYVSGP-----------------NSVKVST-----------------------PLKELEA 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 433 GDIAI--AAITSCTNTSNPYVMLGAGLV-AKKAVEKGLKVPEYVKTSLAPGSKVVTGYLRDAGLQPYLDELGFNLVGYGC 509
Cdd:cd01582 231 QNIKInkAYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGC 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612907865 510 TTCIGNSGPLLPEIEKAIAdedllvtsvlSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTV 572
Cdd:cd01582 311 GPCIGLGQGLLEPGEVGIS----------ATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
85-570 |
1.21e-26 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 114.62 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 85 RVILQDFTGVPAvvdLASLRKAMDDVggditkINPEVPVdLVIDHSVQVDSYAN---PEALERNMKLEFERNYERYqfln 161
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTV------RRPDLTL-AVVDHVVPTRPGRDrgiTDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 162 wATKAFDNYNavpPATGIVHQVNLEYLAsvvhvrdvdgektAFPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQ 240
Cdd:PRK12466 96 -GIRLFDVDD---PRQGIVHVVAPELGL-------------TLPGmVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 241 PSYFPIPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVGKFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVD 320
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 321 DESLKYmkLTGR----SDEHIALVKEYLKQNH----MFFDVEkedpnytdvIELDLSTVEASLSGPKRPQDLIFLSDmks 392
Cdd:PRK12466 239 ETTFDY--LRGRprapKGALWDAALAYWRTLRsdadAVFDRE---------VEIDAADIAPQVTWGTSPDQAVPITG--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 393 sfenSVTAPAGNQGHGLDKSEFDKKAEInfkdGSKATMKTGDIAI--AAITSCTNtsnpyvmlgaG----LVAKKAVEKG 466
Cdd:PRK12466 305 ----RVPDPAAEADPARRAAMERALDYM----GLTPGTPLAGIPIdrVFIGSCTN----------GriedLRAAAAVLRG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 467 LKVPEYVKTSLAPGSKVVTgylRDA---GLQPYLDELGFNLVGYGCTTCIGNSGPLLPEIEKAIAdedllvtsvlSGNRN 543
Cdd:PRK12466 367 RKVAPGVRAMVVPGSGAVR---RQAeaeGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCAS----------TTNRN 433
|
490 500
....*....|....*....|....*..
gi 612907865 544 FEGRIHPLVKAnYLASPQLVVAYALAG 570
Cdd:PRK12466 434 FEGRQGPGART-HLMSPAMVAAAAVAG 459
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
676-838 |
1.80e-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: 84.80 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 676 KFGDSVTTDHISPAGAigkdtpagKYLqdhqvPIREfnsygsrrgNHEVMVRGTFaniriknqlapgteggfttywptNE 755
Cdd:cd01579 1 KVGDNITTDHIMPAGA--------KVL-----PLRS---------NIPAISEFVF-----------------------HR 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 756 VMPIFdaAMKYKEDGTGLVVlAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEFK------KGE 829
Cdd:cd01579 36 VDPTF--AERAKAAGPGFIV-GGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFAdeddydRFE 112
|
....*....
gi 612907865 830 SADSLGLDG 838
Cdd:cd01579 113 QGDQLELPL 121
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
770-844 |
5.37e-18 |
|
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: 79.43 E-value: 5.37e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612907865 770 GTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEFKKGEsaDSLGLDGTEEISV 844
Cdd:cd00404 14 AGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE--DYLKLHTGDELDI 86
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
207-574 |
9.55e-17 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 84.02 E-value: 9.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 207 TLVGTDSHTTMINGIGVLGWGVGGIEAEAGM----LGQPSyfpiPEVIGVRLVNSLPQGATATDLALRVTQELRKKGVVG 282
Cdd:PRK05478 123 TIVCGDSHTSTHGAFGALAFGIGTSEVEHVLatqtLLQKK----PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 283 KFVEFFGPGVQHLPLADRATIANMAPEYGATCGFFPVDDESLKYMKltGR----SDEHIALVKEYLKQNHMffDvekEDP 358
Cdd:PRK05478 199 YVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK--GRpfapKGEDWDKAVAYWKTLKS--D---EDA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 359 NYTDVIELDLSTVEASLSGPKRPQDLIflsdmksSFENSVTAPAGNQGHGLDKSefDKKA--EINFKDGSKATmktgDIA 436
Cdd:PRK05478 272 VFDKVVTLDAADIEPQVTWGTNPGQVI-------SIDGKVPDPEDFADPVKRAS--AERAlaYMGLKPGTPIT----DIK 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 437 I--AAITSCTNtsnpyvmlgaG----LVAKKAVEKGLKVPEYVKTSLAPGSKVVTGYLRDAGLQPYLDELGFNLVGYGCT 510
Cdd:PRK05478 339 IdkVFIGSCTN----------SriedLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCS 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612907865 511 TCIGNSGPLLPEIEKAIAdedllvTSvlsgNRNFEGR------IHplvkanyLASPQLVVAYALAGT-VDI 574
Cdd:PRK05478 409 MCLAMNPDKLPPGERCAS------TS----NRNFEGRqgkggrTH-------LVSPAMAAAAAITGHfVDV 462
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
682-843 |
2.18e-14 |
|
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: 71.35 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 682 TTDHISPAGaigkdtPAGKYlqdhqvpirefnsygsrrgnhevmvRGTFANI-----------------RIKNQLapgte 744
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIsnnlligainaengkanSVKNQV----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 745 ggfttywpTNEVMPIFDAAMKYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLE 824
Cdd:cd01578 51 --------TGEYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLT 122
|
170 180
....*....|....*....|....*
gi 612907865 825 FK------KGESADSLGLDGTEEIS 843
Cdd:cd01578 123 FAdpadydKIHPDDKVDILGLTDFA 147
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
173-381 |
5.95e-12 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 69.65 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 173 VPPATGIVHQVNLEYLASvvhvrdvdGEKTafpdtLVGTDSHTTMiNGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGV 252
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAG--------GGKM-----ILGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 253 RLVNSLPQGATATDLALRVTQELRKKGVV-GKFVEFFGPGVQHLPLADRATIANMAPEygATC--GFFPVDDESLKYMKL 329
Cdd:PRK11413 189 YLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQTDEEVHNWLAL 266
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 612907865 330 TGRSDEHIALvkeylkqnhmffdvEKEDPNYTD-VIELDLSTVEASLSGPKRP 381
Cdd:PRK11413 267 HGRGQDYCEL--------------NPQPMAYYDgCISVDLSAIKPMIALPFHP 305
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
676-850 |
1.36e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 60.97 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 676 KFGDSVTTDHISPagaigkdtpaGKYlQDHQVPIREFNSYgsrrgnhevmvrgTFANIRiknqlapgteggfttywptne 755
Cdd:PRK14023 6 KFGDNINTDDILP----------GKY-APFMVGEDRFHNY-------------AFAHLR--------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 756 vmPIFdaAMKYKedgTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPleFKKGESADSLG 835
Cdd:PRK14023 41 --PEF--ASTVR---PGDILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALE 111
|
170
....*....|....*
gi 612907865 836 lDGtEEISVNIDENV 850
Cdd:PRK14023 112 -DG-DEVELDLETGV 124
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
774-845 |
1.73e-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: 58.37 E-value: 1.73e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612907865 774 VVLAGNDYGMGSSR---DWAAKGtnlLGVKTVIAQSYERIHRSNLVMMGVLPLEFKKGESADSLGLDGtEEISVN 845
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPG-DEVEVD 90
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
676-897 |
7.66e-09 |
|
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: 55.51 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 676 KFGDSVTTDHISPagaigkdtpaGKYLqdhqvpirefnsygsRRGNHEVMVRGTFANIRiknqlapgteggfttywptne 755
Cdd:TIGR02087 5 KFGDDIDTDEIIP----------GRYL---------------RTTDPDELASHAMEGID--------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 756 vmPIFdaamkYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEfkkgesADSLG 835
Cdd:TIGR02087 39 --PEF-----AKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEG 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612907865 836 LDGTEEISVNIDENVqphdyVKVTAKKqdgdlvefdaMVRFDSLVEM--DYYRHGGILQMVLRN 897
Cdd:TIGR02087 106 IKDGDEVTVDLETGE-----IRVNGNE----------EYKGEPLPDFllEILREGGLLEYLKKR 154
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
774-848 |
1.43e-08 |
|
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: 55.56 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 774 VVLAGNDYGMGSSRD---WAAKGtnlLGVKTVIAQSYERIHRSNLVMMGVLPLEFKKGESA---DSLGLDGTEEISVNID 847
Cdd:COG0066 67 ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDalfAAIEANPGDELTVDLE 143
|
.
gi 612907865 848 E 848
Cdd:COG0066 144 A 144
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
676-847 |
3.96e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 53.68 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 676 KFGDSVTTDHISPagaigkdtpaGKYLqdhqvpirefnsygsRRGNHEVMVRGTFANIRiknqlapgteggfttywptne 755
Cdd:PRK00439 6 KFGDNIDTDVIIP----------ARYL---------------NTSDPQELAKHCMEDLD--------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 756 vmPIFdaamkYKEDGTGLVVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLEFKkgESADSLG 835
Cdd:PRK00439 40 --PEF-----AKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECD--EAVDKIE 110
|
170
....*....|..
gi 612907865 836 lDGtEEISVNID 847
Cdd:PRK00439 111 -DG-DEVEVDLE 120
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
774-824 |
1.32e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 44.46 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 612907865 774 VVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMG-VLPLE 824
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
183-288 |
2.99e-04 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 42.24 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612907865 183 VNLEYLASVVHVRDVDGEKTAFPDTlvgtdsHTTMINGIGVLGWgvggieaeagmlgQPSyfPIPEvigvrlvnslPQGA 262
Cdd:pfam02222 71 VPFDRELSVLVVRSVDGETAFYPVV------ETIQEDGICRLSV-------------APA--RVPQ----------AIQA 119
|
90 100
....*....|....*....|....*..
gi 612907865 263 TATDLALRVTQELrkkGVVGKF-VEFF 288
Cdd:pfam02222 120 EAQDIAKRLVDEL---GGVGVFgVELF 143
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
774-822 |
5.09e-03 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 39.34 E-value: 5.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 612907865 774 VVLAGNDYGMGSSRD---WAakgtnLL--GVKTVIAQSYERIHRSNLVMMGVLP 822
Cdd:PRK01641 70 ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| |
