|
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: 1773.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 1 MTSNIKQQAKKTFEANGQSYTYYDLKSLEEQGLTKISKLPYSIRVLLESVLRQEDEFVITDEHIKALGNFGNEG-NEGEV 79
Cdd:PRK09277 1 MSSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAkPDREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 80 PFKPSRVILQDFTGVPAVVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQF 159
Cdd:PRK09277 81 PFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 160 LNWATKAFDNYNAVPPATGIVHQVNLEYLANVVHVRDvDGEQTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLG 239
Cdd:PRK09277 161 LKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTRE-DGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 240 QPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPV 319
Cdd:PRK09277 240 QPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 320 DEESLKYMRLTGRKEEHVELVKAYLEQNNMFFTvDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKSVt 399
Cdd:PRK09277 320 DEETLDYLRLTGRDEEQVALVEAYAKAQGLWRD-PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSA- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 400 tPAGNQGHGLDKSEFdkkaninfadGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAP 479
Cdd:PRK09277 398 -ELGVQGFGLDEAEE----------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 480 GSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLAS 559
Cdd:PRK09277 467 GSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLAS 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 560 PQLVVAYALAGTVDIDLQNEPIGKGKDGQNVYLNDIWPTIQEVADTVDSVVTPELFLEEYKNVYNNNEMWNEIDVTDAPL 639
Cdd:PRK09277 547 PPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPL 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 640 YDFDPNSTYIQNPSFFQGLSKEPGTIEPLKDLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRR 719
Cdd:PRK09277 627 YDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRR 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 720 GNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGV 799
Cdd:PRK09277 707 GNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGV 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 800 KTVIAQSYERIHRSNLVMMGVLPLQFKDGESAESLGLDGKEAISVDIDETVSPRDTVKVHAKKENGEVVDFEAIVRFDSL 879
Cdd:PRK09277 787 KAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFPVLCRIDTA 866
|
890 900
....*....|....*....|..
gi 1081394525 880 VELDYYRHGGILQMVLRNKLAQ 901
Cdd:PRK09277 867 VEVDYYRNGGILQYVLRDLLAS 888
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-901 |
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: 1699.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 3 SNIKQQAKKTFEANGQSYTYYDLKSLEEQGlTKISKLPYSIRVLLESVLRQEDEFVITDEHIKALGNFGNEG-NEGEVPF 81
Cdd:COG1048 1 SMDSFKARKTLTVGGKPYTYYSLPALEEAG-GDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKArGDDEIPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 82 KPSRVILQDFTGVPAVVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQFLN 161
Cdd:COG1048 80 RPARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 162 WATKAFDNYNAVPPATGIVHQVNLEYLANVVHVRDVDGEQTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQP 241
Cdd:COG1048 160 WGQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 242 SYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDE 321
Cdd:COG1048 240 VSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 322 ESLKYMRLTGRKEEHVELVKAYLEQNNMFFTVDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKSVTTP 401
Cdd:COG1048 320 ETLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 402 AGNQGHGLDKSEfdkkaninfADGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAPGS 481
Cdd:COG1048 400 VGEELDKPVRVE---------VDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 482 KVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLASPQ 561
Cdd:COG1048 471 KVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPP 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 562 LVVAYALAGTVDIDLQNEPIGKGKDGQNVYLNDIWPTIQEVADTVDSVVTPELFLEEYKNVYNNNEMWNEIDVTDAPLYD 641
Cdd:COG1048 551 LVVAYALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYD 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 642 FDPNSTYIQNPSFFQGLSKEPGTIEPLKDLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRRGN 721
Cdd:COG1048 631 WDPDSTYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGN 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 722 HEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGVKT 801
Cdd:COG1048 711 HEVMMRGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 802 VIAQSYERIHRSNLVMMGVLPLQFKDGESAESLGLDGKEAISV-DIDETVSPRDTVKVHAKKENGEVVDFEAIVRFDSLV 880
Cdd:COG1048 791 VIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIeGLDEGLAPGKTVTVTATRADGSTEEFPVLHRIDTPV 870
|
890 900
....*....|....*....|.
gi 1081394525 881 ELDYYRHGGILQMVLRNKLAQ 901
Cdd:COG1048 871 EVEYYRAGGILQYVLRQLLAA 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: 1448.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 18 QSYTYYDLKSLEEQGlTKISKLPYSIRVLLESVLRQEDEFVITDEHIKALGNFG-NEGNEGEVPFKPSRVILQDFTGVPA 96
Cdd:TIGR01341 1 KTYYYYSLKALEESG-GKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKiGEVADTEIAFKPARVVMQDFTGVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 97 VVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQFLNWATKAFDNYNAVPPA 176
Cdd:TIGR01341 80 VVDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 177 TGIVHQVNLEYLANVVHVRDVDGEQTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLTN 256
Cdd:TIGR01341 160 TGIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 257 SLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEESLKYMRLTGRKEEH 336
Cdd:TIGR01341 240 KLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 337 VELVKAYLEQNNMFFTvDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKSVTTPAGNQGHGLDKSEFDK 416
Cdd:TIGR01341 320 VELVEKYARAQGLFYD-DSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 417 KANinfadGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAPGSKVVTGYLRDSGLQEY 496
Cdd:TIGR01341 399 KVN-----GQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 497 LDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTVDIDL 576
Cdd:TIGR01341 474 LEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 577 QNEPIGKGKDGQNVYLNDIWPTIQEVADTVDSVVTPELFLEEYKNVYNNNEMWNEIDVTDAPLYDFDPNSTYIQNPSFFQ 656
Cdd:TIGR01341 554 YTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 657 GLSKEPGTIEPLKDLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRRGNHEVMVRGTFANIRIK 736
Cdd:TIGR01341 634 EMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 737 NQLAPGTEGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLV 816
Cdd:TIGR01341 714 NLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLV 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 817 MMGVLPLQFKDGESAESLGLDGKEAISVDIDETVSPRDTVKVHAKKENGEVVDFEAIVRFDSLVELDYYRHGGILQMVLR 896
Cdd:TIGR01341 794 GMGVIPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLR 873
|
...
gi 1081394525 897 NKL 899
Cdd:TIGR01341 874 KFL 876
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-900 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1418.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 1 MTSNIKQqAKKTFEANGQSYTYYDLKSLEEQGLTKISKLPYSIRVLLESVLRQEDEFVITDEHIKALGNFGNEG-NEGEV 79
Cdd:PRK12881 1 MAHNLHK-TLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERkSDDEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 80 PFKPSRVILQDFTGVPAVVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQF 159
Cdd:PRK12881 80 PFVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 160 LNWATKAFDNYNAVPPATGIVHQVNLEYLANVVHVRDVDGEQTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLG 239
Cdd:PRK12881 160 LKWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 240 QPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPV 319
Cdd:PRK12881 240 QPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 320 DEESLKYMRLTGRKEEHVELVKAYLEQNNMFFtVDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKSVT 399
Cdd:PRK12881 320 DEQTLDYLRLTGRTEAQIALVEAYAKAQGLWG-DPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 400 TPAGNQGhgldkseFDKKAninfADGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAP 479
Cdd:PRK12881 399 KPVAENG-------FAKKA----QTSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 480 GSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLAS 559
Cdd:PRK12881 468 GSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLAS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 560 PQLVVAYALAGTVDIDLQNEPIGKGKDGQNVYLNDIWPTIQEVADTVDSVVTPELFLEEYKNVYNNNEMWNEIDVTDAPL 639
Cdd:PRK12881 548 PPLVVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 640 YDFDPNSTYIQNPSFFQGLSKEPGTIEPLKDLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRR 719
Cdd:PRK12881 628 YDWDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRR 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 720 GNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGV 799
Cdd:PRK12881 708 GNHEVMMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 800 KTVIAQSYERIHRSNLVMMGVLPLQFKDGESAESLGLDGKEAISVD-IDETVSPRDTVKVHAKKENGEVVDFEAIVRFDS 878
Cdd:PRK12881 788 KAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRQDVTLVIHRADGSTERVPVLCRIDT 867
|
890 900
....*....|....*....|..
gi 1081394525 879 LVELDYYRHGGILQMVLRNKLA 900
Cdd:PRK12881 868 PIEVDYYKAGGILPYVLRQLLA 889
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
1-901 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1362.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 1 MTSNIKQQAKKTFeANGQSYTYYDLKSLEEqglTKISKLPYSIRVLLESVLRQEDEFVITDEHIKALGNFGNEGNEG-EV 79
Cdd:PTZ00092 11 SRPNPFEKVLKTL-KDGGSYKYYSLNELHD---PRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQiEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 80 PFKPSRVILQDFTGVPAVVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQF 159
Cdd:PTZ00092 87 PFKPARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 160 LNWATKAFDNYNAVPPATGIVHQVNLEYLANVVhvrdVDGEQTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLG 239
Cdd:PTZ00092 167 LKWGSKAFKNLLIVPPGSGIVHQVNLEYLARVV----FNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 240 QPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPV 319
Cdd:PTZ00092 243 QPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 320 DEESLKYMRLTGRKEEHVELVKAYLEQNNMFFTvDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKSVT 399
Cdd:PTZ00092 323 DEKTLDYLKQTGRSEEKVELIEKYLKANGLFRT-YAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 400 TPAGNQGHGLDKSEFDKKANINFaDGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAP 479
Cdd:PTZ00092 402 APVGFKGFGIPEEKHEKKVKFTY-KGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 480 GSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLAS 559
Cdd:PTZ00092 481 GSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLAS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 560 PQLVVAYALAGTVDIDLQNEPIGKGKDGQNVYLNDIWPTIQEVADTVDSVVTPELFLEEYKNVYNNNEMWNEIDVTDAPL 639
Cdd:PTZ00092 561 PPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 640 YDFDPNSTYIQNPSFFQGLSKEPGTIEPLKDLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRR 719
Cdd:PTZ00092 641 YEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 720 GNHEVMVRGTFANIRIKNQLAPGTeGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGV 799
Cdd:PTZ00092 721 GNDEVMVRGTFANIRLINKLCGKV-GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGV 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 800 KTVIAQSYERIHRSNLVMMGVLPLQFKDGESAESLGLDGKEAISVDIDET-VSPRDTVKVhaKKENGEvvDFEAIVRFDS 878
Cdd:PTZ00092 800 KAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGeLKPGQDVTV--KTDTGK--TFDTILRIDT 875
|
890 900
....*....|....*....|...
gi 1081394525 879 LVELDYYRHGGILQMVLRNKLAQ 901
Cdd:PTZ00092 876 EVEVEYFKHGGILQYVLRKLVKG 898
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
22-901 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1174.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 22 YYDLKSLEEqglTKISKLPYSIRVLLESVLRQEDEFVITDEHIKALGNFGNEG-NEGEVPFKPSRVILQDFTGVPAVVDL 100
Cdd:PLN00070 63 YYSLPALND---PRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSpKQVEIPFKPARVLLQDFTGVPAVVDL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 101 ASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQFLNWATKAFDNYNAVPPATGIV 180
Cdd:PLN00070 140 ACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 181 HQVNLEYLANVVHvrDVDGeqTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLTNSLPQ 260
Cdd:PLN00070 220 HQVNLEYLGRVVF--NTDG--ILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 261 GSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEESLKYMRLTGRKEEHVELV 340
Cdd:PLN00070 296 GVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 341 KAYLEQNNMFftVDKEDPE----YTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKSVTTPAGNQGHGLDKSEFDK 416
Cdd:PLN00070 376 EAYLRANKMF--VDYNEPQqervYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 417 KANINFaDGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAPGSKVVTGYLRDSGLQEY 496
Cdd:PLN00070 454 VAKFSF-HGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKY 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 497 LDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTVDIDL 576
Cdd:PLN00070 533 LNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDF 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 577 QNEPIGKGKDGQNVYLNDIWPTIQEVADTVDSVVTPELFLEEYKNVYNNNEMWNEIDVTDAPLYDFDPNSTYIQNPSFFQ 656
Cdd:PLN00070 613 EKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFK 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 657 GLSKEPGTIEPLKDLRVMGKFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRRGNHEVMVRGTFANIRIK 736
Cdd:PLN00070 693 NMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIV 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 737 NQLAPGTEGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLV 816
Cdd:PLN00070 773 NKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLV 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 817 MMGVLPLQFKDGESAESLGLDGKEAISVDIDETVSP-RDTVKVHAKKENGEvvDFEAIVRFDSLVELDYYRHGGILQMVL 895
Cdd:PLN00070 853 GMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNISEiKPGQDVTVTTDNGK--SFTCTLRFDTEVELAYFDHGGILPYVI 930
|
....*.
gi 1081394525 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: 763.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 85 RVILQDFTGVPAVVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSVQVDSYANPDALERNMKLEFERNYERYQFLNWAT 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 165 KAFDNYNAVPPATGIVHQVNLEYLANVVHVRDVDGEQTAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYF 244
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 245 PIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDeesl 324
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 325 kymrltgrkeehvelvkayleqnnmfftvdkedpeyTDVIDLDLSTVEASLSGPKRPQDLIFLsdmkkefeksvttpagn 404
Cdd:cd01586 237 ------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 405 qghgldksefdkkaninfadgstatmkTGDIAIAAITSCTNTSNPYVMLGAGLVAKKAVEKGLKVPEFVKTSLAPGSKVV 484
Cdd:cd01586 264 ---------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 485 TGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSVLSGNRNFEGRIHPLVKANYLASPQLVV 564
Cdd:cd01586 317 TKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVV 396
|
....*...
gi 1081394525 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: 654.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 73 EGNEGEVPFKPSRVILQDFTGVPAVVDLASLRKAMNDVGGDINKINPEVPVDLVIDHSvqvdsyanPDALERNMKLEFER 152
Cdd:pfam00330 10 EELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 153 NYERYQFLNWATKAFdNYNAVPPATGIVHQVNLEYLanvvhvrdvdgeqTAFPD-TLVGTDSHTTMINGIGVLGWGVGGI 231
Cdd:pfam00330 82 NKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGGLGALAFGVGGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 232 EAEAGMLGQPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYG 311
Cdd:pfam00330 148 EAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 312 ATCGFFPVDEESLKYMRLTGRKEEHVelVKAYLEQNNMFFTVDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMK 391
Cdd:pfam00330 228 ATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 392 KE-FEKSVTTPAGnqghgldksefdKKANINFADGSTATMKTGDIAIAAITSCTNTSNPYVMLGAGLVaKKAVEKGLKVP 470
Cdd:pfam00330 306 PDpFADAVKRKAA------------ERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 471 EFVKTSLAPGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLlpeiekavAEKDllvTSVLSGNRNFEGRIHP 550
Cdd:pfam00330 373 PGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRL--------PPGE---RCVSSSNRNFEGRQGP 441
|
490 500
....*....|....*....|
gi 1081394525 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, ... |
676-846 |
3.04e-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: 338.48 E-value: 3.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 676 KFGDSVTTDHISPAGAIGKDTPAGKYLLDHDVSIRNFNSYGSRRGNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTDE 755
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 756 VMPIYDAAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDGESAESLG 835
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|.
gi 1081394525 836 LDGKEAISVDI 846
Cdd:cd01580 161 LTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-572 |
9.49e-95 |
|
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: 303.65 E-value: 9.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 85 RVILQDFTGVPAVVDLASLRKAmndvggdiNKINPEVPVDLVIDHSVQvdsyanpdalernmkLEFERNYERYQFLNWAT 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAAL--------GKVADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 165 KAFDNYNaVPPATGIVHQVNLEYLAnvvhvrdvdgeqtAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYF 244
Cdd:cd01351 58 ALQGIAF-YRPGVGIIHQIMVENLA-------------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 245 PIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEESL 324
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 325 KYMRLTGRKEEHvELVKAYLEQNNmfftvDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEfeksvttpagn 404
Cdd:cd01351 204 KWLEATGRPLLK-NLWLAFPEELL-----ADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEGT----------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 405 qghgldksefdkkaninfadgstatmktgDIAIAAITSCTNtSNPYVMLGAGLVAKKAvekglKVPEFVKTSLAPGSKVV 484
Cdd:cd01351 267 -----------------------------KIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLIVTPGSRMV 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 485 TGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEkavaekdllvTSVLSGNRNFEGRIHPLVKANYLASPQLVV 564
Cdd:cd01351 312 YATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGE----------VGVSSGNRNFPGRLGTYERHVYLASPELAA 381
|
....*...
gi 1081394525 565 AYALAGTV 572
Cdd:cd01351 382 ATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
78-901 |
6.56e-90 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 298.98 E-value: 6.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 78 EVPFKPSRVILQDFTGVPAVVDLASLRKamndvggdinkinPEVPVDLvidhSVQ-VDsyanpdaleRNMKLEFERNYER 156
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMGL-------------DRVKTEL----SVQyVD---------HNLLQADFENADD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 157 YQFLNWATKafdNYNAV--PPATGIVHQVNLEylanvvhvrdvdgeQTAFP-DTLVGTDSHTTMINGIGVLGWGVGGIEA 233
Cdd:PRK07229 78 HRFLQSVAA---KYGIYfsKPGNGICHQVHLE--------------RFAFPgKTLLGSDSHTPTAGGLGMLAIGAGGLDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 234 EAGMLGQPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGAT 313
Cdd:PRK07229 141 ALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 314 CGFFPVDEESLKYMRLTGRKEEHVELVKayleqnnmfftvdKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKE 393
Cdd:PRK07229 221 TSIFPSDERTREFLKAQGREDDWVELLA-------------DPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 394 feksvttpagnqghgldksefdkkaninfadgstatmktgDIAIAAITSCTNTSnpYVMLGAglVAKKAveKGLKVPEFV 473
Cdd:PRK07229 288 ----------------------------------------KVDQVLIGSCTNSS--YEDLMR--AASIL--KGKKVHPKV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 474 KTSLAPGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGnsgpllpeIEKAVAEKDllvTSVLSGNRNFEGRI-HPLV 552
Cdd:PRK07229 322 SLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIG--------MGQAPATGN---VSLRTFNRNFPGRSgTKDA 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 553 KAnYLASPQLVVAYALAGTV----DIDLQNEPIGKGKDGQNVYLNDiwptiqevadtvDSVVTPElflEEYKNVynnnem 628
Cdd:PRK07229 391 QV-YLASPETAAASALTGVItdprTLALENGEYPKLEEPEGFAVDD------------AGIIAPA---EDGSDV------ 448
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 629 wnEIDVtdaplydfDPNstyiqnpsffqglSKEPGTIEPLKD---LRVMGKFGDSVTTDHISPAGAigkdtpagKYLldh 705
Cdd:PRK07229 449 --EVVR--------GPN-------------IKPLPLLEPLPDlleGKVLLKVGDNITTDHIMPAGA--------KWL--- 494
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 706 dvsirnfnSYgsrRGNHEVMVRGTFanIRIKNqlapgteggfttywptdevmpiyDAAMKYKEDGTGLaVLAGNDYGMGS 785
Cdd:PRK07229 495 --------PY---RSNIPNISEFVF--EGVDN-----------------------TFPERAKEQGGGI-VVGGENYGQGS 537
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 786 SRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDGESAESLGLDGKEAIsVDIDETVSPRD-TVKVHAKken 864
Cdd:PRK07229 538 SREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEGDVLEI-EDLREFLPGGPlTVVNVTK--- 613
|
810 820 830
....*....|....*....|....*....|....*...
gi 1081394525 865 gevvDFEAIVRFD-SLVELDYYRHGGILQMVlRNKLAQ 901
Cdd:PRK07229 614 ----DEEIEVRHTlSERQIEILLAGGALNLI-KKKLAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-571 |
7.47e-56 |
|
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: 198.82 E-value: 7.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 85 RVILQDFTGVPAVVDLASlrkamndvggdINKINPEVPVDLVIDHSVQVDSYAnpdalERNMKLEFERNYERYQFLNWAT 164
Cdd:cd01584 1 RVAMQDATAQMALLQFMS-----------SGLPKVAVPSTIHCDHLIEAQVGG-----EKDLKRAKDINKEVYDFLASAG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 165 KAFdNYNAVPPATGIVHQVNLEylanvvhvrdvdgeQTAFPDTL-VGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSY 243
Cdd:cd01584 65 AKY-GIGFWKPGSGIIHQIVLE--------------NYAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 244 FPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEES 323
Cdd:cd01584 130 LKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 324 LKYMRLTGRKEehvelVKAYLEQNNMFFTVDKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMKKEFEKsvttpag 403
Cdd:cd01584 210 KKYLKATGRAE-----IADLADEFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEK------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 404 nQGHGLdksefdkkaninfadgstatmktgDIAIAAITSCTNTSnpYV-MLGAGLVAKKAVEKGLKV-PEFVKTslaPGS 481
Cdd:cd01584 278 -NGWPL------------------------DLRVGLIGSCTNSS--YEdMGRAASIAKQALAHGLKCkSIFTIT---PGS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 482 KVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPllPEIEKavAEKDLLVTSVlsgNRNFEGR--IHPLVKAnYLAS 559
Cdd:cd01584 328 EQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDR--KDIKK--GEKNTIVTSY---NRNFTGRndANPATHA-FVAS 399
|
490
....*....|..
gi 1081394525 560 PQLVVAYALAGT 571
Cdd:cd01584 400 PEIVTAMAIAGT 411
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
152-572 |
2.05e-54 |
|
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: 193.82 E-value: 2.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 152 RNYERYQFLNWATKAFDNYNAvPPATGIVHQVNLEYLAnvvhvrdVDGEqtafpdTLVGTDSHTTMINGIGVLGWGVGGI 231
Cdd:cd01585 44 ENADDHRFLQTVAARYGIYFS-RPGNGICHQVHLERFA-------VPGK------TLLGSDSHTPTAGGLGMLAIGAGGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 232 EAEAGMLGQPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYG 311
Cdd:cd01585 110 DVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 312 ATCGFFPVDEESLKYMRLTGRKEEHVELVKayleqnnmfftvdKEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDMk 391
Cdd:cd01585 190 ATTSIFPSDERTREFLAAQGREDDWVELAA-------------DADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREV- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 392 kefeksvttpagnqghgldksefdkkaninfadgstATMKTGDIAIAaitSCTNTSNPYVMLGAGLVakkaveKGLKVPE 471
Cdd:cd01585 256 ------------------------------------AGIKVDQVAIG---SCTNSSYEDLMTVAAIL------KGRRVHP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 472 FVKTSLAPGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGnsgpllpeIEKAVAEKDLlvtSVLSGNRNFEGRIHPL 551
Cdd:cd01585 291 HVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIG--------MGQAPPTGGV---SVRTFNRNFEGRSGTK 359
|
410 420
....*....|....*....|.
gi 1081394525 552 VKANYLASPQLVVAYALAGTV 572
Cdd:cd01585 360 DDLVYLASPEVAAAAALTGVI 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
71-572 |
3.89e-49 |
|
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: 179.84 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 71 GNEGNEGEVPF-KPSRVILQDFTGVPAVvdlaslrKAMNDVGGDinKI-NPEVPVdLVIDHSVqvdsYANPDALERNMKl 148
Cdd:COG0065 15 GREVEPGEIVLlYIDLHLVHDVTSPQAF-------EGLREAGGR--KVwDPDRIV-AVFDHNV----PTKDPKSAEQVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 149 EFERNYERYQFlnwatKAFDNYNAvppatGIVHQVNLEylanvvhvrdvdgEQTAFP-DTLVGTDSHTTMINGIGVLGWG 227
Cdd:COG0065 80 TLREFAKEFGI-----TFFDVGDP-----GICHVVLPE-------------QGLVLPgMTIVGGDSHTCTHGAFGAFAFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 228 VGGIEAEAGMLGQPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMA 307
Cdd:COG0065 137 IGTTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 308 PEYGATCGFFPVDEESLKYMRltGRKEEHVELVKAyleqnnmfftvDkEDPEYTDVIDLDLSTVEaslsgpkrPQdlifl 387
Cdd:COG0065 217 IEAGAKAGIIAPDETTFEYLK--GRPFAPWRTLKS-----------D-EDAVYDKEVEIDASDLE--------PQ----- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 388 sdmkkefeksVTTPaGNQGHGLDKSEFdkkaninfadgstatmktGDIAI--AAITSCTNtsnpyvmlgaG----LVAKK 461
Cdd:COG0065 270 ----------VAWP-HSPDNVVPVSEL------------------EGIKIdqVFIGSCTN----------GriedLRAAA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 462 AVEKGLKVPEFVKTSLAPGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIG-NSGPLLPEiEKAVAekdllvTSvlsg 540
Cdd:COG0065 311 EILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAPG-ERCAS------TS---- 379
|
490 500 510
....*....|....*....|....*....|...
gi 1081394525 541 NRNFEGRI-HPLVKAnYLASPQLVVAYALAGTV 572
Cdd:COG0065 380 NRNFEGRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
85-572 |
5.27e-47 |
|
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: 172.76 E-value: 5.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 85 RVILQDFTGVPAVvdlASLRKAMNDVGGDINKINpevpvdLVIDHSVQvdsyaNPDALERNMKLEFERNYERyqflnWAT 164
Cdd:cd01583 1 LHLVHDVTSPQAF---EGLREAGREKVWDPEKIV------AVFDHNVP-----TPDIKAAEQVKTLRKFAKE-----FGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 165 KAFDNYNavppaTGIVHQVNLEylanvvhvrdvdgEQTAFP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSY 243
Cdd:cd01583 62 NFFDVGR-----QGICHVILPE-------------KGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLW 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 244 FPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEES 323
Cdd:cd01583 124 FRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 324 LKYMRltGRKEEHVELVKAyleqnnmfftvdKEDPEYTDVIDLDLSTVEASLSGPKRPqdliflsDMKKEFEKSVTTPag 403
Cdd:cd01583 204 FEYLK--GRGKAYWKELKS------------DEDAEYDKVVEIDASELEPQVAWPHSP-------DNVVPVSEVEGIK-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 404 nqghgLDksefdkKANInfadGSTATMKTGDIAIAAitsctntsnpyvmlgaglvakkAVEKGLKVPEFVKTSLAPGSKV 483
Cdd:cd01583 261 -----ID------QVFI----GSCTNGRLEDLRAAA----------------------EILKGRKVADGVRLIVVPASQR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 484 VTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAekdllvTSvlsgNRNFEGRIHPLVKANYLASPQLV 563
Cdd:cd01583 304 VYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS------TS----NRNFKGRMGSPGARIYLASPATA 373
|
....*....
gi 1081394525 564 VAYALAGTV 572
Cdd:cd01583 374 AASAITGEI 382
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
698-828 |
5.68e-45 |
|
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: 157.91 E-value: 5.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 698 AGKYLLDHDVSIRNFNSYGSRRGNHEVMVRGTFANIRIKNQLAPGTEGGFTTYWPTDEVMPIYDAAMKYKEDGTGLAVLA 777
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1081394525 778 GNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDG 828
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
82-570 |
1.39e-37 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 146.09 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 82 KPSRVILQDFTGVPAVvdlaslrKAMNDVGGDinKI-NPEvPVDLVIDHSVQvdsyANPDALERNMKL--EFERnyeRYQ 158
Cdd:PRK00402 27 KVDLVMAHDITGPLAI-------KEFEKIGGD--KVfDPS-KIVIVFDHFVP----AKDIKSAEQQKIlrEFAK---EQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 159 FLNWatkaFDNYNavppatGIVHQVnleyLANVVHVRdvdgeqtafP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAGM 237
Cdd:PRK00402 90 IPNF----FDVGE------GICHQV----LPEKGLVR---------PgDVVVGADSHTCTYGALGAFATGMGSTDMAAAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 238 -LGQpSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGF 316
Cdd:PRK00402 147 aTGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 317 FPVDEESLKYmrLTGRKEEHVELVKAYleqnnmfftvdkEDPEYTDVIDLDLSTVEaslsgpkrPQdliflsdmkkefek 396
Cdd:PRK00402 226 FAPDEKTLEY--LKERAGRDYKPWKSD------------EDAEYEEVYEIDLSKLE--------PQ-------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 397 sVTTPagnqgHGLDksefdkkaniNFADGSTAtmktGDIAI--AAITSCTNtsnpyvmlgaG----LVAKKAVEKGLKVP 470
Cdd:PRK00402 270 -VAAP-----HLPD----------NVKPVSEV----EGTKVdqVFIGSCTN----------GrledLRIAAEILKGRKVA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 471 EFVKTSLAPGSKVVtgYLR--DSGLQEYLDDLGFnLVGY-GCTTCIGNSGPLLPEIEKAVAekdllvTSvlsgNRNFEGR 547
Cdd:PRK00402 320 PGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHMGVLAPGEVCLS------TT----NRNFKGR 386
|
490 500
....*....|....*....|....*
gi 1081394525 548 I-HPlvKAN-YLASPQLVVAYALAG 570
Cdd:PRK00402 387 MgSP--ESEvYLASPAVAAASAVTG 409
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
86-572 |
2.22e-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: 133.73 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 86 VILQDFTGVPAVvdlaslrKAMNDVGGDINKiNPEvPVDLVIDHSVQVDsyanpdalerNMKLEfernyERYQFLNWATK 165
Cdd:TIGR01343 28 AMVHDITAPLAI-------KTLEEYGIDKVW-NPE-KIVIVFDHQVPAD----------TIKAA-----EMQKLAREFVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 166 AFDNYNAVPPATGIVHQVnleyLANVVHVRdvdgeqtafP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYF 244
Cdd:TIGR01343 84 KQGIKYFYDVGEGICHQV----LPEKGLVK---------PgDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 245 PIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEESL 324
Cdd:TIGR01343 151 KVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 325 KYMRLTGRKEEHVelvkayleqnnmffTVDKEDPEYTDVIDLDLSTVEASLSGPKRPQdliflsdmkkefeksvttpagn 404
Cdd:TIGR01343 231 QYLKERRKEPFRV--------------YKSDEDAEYAKEIEIDASQIEPVVACPHNVD---------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 405 qghgldksefdkkaNINFADGSTATmktgDIAIAAITSCTNtsnpyvmlG--AGLVAKKAVEKGLKVPEFVKTSLAPGSK 482
Cdd:TIGR01343 275 --------------NVKPVSEVEGT----EIDQVFIGSCTN--------GrlEDLRVAAKILKGRKVAPDVRLIVIPASR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 483 VVtgYLRdsGLQEYLDDLgfnLVGYGCTTCIGNSGPLLPEIEKAVAEKDLLVTSvlsGNRNFEGRIHPLVKANYLASPQL 562
Cdd:TIGR01343 329 AV--YLQ--ALKEGLIEI---FVKAGAVVSTPGCGPCLGSHQGVLAPGEVCIST---SNRNFKGRMGHPNAEIYLASPAT 398
|
490
....*....|
gi 1081394525 563 VVAYALAGTV 572
Cdd:TIGR01343 399 AAASAVKGYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
85-570 |
1.86e-32 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 131.95 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 85 RVILQDFTGVPAvvdLASLRKAMNDVggdinkINPEVPVdLVIDHSVQVDSYAN---PDALERNMKLEFERNYERYqfln 161
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTV------RRPDLTL-AVVDHVVPTRPGRDrgiTDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 162 wATKAFDNYNavpPATGIVHQVNLEYLAnvvhvrdvdgeqtAFPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAGMLGQ 240
Cdd:PRK12466 96 -GIRLFDVDD---PRQGIVHVVAPELGL-------------TLPGmVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 241 PSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVD 320
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 321 EESLKYMRltGR----KEEHVELVKAYLEQnnmfFTVDkEDPEYTDVIDLDLSTVEASLSGPKRPQDLIFLSDmkkefek 396
Cdd:PRK12466 239 ETTFDYLR--GRprapKGALWDAALAYWRT----LRSD-ADAVFDREVEIDAADIAPQVTWGTSPDQAVPITG------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 397 SVTTPAgnqghglDKSEFDKKANINFA---DGSTATMKTGDIAI--AAITSCTNtsnpyvmlgaG----LVAKKAVEKGL 467
Cdd:PRK12466 305 RVPDPA-------AEADPARRAAMERAldyMGLTPGTPLAGIPIdrVFIGSCTN----------GriedLRAAAAVLRGR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 468 KVPEFVKTSLAPGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAekdllvtsvlSGNRNFEGR 547
Cdd:PRK12466 368 KVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCAS----------TTNRNFEGR 437
|
490 500
....*....|....*....|...
gi 1081394525 548 IHPLVKAnYLASPQLVVAYALAG 570
Cdd:PRK12466 438 QGPGART-HLMSPAMVAAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
138-572 |
2.81e-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: 123.49 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 138 NPD----ALERNMKLEFERNYERY-QFLNWATK-AFDNYnavPPATGIVHQVNLEylanvvhvrdvdgEQTAFPDTL-VG 210
Cdd:cd01582 25 NPDqivmTLDHDVQNKSEKNLKKYkNIESFAKKhGIDFY---PAGRGIGHQIMIE-------------EGYAFPGTLaVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 211 TDSHTTMINGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGVRLTNSLPQGSTATDLALRVTQELRKKGVVGKFVEFFGP 290
Cdd:cd01582 89 SDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 291 GVTDLPLADRATIANMAPEYGATCGFFPVDEESLKymrltgrkeehvelvkayleqnnmfftvdkedpeytdvidLDLST 370
Cdd:cd01582 169 GLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLI----------------------------------------LDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 371 VEASLSGPKRPQdliflsdmkkefeksVTTPAgnqghgldksefdkkaninfadgstATMKTGDIAI--AAITSCTNTSN 448
Cdd:cd01582 209 LSPYVSGPNSVK---------------VSTPL-------------------------KELEAQNIKInkAYLVSCTNSRA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 449 PYVMLGAGLV-AKKAVEKGLKVPEFVKTSLAPGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAV 527
Cdd:cd01582 249 SDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGI 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1081394525 528 AekdllvtsvlSGNRNFEGRIHPLVKANYLASPQLVVAYALAGTV 572
Cdd:cd01582 329 S----------ATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
191-574 |
1.03e-18 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 90.18 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 191 VVHVrdVDGEQTAfpdTLVGT-----DSHTTMINGIGVLGWGVGGIEAEAGM----LGQPSyfpiPEVIGVRLTNSLPQG 261
Cdd:PRK05478 107 IVHV--VGPEQGL---TLPGMtivcgDSHTSTHGAFGALAFGIGTSEVEHVLatqtLLQKK----PKTMKIEVDGKLPPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 262 STATDLALRVTQELRKKGVVGKFVEFFGPGVTDLPLADRATIANMAPEYGATCGFFPVDEESLKYMRltGR----KEEHV 337
Cdd:PRK05478 178 VTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK--GRpfapKGEDW 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 338 ELVKAYLEQnnmFFTvDkEDPEYTDVIDLDLSTVEaslsgpkrPQdliflsdmkkefeksVT---TPAgnQGHGLD---- 410
Cdd:PRK05478 256 DKAVAYWKT---LKS-D-EDAVFDKVVTLDAADIE--------PQ---------------VTwgtNPG--QVISIDgkvp 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 411 --KSEFD--KKANINFA---DGSTATMKTGDIAI--AAITSCTNtsnpyvmlgaG----LVAKKAVEKGLKVPEFVKTSL 477
Cdd:PRK05478 306 dpEDFADpvKRASAERAlayMGLKPGTPITDIKIdkVFIGSCTN----------SriedLRAAAAVVKGRKVAPGVRALV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 478 APGSKVVTGYLRDSGLQEYLDDLGFNLVGYGCTTCIGNSGPLLPEIEKAVAekdllvTSvlsgNRNFEGR------IHpl 551
Cdd:PRK05478 376 VPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPPGERCAS------TS----NRNFEGRqgkggrTH-- 443
|
410 420
....*....|....*....|....
gi 1081394525 552 vkanyLASPQLVVAYALAGT-VDI 574
Cdd:PRK05478 444 -----LVSPAMAAAAAITGHfVDV 462
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
676-829 |
1.09e-18 |
|
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: 82.49 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 676 KFGDSVTTDHISPAGAigkdtpagKYLldhdvsirnfnsygSRRGNHEVMVRGTFAniRIKNQLAPgteggfttywptde 755
Cdd:cd01579 1 KVGDNITTDHIMPAGA--------KVL--------------PLRSNIPAISEFVFH--RVDPTFAE-------------- 42
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081394525 756 vmpiydaamKYKEDGTGLAVlAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDGE 829
Cdd:cd01579 43 ---------RAKAAGPGFIV-GGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADED 106
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
753-845 |
1.46e-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: 78.28 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 753 TDEVMPiydaamkykedGTGLAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDGESAe 832
Cdd:cd00404 8 TDHISP-----------AGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDY- 75
|
90
....*....|...
gi 1081394525 833 sLGLDGKEAISVD 845
Cdd:cd00404 76 -LKLHTGDELDIY 87
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
682-827 |
4.08e-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: 70.58 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 682 TTDHISPAGaigkdtPAGKYLlDHDVSIRNFNSYGSrrgnheVMVRGTFANiRIKNQLapgteggfttywpTDEVMPIYD 761
Cdd:cd01578 7 TTDHISAAG------PWLKYR-GHLDNISNNLLIGA------INAENGKAN-SVKNQV-------------TGEYGPVPD 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081394525 762 AAMKYKEDGTGLAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQFKD 827
Cdd:cd01578 60 TARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAD 125
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
173-381 |
1.15e-12 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 71.96 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 173 VPPATGIVHQVNLEYLANVvhvrdvdGEQtafpdtLVGTDSHTTMiNGIGVLGWGVGGIEAEAGMLGQPSYFPIPEVIGV 252
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG-------GKM------ILGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 253 RLTNSLPQGSTATDLALRVTQELRKKGVV-GKFVEFFGPGVTDLPLADRATIANMAPEygATC--GFFPVDEESLKYMRL 329
Cdd:PRK11413 189 YLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQTDEEVHNWLAL 266
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081394525 330 TGRKEEHVELvkayleqnnmfftvDKEDPEYTD-VIDLDLSTVEASLSGPKRP 381
Cdd:PRK11413 267 HGRGQDYCEL--------------NPQPMAYYDgCISVDLSAIKPMIALPFHP 305
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
676-855 |
5.64e-11 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 62.13 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 676 KFGDSVTTDHISPagaiGKDTPagkYLLDHDvsirNFNSYgsrrgnhevmvrgTFANIRikNQLAPgteggftTYWPTDe 755
Cdd:PRK14023 6 KFGDNINTDDILP----GKYAP---FMVGED----RFHNY-------------AFAHLR--PEFAS-------TVRPGD- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 756 vmpiydaamkykedgtglAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPlqFKDGESAESLG 835
Cdd:PRK14023 52 ------------------ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALE 111
|
170 180
....*....|....*....|
gi 1081394525 836 lDGKEaISVDIDETVSPRDT 855
Cdd:PRK14023 112 -DGDE-VELDLETGVLTRGG 129
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
775-845 |
9.45e-11 |
|
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: 59.14 E-value: 9.45e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081394525 775 VLAGNDYGMGSSR---DWAAKGtnlLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDGESAESLGLDGKEaISVD 845
Cdd:cd01577 21 IVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE-VEVD 90
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
772-897 |
2.35e-08 |
|
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: 53.96 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 772 GLAVLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGVLPLQfkdgesAESLGLDGKEAISVDIDETVs 851
Cdd:TIGR02087 48 GDVIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEGIKDGDEVTVDLETGE- 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1081394525 852 prdtvkvhAKKENGEVVDFEAIVRFdslvELDYYRHGGILQMVLRN 897
Cdd:TIGR02087 121 --------IRVNGNEEYKGEPLPDF----LLEILREGGLLEYLKKR 154
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
775-861 |
1.01e-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: 53.25 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394525 775 VLAGNDYGMGSSRD---WAAKGtnlLGVKTVIAQSYERIHRSNLVMMGVLPLQFKDGESA---ESLGLDGKEAISVDIDE 848
Cdd:COG0066 68 LVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDalfAAIEANPGDELTVDLEA 144
|
90
....*....|....
gi 1081394525 849 -TVSPRDTVKVHAK 861
Cdd:COG0066 145 gTVTNGTGETYPFE 158
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
775-847 |
1.06e-06 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 49.44 E-value: 1.06e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081394525 775 VLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMGvLPLqFKDGESAESLGlDGKEaISVDID 847
Cdd:PRK00439 52 IVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV-LECDEAVDKIE-DGDE-VEVDLE 120
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
775-824 |
1.96e-03 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 41.00 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1081394525 775 VLAGNDYGMGSSRDWAAKGTNLLGVKTVIAQSYERIHRSNLVMMG-VLPLQ 824
Cdd:PLN00072 133 IIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
776-822 |
9.50e-03 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 38.18 E-value: 9.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1081394525 776 LAGNDYGMGSSRD---WAakgtnLL--GVKTVIAQSYERIHRSNLVMMGVLP 822
Cdd:PRK01641 72 LAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| |
