|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-890 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1835.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 1 MSLTLREASKDTLQAENKTWRYYSLP-LAARTLGDISRLPKSLKVLLENLLRWQDGDSVTEEDIQALAGWLKNAHADREI 79
Cdd:PRK09277 1 MSSTDSFKARKTLEVGGKSYDYYSLRaLEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 80 AYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVF 159
Cdd:PRK09277 81 PFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 160 LKWGQQAFSRFSVVPPGTGICHQVNLEYLGKAVWSElQDKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
Cdd:PRK09277 161 LKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTR-EDGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 240 QPVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPI 319
Cdd:PRK09277 240 QPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 320 DSVTLEYMRLSGRSEEQVALVEAYTKAQGMWRNPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAFAASNEL 399
Cdd:PRK09277 320 DEETLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 400 EVNAAQKDHRPVdyvlnGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSDY 479
Cdd:PRK09277 400 GVQGFGLDEAEE-----GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 480 LAQARLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYA 559
Cdd:PRK09277 475 LEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 560 LAGNMNINLATDPIGHDRKNEPVYLKDIWPSSREIARAVEK-VSTEMFRKEYAEVFEGTAEWKAIDVVGSDTYDWQDDST 638
Cdd:PRK09277 555 LAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKaVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDST 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 639 YIRLSPFFDEMLAEPAPLKDIHGARILAMLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMMR 718
Cdd:PRK09277 635 YIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMR 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 719 GTFANIRIRNEMVPGVEGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESF 798
Cdd:PRK09277 715 GTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESF 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 799 ERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEQIDISGLQNLQPGKTVPVKLTRADGTTEVLDCRCRIDTATELTYYQN 878
Cdd:PRK09277 795 ERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFPVLCRIDTAVEVDYYRN 874
|
890
....*....|..
gi 1738305823 879 DGILHYVIRKML 890
Cdd:PRK09277 875 GGILQYVLRDLL 886
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
8-890 |
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: 1754.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 8 ASKDTLQAENKTWRYYSLPLAARTLGDISRLPKSLKVLLENLLRWQDGDSVTEEDIQALAGWLKNAHADREIAYRPARVL 87
Cdd:COG1048 6 KARKTLTVGGKPYTYYSLPALEEAGGDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 88 MQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVFLKWGQQAF 167
Cdd:COG1048 86 MQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 168 SRFSVVPPGTGICHQVNLEYLGKAVWSELQDKEWVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPVSMLIP 247
Cdd:COG1048 166 DNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPVSMLIP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 248 DVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSVTLEYM 327
Cdd:COG1048 246 EVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 328 RLSGRSEEQVALVEAYTKAQGMWRNPGD-EPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAFAASneLEVNAAQK 406
Cdd:COG1048 326 RLTGRSEEQIELVEAYAKAQGLWRDPDApEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA--LAAPVGEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 407 DHRPVDYVLNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSDYLAQARLT 486
Cdd:COG1048 404 LDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 487 PYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNMNI 566
Cdd:COG1048 484 PYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDI 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 567 NLATDPIGHDRKNEPVYLKDIWPSSREIARAVEK-VSTEMFRKEYAEVFEGTAEWKAIDVVGSDTYDWQDDSTYIRLSPF 645
Cdd:COG1048 564 DLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKaVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPF 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 646 FDEMLAEPAPLKDIHGARILAMLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMMRGTFANIR 725
Cdd:COG1048 644 FEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIR 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 726 IRNEMVPGVEGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSN 805
Cdd:COG1048 724 IKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSN 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 806 LIGMGILPLEFPQGVTRKTLGLTGEEQIDISGL-QNLQPGKTVPVKLTRADGTTEVLDCRCRIDTATELTYYQNDGILHY 884
Cdd:COG1048 804 LVGMGVLPLQFPEGESAESLGLTGDETFDIEGLdEGLAPGKTVTVTATRADGSTEEFPVLHRIDTPVEVEYYRAGGILQY 883
|
....*.
gi 1738305823 885 VIRKML 890
Cdd:COG1048 884 VLRQLL 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
18-890 |
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: 1576.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 18 KTWRYYSLPLAARTLGDISRLPKSLKVLLENLLRWQDGDSVTEEDIQALAGWLKNAHADREIAYRPARVLMQDFTGVPAV 97
Cdd:TIGR01341 1 KTYYYYSLKALEESGGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 98 VDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVFLKWGQQAFSRFSVVPPGT 177
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 178 GICHQVNLEYLGKAVWSELQDKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPDVVGFKLTGK 257
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 258 LSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSVTLEYMRLSGRSEEQV 337
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 338 ALVEAYTKAQGMWRNPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAFAAsnELEVNAAQKD----HRPVDY 413
Cdd:TIGR01341 321 ELVEKYARAQGLFYDDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSK--ELEKNGGDKGftlrKEPLKK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 414 VLNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSDYLAQARLTPYLDELG 493
Cdd:TIGR01341 399 KVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 494 FNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNMNINLATDPI 573
Cdd:TIGR01341 479 FNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 574 GHDRKNEPVYLKDIWPSSREIARAVEK-VSTEMFRKEYAEVFEGTAEWKAIDVVGSDTYDWQDDSTYIRLSPFFDEMLAE 652
Cdd:TIGR01341 559 GTDKDGKPVYLRDIWPSNKEIAAYVNMaVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQD 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 653 PAPLKDIHGARILAMLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMMRGTFANIRIRNEMVP 732
Cdd:TIGR01341 639 PEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMVK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 733 GVEGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGIL 812
Cdd:TIGR01341 719 GKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGVI 798
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738305823 813 PLEFPQGVTRKTLGLTGEEQIDISGLQNLQPGKTVPVKLTRADGTTEVLDCRCRIDTATELTYYQNDGILHYVIRKML 890
Cdd:TIGR01341 799 PLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLRKFL 876
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-890 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1537.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 1 MSLTLREASKdTLQAENKTWRYYSLPLAARTLG-DISRLPKSLKVLLENLLRWQDGDSVTEEDIQALAGWLKNAHADREI 79
Cdd:PRK12881 1 MAHNLHKTLK-EFDVGGKTYKFYSLPALGKELGgDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 80 AYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVF 159
Cdd:PRK12881 80 PFVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 160 LKWGQQAFSRFSVVPPGTGICHQVNLEYLGKAVWSELQDKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
Cdd:PRK12881 160 LKWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 240 QPVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPI 319
Cdd:PRK12881 240 QPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 320 DSVTLEYMRLSGRSEEQVALVEAYTKAQGMWRNPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAFAASNEL 399
Cdd:PRK12881 320 DEQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 400 EVNAAQKDHRPVDyvlnGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSDY 479
Cdd:PRK12881 400 PVAENGFAKKAQT----SNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 480 LAQARLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYA 559
Cdd:PRK12881 476 LERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAYA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 560 LAGNMNINLATDPIGHDRKNEPVYLKDIWPSSREIARAVE-KVSTEMFRKEYAEVFEGTAEWKAIDVVGSDTYDWQDDST 638
Cdd:PRK12881 556 LAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAfAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKST 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 639 YIRLSPFFDEMLAEPAPLKDIHGARILAMLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMMR 718
Cdd:PRK12881 636 YIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMMR 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 719 GTFANIRIRNEMVPGVEGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESF 798
Cdd:PRK12881 716 GTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESF 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 799 ERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEQIDISGL-QNLQPGKTVPVKLTRADGTTEVLDCRCRIDTATELTYYQ 877
Cdd:PRK12881 796 ERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRIDTPIEVDYYK 875
|
890
....*....|...
gi 1738305823 878 NDGILHYVIRKML 890
Cdd:PRK12881 876 AGGILPYVLRQLL 888
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
7-890 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1330.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 7 EASKDTLQaENKTWRYYSLPlaarTLGD--ISRLPKSLKVLLENLLRWQDGDSVTEEDIQALAGWLKNAHADREIAYRPA 84
Cdd:PTZ00092 17 EKVLKTLK-DGGSYKYYSLN----ELHDprLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVFLKWGQ 164
Cdd:PTZ00092 92 RVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 165 QAFSRFSVVPPGTGICHQVNLEYLGKAVWselqDKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:PTZ00092 172 KAFKNLLIVPPGSGIVHQVNLEYLARVVF----NKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 245 LIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSVTL 324
Cdd:PTZ00092 248 VLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 325 EYMRLSGRSEEQVALVEAYTKAQGMWRNPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAFAASNELEVN-- 402
Cdd:PTZ00092 328 DYLKQTGRSEEKVELIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGfk 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 403 ----AAQKDHRPVDYVLNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSD 478
Cdd:PTZ00092 408 gfgiPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 479 YLAQARLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAY 558
Cdd:PTZ00092 488 YLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAY 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 559 ALAGNMNINLATDPIGHDRKNEPVYLKDIWPSSREIARAVEK-VSTEMFRKEYAEVFEGTAEWKAIDVVGSDTYDWQDDS 637
Cdd:PTZ00092 568 ALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKyVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 638 TYIRLSPFFDEMLAEPAPLKDIHGARILAMLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMM 717
Cdd:PTZ00092 648 TYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMV 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 718 RGTFANIRIRNEMVPGVeGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAES 797
Cdd:PTZ00092 728 RGTFANIRLINKLCGKV-GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAES 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 798 FERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEQIDISGLQ-NLQPGKTVPVKltRADGTTevLDCRCRIDTATELTYY 876
Cdd:PTZ00092 807 FERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVK--TDTGKT--FDTILRIDTEVEVEYF 882
|
890
....*....|....
gi 1738305823 877 QNDGILHYVIRKML 890
Cdd:PTZ00092 883 KHGGILQYVLRKLV 896
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
21-890 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1126.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 21 RYYSLPlaarTLGD--ISRLPKSLKVLLENLLRWQDGDSVTEEDIQALAGWLKNAHADREIAYRPARVLMQDFTGVPAVV 98
Cdd:PLN00070 62 KYYSLP----ALNDprIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKPARVLLQDFTGVPAVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 99 DLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVFLKWGQQAFSRFSVVPPGTG 178
Cdd:PLN00070 138 DLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 179 ICHQVNLEYLGKAVWSelqdKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPDVVGFKLTGKL 258
Cdd:PLN00070 218 IVHQVNLEYLGRVVFN----TDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 259 SEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSVTLEYMRLSGRSEEQVA 338
Cdd:PLN00070 294 RDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 339 LVEAYTKAQGM---WRNPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVP-------------KAFAASNElevn 402
Cdd:PLN00070 374 MIEAYLRANKMfvdYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKadwhscldnkvgfKGFAVPKE---- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 403 aaqKDHRPVDYVLNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSDYLAQ 482
Cdd:PLN00070 450 ---AQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 483 ARLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAG 562
Cdd:PLN00070 527 SGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAG 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 563 NMNINLATDPIGHDRKNEPVYLKDIWPSSREIARAVEK-VSTEMFRKEYAEVFEGTAEWKAIDVVGSDTYDWQDDSTYIR 641
Cdd:PLN00070 607 TVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSsVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIH 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 642 LSPFFDEMLAEPAPLKDIHGARILAMLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMMRGTF 721
Cdd:PLN00070 687 EPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTF 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 722 ANIRIRNEMVPGVEGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERI 801
Cdd:PLN00070 767 ANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERI 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 802 HRSNLIGMGILPLEFPQGVTRKTLGLTGEEQIDI---SGLQNLQPGKTVPVKLTRADGTTevldCRCRIDTATELTYYQN 878
Cdd:PLN00070 847 HRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIdlpSNISEIKPGQDVTVTTDNGKSFT----CTLRFDTEVELAYFDH 922
|
890
....*....|..
gi 1738305823 879 DGILHYVIRKML 890
Cdd:PLN00070 923 GGILPYVIRNLI 934
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
85-564 |
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: 764.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDHFGDDDAFGENVRLEMERNHERYVFLKWGQ 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 165 QAFSRFSVVPPGTGICHQVNLEYLGKAVWSELQDKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 245 LIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDsvtl 324
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 325 eymrlsgrseeqvalveaytkaqgmwrnpgdepvfTSTLELDMGTVEASLAGPKRPQDRVALsnvpkafaasnelevnaa 404
Cdd:cd01586 237 -----------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL------------------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 405 qkdhrpvdyvlnghqyqlpDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQPWVKASLAPGSKVVSDYLAQAR 484
Cdd:cd01586 264 -------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEASG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 485 LTPYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKQGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNM 564
Cdd:cd01586 325 LLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
72-562 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 651.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 72 NAHADRE----IAYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSvtvdhfgdDDAFGENVR 147
Cdd:pfam00330 5 DAHLVEEldgsLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 148 LEMERNHERYVFLKWGQQAFSrFSVVPPGTGICHQVNLEYLgkavwselqdkewVAYPD-TLVGTDSHTTMINglgvlgw 226
Cdd:pfam00330 77 DEISRNKEQYDFLEWNAKKFG-IRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGglgalaf 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 227 gvggIEAEAAMLGQPVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANM 306
Cdd:pfam00330 143 gvggSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 307 APEYGATCGFFPIDSVTLEYMRLSGRSEEQValVEAYTKAQGMWRNPGDE-PVFTSTLELDMGTVEASLAGPKRPQDRVA 385
Cdd:pfam00330 223 AIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPgAEYDKVVEIDLSTIEPMVTGPTRPQDAVP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 386 LS-NVPKAFAasnelEVNAAQKDHRPVDYVLNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLaKKAVELGLKPQPW 464
Cdd:pfam00330 301 LSeLVPDPFA-----DAVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 465 VKASLAPGSKVVSDYLAQARLTPYLDELGFNLVGYGCTTCIGNSGPLPEpiemaikqGDLtvgAVLSGNRNFEGRIHPLV 544
Cdd:pfam00330 375 VKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--------GER---CVSSSNRNFEGRQGPGG 443
|
490
....*....|....*...
gi 1738305823 545 KTnWLASPPLVVAYALAG 562
Cdd:pfam00330 444 RT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
667-837 |
4.08e-119 |
|
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: 358.51 E-value: 4.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 667 MLGDSVTTDHISPAGSIKADSPAGRYLQSRGVERRDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGMTRHLPDTE 746
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 747 VISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPQGVTRKTLG 826
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|.
gi 1738305823 827 LTGEEQIDISG 837
Cdd:cd01580 161 LTGEETYDIIG 171
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
78-860 |
6.11e-84 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 282.42 E-value: 6.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 78 EIAYRPARVLMQDFTGVPAVVDLAAMreavkrlGGDTAKVnPLSpvdlvIDHsvtVDHfgdddafgeNVRLEMERNHERY 157
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAM-------GLDRVKT-ELS-----VQY---VDH---------NLLQADFENADDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 158 VFLkwgQQAFSRFSVV--PPGTGICHQVNLEYLGKavwselqdkewvayP-DTLVGTDSHTT------MInglgvlgwgv 228
Cdd:PRK07229 79 RFL---QSVAAKYGIYfsKPGNGICHQVHLERFAF--------------PgKTLLGSDSHTPtagglgML---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 229 gGI-----EAEAAMLGQPVSMLIPDVVGFKLTGKLSEGITATDLVLTvtqMLRKHGV---VGKFVEFYGDGLDSLPLADR 300
Cdd:PRK07229 132 -AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILE---LLRRLTVkggVGKIIEYFGPGVATLSVPER 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 301 ATIANMAPEYGATCGFFPIDSVTLEYMRLSGRSEEQVALVeaytkaqgmwrnPGDEPVFTSTLELDMGTVEASLAGPKRP 380
Cdd:PRK07229 208 ATITNMGAELGATTSIFPSDERTREFLKAQGREDDWVELL------------ADPDAEYDEVIEIDLSELEPLIAGPHSP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 381 QDRVALSNVPKAfaasnelevnaaqkdhrPVDYVLnghqyqlpdgavviaaITSCTNTSNPSVLMAAGLLAKKAVElglk 460
Cdd:PRK07229 276 DNVVPVSEVAGI-----------------KVDQVL----------------IGSCTNSSYEDLMRAASILKGKKVH---- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 461 pqpwVKASL--APGSKVVSDYLAQARLTPYLDELGFNLVGYGCTTCIGNSGplpEPIEMAIkqgdltvgAVLSGNRNFEG 538
Cdd:PRK07229 319 ----PKVSLviNPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNV--------SLRTFNRNFPG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 539 RIHPLVKTNWLASPPLVVAYALAGNMninlaTDPIGHDRKN-EPVYLKDiwPSSREiaravekVSTEMFRKEyaevfegT 617
Cdd:PRK07229 384 RSGTKDAQVYLASPETAAASALTGVI-----TDPRTLALENgEYPKLEE--PEGFA-------VDDAGIIAP-------A 442
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 618 AEWKAIDVVGSDTYDwqddstyiRLSPFfdemlaepAPLKDIHGARILAMLGDSVTTDHISPAGSikadspagRYLQSRG 697
Cdd:PRK07229 443 EDGSDVEVVRGPNIK--------PLPLL--------EPLPDLLEGKVLLKVGDNITTDHIMPAGA--------KWLPYRS 498
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 698 verrdfnsygsrrgnhevmmrgtfaNI-RIRNEMVPGVEGgmtrhlpdtevisiyDAAMKYQQQGtPLAVIAGKEYGSGS 776
Cdd:PRK07229 499 -------------------------NIpNISEFVFEGVDN---------------TFPERAKEQG-GGIVVGGENYGQGS 537
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 777 SRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEF---------PQGVTrktlgltgeeqIDISGLQNLQPGKTV 847
Cdd:PRK07229 538 SREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFadpadydkiEEGDV-----------LEIEDLREFLPGGPL 606
|
810
....*....|...
gi 1738305823 848 PVKLTRADGTTEV 860
Cdd:PRK07229 607 TVVNVTKDEEIEV 619
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-562 |
1.92e-82 |
|
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: 270.52 E-value: 1.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVVDLAAMREAVKrlggdtakVNPLSPVDLVIDHSVtvdhfgdddafgenvRLEMERNHERYVFLKWgq 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAV---------------QLEKPVNNEGHKFLSF-- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 165 qaFSR---FSVVPPGTGICHQVNLEYLGKavwselqdkewvaYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQP 241
Cdd:cd01351 56 --FAAlqgIAFYRPGVGIIHQIMVENLAL-------------PGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 242 VSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDS 321
Cdd:cd01351 121 AWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 322 VTLEYMRLSGRSEEQvALVEAYTKAQgmwrNPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKafaasnelev 401
Cdd:cd01351 201 TTLKWLEATGRPLLK-NLWLAFPEEL----LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG---------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 402 naaqkdhrpvdyvlnghqyqlpdGAVVIAAITSCTNtSNPSVLMAAGLLAKKAvelglKPQPWVKASLAPGSKVVSDYLA 481
Cdd:cd01351 266 -----------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLIVTPGSRMVYATLS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 482 QARLTPYLDELGFNLVGYGCTTCIGNSGPLPepiemaikqGDLTVGaVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALA 561
Cdd:cd01351 317 REGYYEILVDSGARILPPGCGPCMGNGARLV---------ADGEVG-VSSGNRNFPGRLGTYERHVYLASPELAAATAIA 386
|
.
gi 1738305823 562 G 562
Cdd:cd01351 387 G 387
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
689-819 |
9.33e-63 |
|
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: 207.60 E-value: 9.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 689 AGRYLQSRGVERRDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGMTRHLPDTEVISIYDAAMKYQQQGTPLAVIA 768
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1738305823 769 GKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPQG 819
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
87-562 |
1.02e-46 |
|
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: 171.86 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 87 LMQDFTGVPAVVDLAAMreavkrlGGDTAKVnPLSPVdlVIDHSVTVDHFgdddafgenvrlemeRNHERYVFLkwgQQA 166
Cdd:cd01585 4 LTQDATGTMAYLQFEAM-------GVDRVRT-ELSVS--YVDHNTLQTDF---------------ENADDHRFL---QTV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 167 FSRFSVV--PPGTGICHQVNLEYLGKAvwselqdkewvayPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:cd01585 56 AARYGIYfsRPGNGICHQVHLERFAVP-------------GKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 245 LIPDVVGFKLTGKLSEGITATDLVLtvtQMLRKHGV---VGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDS 321
Cdd:cd01585 123 PMPKVVGVRLTGELPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 322 VTLEYMRLSGRSEEQVALVeaytkaqgmwrnPGDEPVFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAfaasnelev 401
Cdd:cd01585 200 RTREFLAAQGREDDWVELA------------ADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREVAGI--------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 402 naaqkdhrPVDYVlnghqyqlpdgavviaAITSCTNTSNPSVLMAAGLLAKKAVelglkpQPWVKASLAPGSKVVSDYLA 481
Cdd:cd01585 259 --------KVDQV----------------AIGSCTNSSYEDLMTVAAILKGRRV------HPHVSMVVAPGSKQVLEMLA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 482 QARLTPYLDELGFNLVGYGCTTCIGnsgplpepiemaIKQGDLTVG-AVLSGNRNFEGRIHPLVKTNWLASPPLVVAYAL 560
Cdd:cd01585 309 RNGALADLLAAGARILESACGPCIG------------MGQAPPTGGvSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAAL 376
|
..
gi 1738305823 561 AG 562
Cdd:cd01585 377 TG 378
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
85-562 |
3.60e-39 |
|
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: 150.03 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVvdlAAMREAVKRLGGDTAKVNplspvdLVIDHSVtvdhFGDDDAFGENVrlemerNHERYVFLKWGQ 164
Cdd:cd01583 1 LHLVHDVTSPQAF---EGLREAGREKVWDPEKIV------AVFDHNV----PTPDIKAAEQV------KTLRKFAKEFGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 165 QAFSRfsvvpPGTGICHQVNLEylgkavwselqdKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:cd01583 62 NFFDV-----GRQGICHVILPE------------KGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 245 LIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSVTL 324
Cdd:cd01583 125 RVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 325 EYMRLSGRSEEQVAlveaytkaqgmwrnPGDEP-VFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKAfaasnelevna 403
Cdd:cd01583 205 EYLKGRGKAYWKEL--------------KSDEDaEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI----------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 404 aqkdhrPVDYVLnghqyqlpdgavviaaITSCTNTSNPSVLMAAGLLAKKavelglKPQPWVKASLAPGSKVVsdYL-AQ 482
Cdd:cd01583 260 ------KIDQVF----------------IGSCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPASQRV--YKqAE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 483 AR-LTPYLDELGFNLVGYGCTTCIG-NSGPLPEpiemaikqGDLtvgAVLSGNRNFEGRI-HPLVKTnWLASPPLVVAYA 559
Cdd:cd01583 310 KEgLIEIFIEAGAEVRPPGCGACLGgHMGVLAP--------GER---CVSTSNRNFKGRMgSPGARI-YLASPATAAASA 377
|
...
gi 1738305823 560 LAG 562
Cdd:cd01583 378 ITG 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
85-562 |
1.72e-38 |
|
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: 148.64 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVvdlAAMREAVKRlggdtaKV-NPlspvDLVIdhsVTVDHF--GDDDAFGENVRlEMERNHERY--VF 159
Cdd:COG0065 30 LHLVHDVTSPQAF---EGLREAGGR------KVwDP----DRIV---AVFDHNvpTKDPKSAEQVK-TLREFAKEFgiTF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 160 LKWGQQafsrfsvvppgtGICHQVNLEyLGkavwselqdkewVAYP-DTLVGTDSHTTM----------INGLgvlgwgv 228
Cdd:COG0065 93 FDVGDP------------GICHVVLPE-QG------------LVLPgMTIVGGDSHTCThgafgafafgIGTT------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 229 ggiEAEAAMLGQPVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAP 308
Cdd:COG0065 141 ---DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 309 EYGATCGFFPIDSVTLEYMRlsGRseeqvalveAYTKAQGMWRNPGdePVFTSTLELDMGTVEASLAGPKRPQDRVALSN 388
Cdd:COG0065 218 EAGAKAGIIAPDETTFEYLK--GR---------PFAPWRTLKSDED--AVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 389 VpkafaasnelevnaaqkDHRPVDYVLnghqyqlpdgavviaaITSCTNtsnpSVL----MAAGLLAkkavelGLKPQPW 464
Cdd:COG0065 285 L-----------------EGIKIDQVF----------------IGSCTN----GRIedlrAAAEILK------GRKVAPG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 465 VKASLAPGSKVVsdyLAQARLTPYLDEL---GFNLVGYGCTTCIG-NSGPLPEpiemaikqGDLTVGavlSGNRNFEGRI 540
Cdd:COG0065 322 VRAIVVPGSQEV---YRQAEAEGLDEIFieaGAEWREPGCGMCLGmNMGVLAP--------GERCAS---TSNRNFEGRM 387
|
490 500
....*....|....*....|...
gi 1738305823 541 -HPLVKTnWLASPPLVVAYALAG 562
Cdd:COG0065 388 gSPGSRT-YLASPATAAASAIAG 409
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-564 |
1.97e-38 |
|
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: 148.36 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVvdLAAMREAVKRlggdtakvnPLSPVDLVIDHSVTVDHFGDDDafgenVRLEMERNHERYVFLkwgQ 164
Cdd:cd01584 1 RVAMQDATAQMAL--LQFMSSGLPK---------VAVPSTIHCDHLIEAQVGGEKD-----LKRAKDINKEVYDFL---A 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 165 QAFSRFSV--VPPGTGICHQVNLE-YlgkavwselqdkewvAYPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ 240
Cdd:cd01584 62 SAGAKYGIgfWKPGSGIIHQIVLEnY---------------AFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 241 PVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPID 320
Cdd:cd01584 127 PWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 321 SVTLEYMRLSGRSEeqVALVEAYTKAQGMWRNPGDEpvFTSTLELDMGTVEASLAGPKRPQDRVALSNVPKafaasnele 400
Cdd:cd01584 207 ERMKKYLKATGRAE--IADLADEFKDDLLVADEGAE--YDQLIEINLSELEPHINGPFTPDLATPVSKFKE--------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 401 vnAAQKDHRPVDyvlnghqyqlpdgaVVIAAITSCTNTSNPSVLMAAGlLAKKAVELGLKPQpwVKASLAPGSKVVSDYL 480
Cdd:cd01584 274 --VAEKNGWPLD--------------LRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTITPGSEQIRATI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 481 AQARLTPYLDELGFNLVGYGCTTCIGNSGplpepiEMAIKQGDLTVgAVLSGNRNFEGRIHPLVKT-NWLASPPLVVAYA 559
Cdd:cd01584 335 ERDGLLQTFRDAGGIVLANACGPCIGQWD------RKDIKKGEKNT-IVTSYNRNFTGRNDANPAThAFVASPEIVTAMA 407
|
....*
gi 1738305823 560 LAGNM 564
Cdd:cd01584 408 IAGTL 412
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
73-572 |
4.49e-31 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 126.83 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 73 AHADRE------IAYRPARVLMQDFTGVPAVvdlaamrEAVKRLGGDtaKVNPLSPVDLVIDHSVTvdhfGDDDAFGENV 146
Cdd:PRK00402 12 RHSGRDvspgdiVEAKVDLVMAHDITGPLAI-------KEFEKIGGD--KVFDPSKIVIVFDHFVP----AKDIKSAEQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 147 RleMERNHERyvflkwgQQAFSRFSVVppGTGICHQVnleylgkavwseLQDKEWVAYPDTLVGTDSHTT---------- 216
Cdd:PRK00402 79 K--ILREFAK-------EQGIPNFFDV--GEGICHQV------------LPEKGLVRPGDVVVGADSHTCtygalgafat 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 217 ------MinglgvlgwgvggieAEAAMLGQpVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGD 290
Cdd:PRK00402 136 gmgstdM---------------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 291 GLDSLPLADRATIANMAPEYGATCGFFPIDSVTLEYmrLSGRSEEQVALVEAytkaqgmwrnpgDEP-VFTSTLELDMGT 369
Cdd:PRK00402 200 TIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEY--LKERAGRDYKPWKS------------DEDaEYEEVYEIDLSK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 370 VEASLAGPKRPqdrvalSNVpkafaasneleVNAAQKDHRPVDYVLnghqyqlpdgavviaaITSCTNTSNPSVLMAAGL 449
Cdd:PRK00402 266 LEPQVAAPHLP------DNV-----------KPVSEVEGTKVDQVF----------------IGSCTNGRLEDLRIAAEI 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 450 LAKKAVelglkpQPWVKASLAPGSKvvSDYLaQARLTPYLDEL---GFnLVGY-GCTTCIGNS-GPLPEpiemaikqGDL 524
Cdd:PRK00402 313 LKGRKV------APGVRLIVIPASQ--KIYL-QALKEGLIEIFvdaGA-VVSTpTCGPCLGGHmGVLAP--------GEV 374
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1738305823 525 tvgAVLSGNRNFEGRI-HPLVKTnWLASPPLVVAYALAGNMninlaTDP 572
Cdd:PRK00402 375 ---CLSTTNRNFKGRMgSPESEV-YLASPAVAAASAVTGKI-----TDP 414
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
86-562 |
1.88e-28 |
|
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: 119.09 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 86 VLMQDFTGVPAVvdlaamrEAVKRLGGDTAKvNPlSPVDLVIDHSVTVDhfgdddafgeNVRL-EMERNHERYVfLKWGQ 164
Cdd:TIGR01343 28 AMVHDITAPLAI-------KTLEEYGIDKVW-NP-EKIVIVFDHQVPAD----------TIKAaEMQKLAREFV-KKQGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 165 QAFSrfsvvPPGTGICHQVnleylgkavwseLQDKEWVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:TIGR01343 88 KYFY-----DVGEGICHQV------------LPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 245 LIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSVTL 324
Cdd:TIGR01343 151 KVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 325 EYMRLSGRSEEQVAlveaytkaqgmwrnPGDEPV-FTSTLELDMGTVEASLAGPKRPqdrvalSNVPKAfaasnelevna 403
Cdd:TIGR01343 231 QYLKERRKEPFRVY--------------KSDEDAeYAKEIEIDASQIEPVVACPHNV------DNVKPV----------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 404 AQKDHRPVDYVLnghqyqlpdgavviaaITSCTNTSNPSVLMAAGLLAKKAVElglkpqPWVKASLAPGSKVVsdYLaQA 483
Cdd:TIGR01343 280 SEVEGTEIDQVF----------------IGSCTNGRLEDLRVAAKILKGRKVA------PDVRLIVIPASRAV--YL-QA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 484 rltpyLDE-LGFNLVGYGCTTCIGNSGPLpepieMAIKQGDLTVGAVL--SGNRNFEGRIHPLVKTNWLASPPLVVAYAL 560
Cdd:TIGR01343 335 -----LKEgLIEIFVKAGAVVSTPGCGPC-----LGSHQGVLAPGEVCisTSNRNFKGRMGHPNAEIYLASPATAAASAV 404
|
..
gi 1738305823 561 AG 562
Cdd:TIGR01343 405 KG 406
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
64-572 |
2.65e-27 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273960 Cd Length: 413 Bit Score: 115.63 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 64 QALAGWLKNAHADREIA------YRPARVLMQDFTGVPAVvdlaamrEAVKRLGgdTAKVNPLSPVDLVIDHSVTvdhfg 137
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCageiveVEVDLAMTHDGTGPLAI-------KALRELG--VARVWDPEKIVIAFDHNVP----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 138 dddafGENVRL-EMERnheryVFLKWGQQafSRFSVVPPGTGICHQVNLEylgkavwselqdKEWVAYPDTLVGTDSHTT 216
Cdd:TIGR02086 67 -----PPTVEAaEMQK-----EIREFAKR--HGIKNFDVGEGICHQILAE------------EGYALPGMVVVGGDSHTC 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 217 MINGLGVLGWGVGGIE-AEAAMLGQPVSMlIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSL 295
Cdd:TIGR02086 123 TSGAFGAFATGMGATDmAIALATGKTWIK-VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 296 PLADRATIANMAPEYGATCGFFPIDSVTLEYMRLSGRSEEQVAlveaytkaqgmwrNPGDEPVFTSTLELDMGTVEASLA 375
Cdd:TIGR02086 202 DMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRGLEFRIL-------------VPDPGANYYKEIEIDLSDLEPQVA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 376 GPKRPqdrvalsnvpkafaaSNELEVNAAQKDHrpVDYVLnghqyqlpdgavviaaITSCTNTSNPSVLMAAGLLAkkav 455
Cdd:TIGR02086 269 VPHSV---------------DNVKPVSDVEGTE--IDQVF----------------IGSCTNGRLEDLRIAAEILK---- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 456 elGLKPQPWVKASLAPGSKVVSDYLAQARLTPYLDELGFNLVGYGCTTCIGnsgplpepiemaIKQGDLTVGAVL--SGN 533
Cdd:TIGR02086 312 --GRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLG------------AHMGVLGDGEVClsTTN 377
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1738305823 534 RNFEGRI-HPLVKTnWLASPPLVVAYALAGNMninlaTDP 572
Cdd:TIGR02086 378 RNFKGRMgSPNAEI-YLASPATAAASAVEGYI-----TDP 411
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
85-562 |
6.29e-24 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 106.14 E-value: 6.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 85 RVLMQDFTGVPAVVDLAAMREAVKRLGGDTAkvnplspvdlVIDHSVTVDHFGDD---DAFGENVRLEMERNHERYvflk 161
Cdd:PRK12466 30 RHLLNEYTSPQAFSGLRARGRTVRRPDLTLA----------VVDHVVPTRPGRDRgitDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 162 wgqqAFSRFSVVPPGTGICHQVNLEyLGkavwselqdkewVAYPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ 240
Cdd:PRK12466 96 ----GIRLFDVDDPRQGIVHVVAPE-LG------------LTLPGmVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 241 PVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPID 320
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 321 SVTLEYMRlsGRSEE-QVALVEAytkAQGMWRN-PGDE-PVFTSTLELDMGTVEASLAGPKRPQDRVALS-NVPKAFAAS 396
Cdd:PRK12466 239 ETTFDYLR--GRPRApKGALWDA---ALAYWRTlRSDAdAVFDREVEIDAADIAPQVTWGTSPDQAVPITgRVPDPAAEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 397 NELEVNAAQkdhRPVDYV-LNGHQyQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAkkavelGLKPQPWVKASLAPGSKV 475
Cdd:PRK12466 314 DPARRAAME---RALDYMgLTPGT-PLAGIPIDRVFIGSCTNGRIEDLRAAAAVLR------GRKVAPGVRAMVVPGSGA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 476 VSDYLAQARLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIEMAIKqgdltvgavlSGNRNFEGRIHPLVKTNwLASPPLV 555
Cdd:PRK12466 384 VRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCAS----------TTNRNFEGRQGPGARTH-LMSPAMV 452
|
....*..
gi 1738305823 556 VAYALAG 562
Cdd:PRK12466 453 AAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
174-564 |
1.27e-23 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 103.46 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 174 PPGTGICHQVNLEylgkavwselqdkEWVAYPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPDVVGF 252
Cdd:cd01582 64 PAGRGIGHQIMIE-------------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 253 KLTGKLSEGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPIDSvtleymrlsgr 332
Cdd:cd01582 131 ELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA----------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 333 seeqvalveaytkaqgmwrnpgdepvftSTLELDMGTVEASLAGPkrpqdrvalsNVPKAFAASNELEVNaaqkdhrpvd 412
Cdd:cd01582 200 ----------------------------KHLILDLSTLSPYVSGP----------NSVKVSTPLKELEAQ---------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 413 yvlnghqyqlpDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVELGLKPQ-PWVKASLAPGSKVVSDYLAQARLTPYLDE 491
Cdd:cd01582 232 -----------NIKINKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIPVaPGVEFYVAAASSEVQAAAEKNGDWQTLLE 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1738305823 492 LGFNLVGYGCTTCIGNSGPLPEPIEMAIKqgdltvgavlSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNM 564
Cdd:cd01582 301 AGATPLPAGCGPCIGLGQGLLEPGEVGIS----------ATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
761-837 |
4.01e-23 |
|
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: 94.07 E-value: 4.01e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1738305823 761 GTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPqgVTRKTLGLTGEEQIDISG 837
Cdd:cd00404 14 AGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFA--DPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
668-816 |
6.35e-20 |
|
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: 86.34 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 668 LGDSVTTDHISPAGSikadspagRYLqsrgverrdfnsygSRRGNHEVMMRGTFAniRIRNEMVPGVeggmtrhlpdtev 747
Cdd:cd01579 2 VGDNITTDHIMPAGA--------KVL--------------PLRSNIPAISEFVFH--RVDPTFAERA------------- 44
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738305823 748 isiydaamkyqQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEF 816
Cdd:cd01579 45 -----------KAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
673-844 |
5.01e-19 |
|
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: 84.44 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 673 TTDHISPAGsikadsPAGRYlqsrgverrdfnsygsrrgnhevmmRGTFANIRirNEMVPG---VEGGMTRHLPDT---E 746
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIS--NNLLIGainAENGKANSVKNQvtgE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 747 VISIYDAAMKYQQQGTPLAVIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEF--PQGVTRkt 824
Cdd:cd01578 54 YGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFadPADYDK-- 131
|
170 180
....*....|....*....|
gi 1738305823 825 lgLTGEEQIDISGLQNLQPG 844
Cdd:cd01578 132 --IHPDDKVDILGLTDFAPG 149
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
243-562 |
1.57e-18 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 89.41 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 243 SMLIpdvvgfKLTGKLSEGITATDLVLTVtqmLRKHGV---VGKFVEFYGDGLDSLPLADRATIANMAPEYGATCGFFPI 319
Cdd:PRK05478 165 TMKI------EVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 320 DSVTLEYMRlsGRseEQVALVEAYTKAQGMWRN-PGDE-PVFTSTLELDMGTVEASLAGPKRPQDRVALS-NVPKAFAAS 396
Cdd:PRK05478 236 DETTFEYLK--GR--PFAPKGEDWDKAVAYWKTlKSDEdAVFDKVVTLDAADIEPQVTWGTNPGQVISIDgKVPDPEDFA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 397 NELEVNAAQkdhRPVDYV-LNGHQYqLPDGAVVIAAITSCTNtSNPSVLMAAGLLAKkavelGLKPQPWVKASLAPGSKV 475
Cdd:PRK05478 312 DPVKRASAE---RALAYMgLKPGTP-ITDIKIDKVFIGSCTN-SRIEDLRAAAAVVK-----GRKVAPGVRALVVPGSGL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 476 VSdylAQAR---LTPYLDELGFNLVGYGCTTCIG-NSGPLPEpiemaikqGDLtvgAVLSGNRNFEGRIHPLVKTNwLAS 551
Cdd:PRK05478 382 VK---AQAEaegLDKIFIEAGFEWREPGCSMCLAmNPDKLPP--------GER---CASTSNRNFEGRQGKGGRTH-LVS 446
|
330
....*....|.
gi 1738305823 552 PPLVVAYALAG 562
Cdd:PRK05478 447 PAMAAAAAITG 457
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
655-823 |
3.53e-12 |
|
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: 65.96 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 655 PLKDIHGaRILAMLGDSVTTDHISPAgsikadspagRYLQSrgVERRDFnsygsrrGNHevmmrgTFANIRIRNEMVPG- 733
Cdd:COG0066 2 KFTTLTG-RAVPLDGDNIDTDQIIPA----------RFLKT--IDREGL-------GKH------LFEDWRYDRSPDPDf 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 734 ------VEGGmtrhlpdteviSIydaamkyqqqgtplaVIAGKEYGSGSSRD---WAAKGprlLGVRVVIAESFERIHRS 804
Cdd:COG0066 56 vlnqprYQGA-----------DI---------------LVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYR 106
|
170
....*....|....*....
gi 1738305823 805 NLIGMGILPLEFPQGVTRK 823
Cdd:COG0066 107 NAINNGLLPIELPEEAVDA 125
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
766-820 |
4.77e-12 |
|
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: 62.61 E-value: 4.77e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1738305823 766 VIAGKEYGSGSSR---DWAAKGprlLGVRVVIAESFERIHRSNLIGMGILPLEFPQGV 820
Cdd:cd01577 21 IVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADED 75
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
766-850 |
2.52e-10 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 59.84 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 766 VIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPQgvTRKTLGlTGEE-QIDISG--LQNLQ 842
Cdd:PRK00439 52 IVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDE--AVDKIE-DGDEvEVDLETgvITNLT 128
|
....*...
gi 1738305823 843 PGKTVPVK 850
Cdd:PRK00439 129 TGEEYKFK 136
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
766-818 |
4.45e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 59.43 E-value: 4.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1738305823 766 VIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPQ 818
Cdd:PRK14023 53 LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEE 105
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
766-817 |
2.79e-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: 2.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1738305823 766 VIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFP 817
Cdd:TIGR02087 51 IVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIEAK 102
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
767-818 |
6.35e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 50.90 E-value: 6.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1738305823 767 IAGKEYGSGSSRD---WAakgprLL--GVRVVIAESFERIHRSNLIGMGILPLEFPQ 818
Cdd:PRK01641 72 LAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIVLPE 123
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
173-389 |
8.94e-06 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 49.62 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 173 VPPGTGICHQVNLEYL---GKAVwselqdkewvaypdtlVGTDSHT------TMinglgvlgwgvgGI-----EAEAAML 238
Cdd:PRK11413 123 VPPHIAVIHQYMREMMaggGKMI----------------LGSDSHTrygalgTM------------AVgegggELVKQLL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738305823 239 GQPVSMLIPDVVGFKLTGKLSEGITATDLVLTVTQMLRKHGVV-GKFVEFYGDGLDSLPLADRATIANMAPEygATC--G 315
Cdd:PRK11413 175 NDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsS 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738305823 316 FFPIDSVTLEYMRLSGRSEEQVALveaytkaqgmwrNPGDEPVFTSTLELDMGTVEASLAGPKRPqdrvalSNV 389
Cdd:PRK11413 253 IWQTDEEVHNWLALHGRGQDYCEL------------NPQPMAYYDGCISVDLSAIKPMIALPFHP------SNV 308
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
774-835 |
8.71e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 42.79 E-value: 8.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738305823 774 SGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEQIDI 835
Cdd:PRK14812 2 AGSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTV 63
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
766-815 |
5.50e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 42.54 E-value: 5.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1738305823 766 VIAGKEYGSGSSRDWAAKGPRLLGVRVVIAESFERIHRSNLIGMG-ILPLE 815
Cdd:PLN00072 133 IIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| |
