|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
69-945 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1723.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 69 LSVNGNEYHYYSLKEAERGGLKDLSKLPFTLKILLENLLRHLDGHTVTVDDLKAIIEWLKLKSSDHEIAYRPARVLMQDF 148
Cdd:PRK09277 13 LEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIPFRPARVVMQDF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 149 TGVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQMEMERNHERYEFLRWGQKAFKNFR 228
Cdd:PRK09277 93 TGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFLKWGQKAFDNFR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 229 VVPPDTGICHQINLEYLAKTVWTQQiNGKIYAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPISLLIPEVIG 308
Cdd:PRK09277 173 VVPPGTGICHQVNLEYLAPVVWTRE-DGELVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPSSMLIPEVVG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 309 VKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDYLRLSG 388
Cdd:PRK09277 252 VKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 389 REEQDIALVEAYAKTQGLWHNPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTFNQFLTENNRTEEKEKSfI 468
Cdd:PRK09277 332 RDEEQVALVEAYAKAQGLWRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQGFGLDEA-E 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 469 TDSNFEMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRKPWVKTSFAPGSQVVTRYLEETNLQKYLNELGFT 548
Cdd:PRK09277 411 EGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLPYLEALGFN 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 549 LVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGTTLIDLTKDPLGK 628
Cdd:PRK09277 491 LVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDIDLEKDPLGT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 629 DASGNPVYLKDIWPTNAEIACEVAK-ISRNMFHDTYAHIFEGTDEWRAMKISKSDTYAWPVNSTYIQHPPYFDEMNVNPE 707
Cdd:PRK09277 571 DKDGNPVYLKDIWPSDEEIDAVVAKaVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPYFEGMLAEPG 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 708 KIKEIKGARILALFGDSITTDHISPAGSIKPDSPAGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPDV 787
Cdd:PRK09277 651 PVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGV 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 788 EGGFTKHIPNNEILPIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPL 867
Cdd:PRK09277 731 EGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPL 810
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179981458 868 EFPEGVTRKTLQITGSELIDIVGLThEMKPRMQVKVIIHNEDKTQNEIHLILRIDTLNELDYYKNGGILHYVLRGMLK 945
Cdd:PRK09277 811 QFKPGESRKTLGLDGTETFDIEGLE-DLKPGATVTVVITRADGEVVEFPVLCRIDTAVEVDYYRNGGILQYVLRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
64-945 |
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: 1684.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 64 SIQQILSVNGNEYHYYSLKEAERGGlKDLSKLPFTLKILLENLLRHLDGHTVTVDDLKAIIEWLKLKSSDHEIAYRPARV 143
Cdd:COG1048 6 KARKTLTVGGKPYTYYSLPALEEAG-GDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 144 LMQDFTGVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQMEMERNHERYEFLRWGQKA 223
Cdd:COG1048 85 LMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 224 FKNFRVVPPDTGICHQINLEYLAKTVWTQQINGKIYAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPISLLI 303
Cdd:COG1048 165 FDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPVSMLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 304 PEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDY 383
Cdd:COG1048 245 PEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 384 LRLSGREEQDIALVEAYAKTQGLWHNPH-LEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTFNQFLTE--NNRT 460
Cdd:COG1048 325 LRLTGRSEEQIELVEAYAKAQGLWRDPDaPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAApvGEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 461 EEKEKSFITDSNFEMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRKPWVKTSFAPGSQVVTRYLEETNLQK 540
Cdd:COG1048 405 DKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLP 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 541 YLNELGFTLVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGTTLID 620
Cdd:COG1048 485 YLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDID 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 621 LTKDPLGKDASGNPVYLKDIWPTNAEIACEVAK-ISRNMFHDTYAHIFEGTDEWRAMKISKSDTYAWPVNSTYIQHPPYF 699
Cdd:COG1048 565 LTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKaVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFF 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 700 DEMNVNPEKIKEIKGARILALFGDSITTDHISPAGSIKPDSPAGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIRI 779
Cdd:COG1048 645 EGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRI 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 780 RNEMTPDVEGGFTKHIPNNEILPIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNL 859
Cdd:COG1048 725 KNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNL 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 860 IGMGILPLEFPEGVTRKTLQITGSELIDIVGLTHEMKPRMQVKVIIHNEDKTQNEIHLILRIDTLNELDYYKNGGILHYV 939
Cdd:COG1048 805 VGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAPGKTVTVTATRADGSTEEFPVLHRIDTPVEVEYYRAGGILQYV 884
|
....*.
gi 1179981458 940 LRGMLK 945
Cdd:COG1048 885 LRQLLA 890
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
69-945 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1476.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 69 LSVNGNEYHYYSLKEAERGGLKDLSKLPFTLKILLENLLRHLDGHTVTVDDLKAIIEWLKLKSSDHEIAYRPARVLMQDF 148
Cdd:PRK12881 12 FDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIPFVPARVVMQDF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 149 TGVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQMEMERNHERYEFLRWGQKAFKNFR 228
Cdd:PRK12881 92 TGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQAFDNFR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 229 VVPPDTGICHQINLEYLAKTVWTQQINGKIYAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISLLIPEVIG 308
Cdd:PRK12881 172 VVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 309 VKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDYLRLSG 388
Cdd:PRK12881 252 VELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 389 REEQDIALVEAYAKTQGLWHNPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTFNQFLTENNRTEEKEKSFI 468
Cdd:PRK12881 332 RTEAQIALVEAYAKAQGLWGDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKAQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 469 TDSNFEMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRKPWVKTSFAPGSQVVTRYLEETNLQKYLNELGFT 548
Cdd:PRK12881 412 TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFG 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 549 LVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGTTLIDLTKDPLGK 628
Cdd:PRK12881 492 IVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAYALAGTVRRDLMTEPLGK 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 629 DASGNPVYLKDIWPTNAEIACEVA-KISRNMFHDTYAHIFEGTDEWRAMKISKSDTYAWPVNSTYIQHPPYFDEMNVNPE 707
Cdd:PRK12881 572 GKDGRPVYLKDIWPSSAEIDALVAfAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKSTYIRRPPFFDFSMGPAA 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 708 KIKEIKGARILALFGDSITTDHISPAGSIKPDSPAGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPDV 787
Cdd:PRK12881 652 SIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMMRGTFANVRIKNLMIPGK 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 788 EGGFTKHIPNNEILPIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPL 867
Cdd:PRK12881 732 EGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPL 811
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179981458 868 EFPEGVTRKTLQITGSELIDIVGLTHEMKPRMQVKVIIHNEDKTQNEIHLILRIDTLNELDYYKNGGILHYVLRGMLK 945
Cdd:PRK12881 812 QFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVTLVIHRADGSTERVPVLCRIDTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
75-944 |
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: 1357.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 75 EYHYYSLKEAERGGLKdLSKLPFTLKILLENLLRHLDGHTVTVDDLKAIIEWLKLKSSDHEIAYRPARVLMQDFTGVPAI 154
Cdd:TIGR01341 2 TYYYYSLKALEESGGK-ISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 155 VDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQMEMERNHERYEFLRWGQKAFKNFRVVPPDT 234
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 235 GICHQINLEYLAKTVWTQQINGKIYAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISLLIPEVIGVKLVGQ 314
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 315 LQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDYLRLSGREEQDI 394
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 395 ALVEAYAKTQGLWHNPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTFNQFLTEN----NRTEEKEKSF--I 468
Cdd:TIGR01341 321 ELVEKYARAQGLFYDDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNggdkGFTLRKEPLKkkV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 469 TDSNFEMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRKPWVKTSFAPGSQVVTRYLEETNLQKYLNELGFT 548
Cdd:TIGR01341 401 NGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELGFN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 549 LVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGTTLIDLTKDPLGK 628
Cdd:TIGR01341 481 LVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPIGT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 629 DASGNPVYLKDIWPTNAEIACEVAK-ISRNMFHDTYAHIFEGTDEWRAMKISKSDTYAWPVNSTYIQHPPYFDEMNVNPE 707
Cdd:TIGR01341 561 DKDGKPVYLRDIWPSNKEIAAYVNMaVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQDPE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 708 KIKEIKGARILALFGDSITTDHISPAGSIKPDSPAGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPDV 787
Cdd:TIGR01341 641 EVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMVKGK 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 788 EGGFTKHIPNNEILPIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPL 867
Cdd:TIGR01341 721 EGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGVIPL 800
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179981458 868 EFPEGVTRKTLQITGSELIDIVGLThEMKPRMQVKVIIHNEDKTQNEIHLILRIDTLNELDYYKNGGILHYVLRGML 944
Cdd:TIGR01341 801 QFPQGEDAETLGLTGDETIDIDGIK-DLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLRKFL 876
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
72-945 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1304.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 72 NGNEYHYYSLKEaerggLKD--LSKLPFTLKILLENLLRHLDGHTVTVDDLKAIIEWLKLKSSDHEIAYRPARVLMQDFT 149
Cdd:PTZ00092 25 DGGSYKYYSLNE-----LHDprLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPARVLLQDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 150 GVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQMEMERNHERYEFLRWGQKAFKNFRV 229
Cdd:PTZ00092 100 GVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSKAFKNLLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 230 VPPDTGICHQINLEYLAKTVWtqqiNGKIYAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISLLIPEVIGV 309
Cdd:PTZ00092 180 VPPGSGIVHQVNLEYLARVVF----NKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 310 KLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDYLRLSGR 389
Cdd:PTZ00092 256 KLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 390 EEQDIALVEAYAKTQGLWHNPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTFNQFLTEN------NRTEEK 463
Cdd:PTZ00092 336 SEEKVELIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPvgfkgfGIPEEK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 464 EKSFIT----DSNFEMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRKPWVKTSFAPGSQVVTRYLEETNLQ 539
Cdd:PTZ00092 416 HEKKVKftykGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 540 KYLNELGFTLVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGTTLI 619
Cdd:PTZ00092 496 KYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGRVNI 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 620 DLTKDPLGKDASGNPVYLKDIWPTNAEIACEVAK-ISRNMFHDTYAHIFEGTDEWRAMKISKSDTYAWPVNSTYIQHPPY 698
Cdd:PTZ00092 576 DFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKyVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTYIHNPPF 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 699 FDEMNVNPEKIKEIKGARILALFGDSITTDHISPAGSIKPDSPAGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIR 778
Cdd:PTZ00092 656 FQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRGTFANIR 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 779 IRNEMTPDVeGGFTKHIPNNEILPIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSN 858
Cdd:PTZ00092 736 LINKLCGKV-GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSN 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 859 LIGMGILPLEFPEGVTRKTLQITGSELIDIVGLTHEMKPRMQVKViihnedKTQN--EIHLILRIDTLNELDYYKNGGIL 936
Cdd:PTZ00092 815 LVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQDVTV------KTDTgkTFDTILRIDTEVEVEYFKHGGIL 888
|
....*....
gi 1179981458 937 HYVLRGMLK 945
Cdd:PTZ00092 889 QYVLRKLVK 897
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
50-946 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1109.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 50 RTSSNLVLTHEFHKSIQQILSVNGNEY-HYYSLKeaergGLKD--LSKLPFTLKILLENLLRHLDGHTVTVDDLKAIIEW 126
Cdd:PLN00070 34 RKFASMASENPFKGILTSLPKPGGGEFgKYYSLP-----ALNDprIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 127 LKLKSSDHEIAYRPARVLMQDFTGVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQME 206
Cdd:PLN00070 109 ENTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 207 MERNHERYEFLRWGQKAFKNFRVVPPDTGICHQINLEYLAKTVWtqqiNGKIYAYPDTLVGTDSHTTMINGLGVLGWGVG 286
Cdd:PLN00070 189 FQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVF----NTDGILYPDSVVGTDSHTTMIDGLGVAGWGVG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 287 GIEAEAAMLGQPISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPE 366
Cdd:PLN00070 265 GIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 367 YGATCGFFPIDEITLDYLRLSGREEQDIALVEAYAKTQGLW--HN-PHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVEL 443
Cdd:PLN00070 345 YGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFvdYNePQQERVYSSYLELDLEDVEPCISGPKRPHDRVPL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 444 SYLTSTFNQFLteNNRT---------EEKEKsfITDSNF-----EMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVE 509
Cdd:PLN00070 425 KEMKADWHSCL--DNKVgfkgfavpkEAQSK--VAKFSFhgqpaELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACE 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 510 KGITRKPWVKTSFAPGSQVVTRYLEETNLQKYLNELGFTLVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNF 589
Cdd:PLN00070 501 LGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNF 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 590 EGRIHPLVKANWLASPPLVVAFALAGTTLIDLTKDPLGKDASGNPVYLKDIWPTNAEIAcEVAKIS--RNMFHDTYAHIF 667
Cdd:PLN00070 581 EGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVA-EVVQSSvlPDMFKSTYEAIT 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 668 EGTDEWRAMKISKSDTYAWPVNSTYIQHPPYFDEMNVNPEKIKEIKGARILALFGDSITTDHISPAGSIKPDSPAGKYLQ 747
Cdd:PLN00070 660 KGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLM 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 748 SKGVSIKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPDVEGGFTKHIPNNEILPIYDAAMRYKKERTALVIIAGKEYGT 827
Cdd:PLN00070 740 ERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGS 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 828 GSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGVTRKTLQITGSEL--IDIVGLTHEMKPRMQVKVII 905
Cdd:PLN00070 820 GSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERytIDLPSNISEIKPGQDVTVTT 899
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 1179981458 906 HNedktQNEIHLILRIDTLNELDYYKNGGILHYVLRGMLKT 946
Cdd:PLN00070 900 DN----GKSFTCTLRFDTEVELAYFDHGGILPYVIRNLIKQ 936
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
142-616 |
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: 735.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 142 RVLMQDFTGVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHSIQVDEFLTPNAFTVNAQMEMERNHERYEFLRWGQ 221
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 222 KAFKNFRVVPPDTGICHQINLEYLAKTVWTQQINGKIYAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISL 301
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 302 LIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDeitl 381
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 382 dylrlsgreeqdialveayaktqglwhnphlepvyTDIVTLDLSSIKACIAGPKRPQDRVELsyltstfnqfltennrte 461
Cdd:cd01586 237 -----------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL------------------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 462 ekeksfitdsnfemhHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRKPWVKTSFAPGSQVVTRYLEETNLQKY 541
Cdd:cd01586 264 ---------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEASGLLPY 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179981458 542 LNELGFTLVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGT 616
Cdd:cd01586 329 LEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAGT 403
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
133-615 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 625.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 133 DHEIAYRPARVLMQDFTGVPAIVDLAAMRAAIKKLGGNSEQINPLSPVDLIIDHsiqvdeflTPNAFTVNAQMEMERNHE 212
Cdd:pfam00330 13 DGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDH--------APDALDKNIEDEISRNKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 213 RYEFLRWGQKAFkNFRVVPPDTGICHQINLEYLaktvwtqqingkiYAYPD-TLVGTDSHTTMINglgvlgwgvggIEAE 291
Cdd:pfam00330 85 QYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGglgalafgvggSEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 292 AAMLGQPISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATC 371
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 372 GFFPIDEITLDYLRLSGREEqdIALVEAYAKTQGLWHNPHLE-PVYTDIVTLDLSSIKACIAGPKRPQDRVELSyltSTF 450
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRPE--APKGEAYDKAVAWKTLASDPgAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLS---ELV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 451 NQFLTENNRTEEKEKSF---ITDSNFEMHHGDVVIAAITSCTNTSNPNVLVAAGLLaKKAVEKGITRKPWVKTSFAPGSQ 527
Cdd:pfam00330 306 PDPFADAVKRKAAERALeymGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASVVPGSE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 528 VVTRYLEETNLQKYLNELGFTLVGYGCTTCIGNSGPLLesvektviEHDLIVSavlSGNRNFEGRIHPLVKAnWLASPPL 607
Cdd:pfam00330 385 VVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP--------PGERCVS---SSNRNFEGRQGPGGRT-HLASPAL 452
|
....*...
gi 1179981458 608 VVAFALAG 615
Cdd:pfam00330 453 VAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
720-890 |
7.55e-113 |
|
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: 343.87 E-value: 7.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 720 LFGDSITTDHISPAGSIKPDSPAGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPDVEGGFTKHIPNNE 799
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 800 ILPIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGVTRKTLQ 879
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|.
gi 1179981458 880 ITGSELIDIVG 890
Cdd:cd01580 161 LTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
142-616 |
1.59e-86 |
|
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: 282.46 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 142 RVLMQDFTGVPAIVDLAAMRAAIKklggnseqINPLSPVDLIIDHSIQVDEfltpnaftvnaqmemERNHERYEFLRWGQ 221
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAVQLEK---------------PVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 222 KAFKnFRVVPPDTGICHQINLEYLAKtvwtqqingkiyaYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISL 301
Cdd:cd01351 58 ALQG-IAFYRPGVGIIHQIMVENLAL-------------PGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 302 LIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITL 381
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 382 DYLRLSGREEQDIaLVEAYAKTQglwhNPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSyltstfnqfltennrte 461
Cdd:cd01351 204 KWLEATGRPLLKN-LWLAFPEEL----LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVS----------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 462 ekeksfitdsnfEMHHGDVVIAAITSCTNtSNPNVLVAAGLLAKKAVEkgitrKPWVKTSFAPGSQVVTRYLEETNLQKY 541
Cdd:cd01351 262 ------------EVEGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGAKV-----APGVRLIVTPGSRMVYATLSREGYYEI 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179981458 542 LNELGFTLVGYGCTTCIGNSGPLLESVEKtviehdlivsAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAGT 616
Cdd:cd01351 324 LVDSGARILPPGCGPCMGNGARLVADGEV----------GVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGK 388
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
135-939 |
1.86e-83 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 282.42 E-value: 1.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 135 EIAYRPARVLMQDFTGVPAIVDLAAM---RAAIkklggnseqinPLSpVDLIiDHS-IQVDEfltpnaftvnaqmemeRN 210
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgldRVKT-----------ELS-VQYV-DHNlLQADF----------------EN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 211 HERYEFLrwgQKAFKNFRVV--PPDTGICHQINLEYlaktvwtqqingkiYAYP-DTLVGTDSHTT------MInglgvl 281
Cdd:PRK07229 75 ADDHRFL---QSVAAKYGIYfsKPGNGICHQVHLER--------------FAFPgKTLLGSDSHTPtagglgML------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 282 gwgvgGI-----EAEAAMLGQPISLLIPEVIGVKLVGQLQEGITATDLVLsitHLLRE---KGVVGKFVEYFGDGLRYLS 353
Cdd:PRK07229 132 -----AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL---ELLRRltvKGGVGKIIEYFGPGVATLS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 354 IADRATIGNMSPEYGATCGFFPIDEITLDYLRLSGREEqdiALVEAYAktqglwhNPhlEPVYTDIVTLDLSSIKACIAG 433
Cdd:PRK07229 204 VPERATITNMGAELGATTSIFPSDERTREFLKAQGRED---DWVELLA-------DP--DAEYDEVIEIDLSELEPLIAG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 434 PKRPQDRVELSyltstfnqfltennrtEEKEKsfitdsnfemhhgDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEkgit 513
Cdd:PRK07229 272 PHSPDNVVPVS----------------EVAGI-------------KVDQVLIGSCTNSSYEDLMRAASILKGKKVH---- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 514 rkpwVKTSF--APGSQVVTRYLEETNLQKYLNELGFTLVGYGCTTCIGNSGpllESVEKTVIehdlivsaVLSGNRNFEG 591
Cdd:PRK07229 319 ----PKVSLviNPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNVS--------LRTFNRNFPG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 592 RI-HPLVKAnWLASPPLVVAFALAGttliDLTkDPLgKDASGNPVYLKDIWPTNAEiacevakISRNMFhdtyahIFEGT 670
Cdd:PRK07229 384 RSgTKDAQV-YLASPETAAASALTG----VIT-DPR-TLALENGEYPKLEEPEGFA-------VDDAGI------IAPAE 443
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 671 DEwRAMKISKSDTyawpvnstyIQHPPYFDEMnvnpekiKEIKGARILALFGDSITTDHISPAGSikpdspagKYLqskg 750
Cdd:PRK07229 444 DG-SDVEVVRGPN---------IKPLPLLEPL-------PDLLEGKVLLKVGDNITTDHIMPAGA--------KWL---- 494
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 751 vsikdfnSYgsrRGNHEVMMRGTFanIRIRNEmtpdveggFTKHIpnneilpiydaamrykKERTALVIIAGKEYGTGSS 830
Cdd:PRK07229 495 -------PY---RSNIPNISEFVF--EGVDNT--------FPERA----------------KEQGGGIVVGGENYGQGSS 538
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 831 RDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEF--PEGVTRktlqITGSELIDIVGLThEMKPRMQVKVIIHNE 908
Cdd:PRK07229 539 REHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFadPADYDK----IEEGDVLEIEDLR-EFLPGGPLTVVNVTK 613
|
810 820 830
....*....|....*....|....*....|...
gi 1179981458 909 DKtqnEIHLILridTLNE--LDYYKNGGILHYV 939
Cdd:PRK07229 614 DE---EIEVRH---TLSErqIEILLAGGALNLI 640
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
742-872 |
1.54e-54 |
|
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: 185.26 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 742 AGKYLQSKGVSIKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPDVEGGFTKHIPNNEILPIYDAAMRYKKERTALVIIA 821
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1179981458 822 GKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEG 872
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
232-615 |
3.18e-47 |
|
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: 173.40 E-value: 3.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 232 PDTGICHQINLEYLAKTvwtqqinGKiyaypdTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISLLIPEVIGVKL 311
Cdd:cd01585 66 PGNGICHQVHLERFAVP-------GK------TLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 312 VGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDYLRLSGREE 391
Cdd:cd01585 133 TGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRED 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 392 QDIALVeayaktqglwhnPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTfnqfltennrteekeksfitds 471
Cdd:cd01585 213 DWVELA------------ADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREVAGI---------------------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 472 nfemhhgDVVIAAITSCTNTSNPNVLVAAGLLAKKAVEkgitrkPWVKTSFAPGSQVVTRYLEETNLQKYLNELGFTLVG 551
Cdd:cd01585 259 -------KVDQVAIGSCTNSSYEDLMTVAAILKGRRVH------PHVSMVVAPGSKQVLEMLARNGALADLLAAGARILE 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179981458 552 YGCTTCIG-NSGPLLESVektviehdlivsAVLSGNRNFEGRIHPLVKANWLASPPLVVAFALAG 615
Cdd:cd01585 326 SACGPCIGmGQAPPTGGV------------SVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTG 378
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
142-617 |
1.28e-45 |
|
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: 169.54 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 142 RVLMQDFTGVPAIvdLAAMRAAIKKlggnseqinPLSPVDLIIDHSIQVDefltpnaftVNAQMEMER----NHERYEFL 217
Cdd:cd01584 1 RVAMQDATAQMAL--LQFMSSGLPK---------VAVPSTIHCDHLIEAQ---------VGGEKDLKRakdiNKEVYDFL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 218 RWGQKAFkNFRVVPPDTGICHQINLEYlaktvwtqqingkiYAYPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 296
Cdd:cd01584 61 ASAGAKY-GIGFWKPGSGIIHQIVLEN--------------YAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 297 QPISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPI 376
Cdd:cd01584 126 IPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 377 DEITLDYLRLSGREEqdialVEAYAKtqgLWHNPHLEP----VYTDIVTLDLSSIKACIAGPKRPqdrvELSYLTSTFNQ 452
Cdd:cd01584 206 NERMKKYLKATGRAE-----IADLAD---EFKDDLLVAdegaEYDQLIEINLSELEPHINGPFTP----DLATPVSKFKE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 453 FLTENNRTEekeksfitdsnfemhhgDVVIAAITSCTNTSNPNVLVAAGlLAKKAVEKGItrKPWVKTSFAPGSQVVTRY 532
Cdd:cd01584 274 VAEKNGWPL-----------------DLRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGL--KCKSIFTITPGSEQIRAT 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 533 LEETNLQKYLNELGFTLVGYGCTTCIGN-SGPLLESVEKTVIehdlivsaVLSGNRNFEGR--IHPLVKAnWLASPPLVV 609
Cdd:cd01584 334 IERDGLLQTFRDAGGIVLANACGPCIGQwDRKDIKKGEKNTI--------VTSYNRNFTGRndANPATHA-FVASPEIVT 404
|
....*...
gi 1179981458 610 AFALAGTT 617
Cdd:cd01584 405 AMAIAGTL 412
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
142-615 |
2.08e-43 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 162.36 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 142 RVLMQDFTGVPAIvdlAAMRAAIKKLGGNSEQINplspvdLIIDHSIQvdeflTPNAFTVNAQMEMERNheryeFLRWGQ 221
Cdd:cd01583 1 LHLVHDVTSPQAF---EGLREAGREKVWDPEKIV------AVFDHNVP-----TPDIKAAEQVKTLRKF-----AKEFGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 222 KAFKNFRvvppdTGICHQInleyLAKTVWTQqingkiyayP-DTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPIS 300
Cdd:cd01583 62 NFFDVGR-----QGICHVI----LPEKGLTL---------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLW 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 301 LLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEIT 380
Cdd:cd01583 124 FRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 381 LDYLRLSGREEQDIALVEAYAKtqglwhnphlepvYTDIVTLDLSSIKACIAGPKRPQDRVELSyltstfnqfltennrt 460
Cdd:cd01583 204 FEYLKGRGKAYWKELKSDEDAE-------------YDKVVEIDASELEPQVAWPHSPDNVVPVS---------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 461 eEKEKSFItdsnfemhhgDVVIaaITSCTNTSNPNVLVAAGLLakkaveKGITRKPWVKTSFAPGSQVVTRYLEETNLQK 540
Cdd:cd01583 255 -EVEGIKI----------DQVF--IGSCTNGRLEDLRAAAEIL------KGRKVADGVRLIVVPASQRVYKQAEKEGLIE 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179981458 541 YLNELGFTLVGYGCTTCIGNSGPLLEsvektviEHDLIVSavlSGNRNFEGRIHPLVKANWLASPPLVVAFALAG 615
Cdd:cd01583 316 IFIEAGAEVRPPGCGACLGGHMGVLA-------PGERCVS---TSNRNFKGRMGSPGARIYLASPATAAASAITG 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
142-615 |
2.19e-41 |
|
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: 157.50 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 142 RVLMQDFTGVPAIVDLaamraaikklggnsEQINPLSPVD-----LIIDHSIQvdeflTPNAFTVNAQMEMERNHERY-- 214
Cdd:COG0065 30 LHLVHDVTSPQAFEGL--------------REAGGRKVWDpdrivAVFDHNVP-----TKDPKSAEQVKTLREFAKEFgi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 215 EFLRWGqkafknfrvvppDTGICHQINLEylaktvwtqqingKIYAYP-DTLVGTDSHTTM----------INGLgvlgw 283
Cdd:COG0065 91 TFFDVG------------DPGICHVVLPE-------------QGLVLPgMTIVGGDSHTCThgafgafafgIGTT----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 284 gvggiEAEAAMLGQPISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNM 363
Cdd:COG0065 141 -----DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 364 SPEYGATCGFFPIDEITLDYLRlsGReeqdialveAYAKTQGLWHNPhlEPVYTDIVTLDLSSIKACIAGPKRPQDRVEL 443
Cdd:COG0065 216 AIEAGAKAGIIAPDETTFEYLK--GR---------PFAPWRTLKSDE--DAVYDKEVEIDASDLEPQVAWPHSPDNVVPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 444 SyltstfnqfltennrteekeksfitdsnfEMhhGDVVI--AAITSCTNTSNPNVLVAAGLLAKKAVekgitrKPWVKTS 521
Cdd:COG0065 283 S-----------------------------EL--EGIKIdqVFIGSCTNGRIEDLRAAAEILKGRKV------APGVRAI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 522 FAPGSQVVTRYLEETNLQKYLNELGFTLVGYGCTTCIGNSGPLLESVEKTviehdliVSavlSGNRNFEGR-------IH 594
Cdd:COG0065 326 VVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERC-------AS---TSNRNFEGRmgspgsrTY 395
|
490 500
....*....|....*....|.
gi 1179981458 595 plvkanwLASPPLVVAFALAG 615
Cdd:COG0065 396 -------LASPATAAASAIAG 409
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
143-615 |
2.69e-34 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 136.46 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 143 VLMQDFTGVPAIvdlaamrAAIKKLGGnsEQINPLSPVDLIIDHsiqvdefLTPNAfTVNA--QMEMERnheryEFLRwg 220
Cdd:PRK00402 31 VMAHDITGPLAI-------KEFEKIGG--DKVFDPSKIVIVFDH-------FVPAK-DIKSaeQQKILR-----EFAK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 221 QKAFKNFRVVPpdTGICHQINLEylaktvwtqqingKIYAYP-DTLVGTDSHTT----------------Minglgvlgw 283
Cdd:PRK00402 87 EQGIPNFFDVG--EGICHQVLPE-------------KGLVRPgDVVVGADSHTCtygalgafatgmgstdM--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 284 gvggieAEAAMLGQpISLLIPEVIGVKLVGQLQEGITATDLVLsitHLLREKGVVG---KFVEYFGDGLRYLSIADRATI 360
Cdd:PRK00402 143 ------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVIL---HIIGDIGVDGatyKALEFTGETIEALSMDERMTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 361 GNMSPEYGATCGFFPIDEITLDYLRlsGREEQDIALVEAYAktqglwhnphlEPVYTDIVTLDLSSIKACIAGPkrpqdr 440
Cdd:PRK00402 213 ANMAIEAGAKAGIFAPDEKTLEYLK--ERAGRDYKPWKSDE-----------DAEYEEVYEIDLSKLEPQVAAP------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 441 velsyltstfnqFLTENNRT-EEKEKSFItdsnfemhhgDVVIaaITSCTNTSNPNVLVAAGLLAKKAVekgitrKPWVK 519
Cdd:PRK00402 274 ------------HLPDNVKPvSEVEGTKV----------DQVF--IGSCTNGRLEDLRIAAEILKGRKV------APGVR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 520 TSFAPGSQVVTRYLEETNLQKYLNELGFTLVGYGCTTCIGNSGPLLESVEKtviehdlivsAVLSGNRNFEGRI-HPlvK 598
Cdd:PRK00402 324 LIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEV----------CLSTTNRNFKGRMgSP--E 391
|
490
....*....|....*...
gi 1179981458 599 AN-WLASPPLVVAFALAG 615
Cdd:PRK00402 392 SEvYLASPAVAAASAVTG 409
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
139-615 |
8.84e-34 |
|
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: 134.89 E-value: 8.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 139 RPARVLMQDFTGVPAIvdlaamrAAIKKLGgnseQINPLSP--VDLIIDHSIQvdeflTPNAFTVNAQMEMErnheryEF 216
Cdd:TIGR02086 25 EVDLAMTHDGTGPLAI-------KALRELG----VARVWDPekIVIAFDHNVP-----PPTVEAAEMQKEIR------EF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 217 LRwgQKAFKNFRVvppDTGICHQINLEylaktvwtqqingKIYAYP-DTLVGTDSHTTMINGLGVLGWGVGGIE-AEAAM 294
Cdd:TIGR02086 83 AK--RHGIKNFDV---GEGICHQILAE-------------EGYALPgMVVVGGDSHTCTSGAFGAFATGMGATDmAIALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 295 LGQpISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFF 374
Cdd:TIGR02086 145 TGK-TWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGII 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 375 PIDEITLDYLRLSGREEQDIAlveayaktqglwhNPHLEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSyltstfnqfl 454
Cdd:TIGR02086 224 EPDEETYEYLKKRRGLEFRIL-------------VPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVS---------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 455 tennrteEKEKSFItDSNFemhhgdvviaaITSCTNTSNPNVLVAAGLLAKKAVEkgitrkPWVKTSFAPGS-QVVTRYL 533
Cdd:TIGR02086 281 -------DVEGTEI-DQVF-----------IGSCTNGRLEDLRIAAEILKGRRVH------PDVRLIVIPASrKVYLRAL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 534 EETNLQkylnelgfTLVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSavlSGNRNFEGRI-HPLVKAnWLASPPLVVAFA 612
Cdd:TIGR02086 336 EEGIIL--------TLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLS---TTNRNFKGRMgSPNAEI-YLASPATAAASA 403
|
...
gi 1179981458 613 LAG 615
Cdd:TIGR02086 404 VEG 406
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
231-615 |
1.19e-26 |
|
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: 112.71 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 231 PPDTGICHQINLEylaktvwtqqingKIYAYPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISLLIPEVIGV 309
Cdd:cd01582 64 PAGRGIGHQIMIE-------------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 310 KLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDeitldylrlsgr 389
Cdd:cd01582 131 ELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD------------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 390 eeqdialveayAKtqglwhnpHLepvytdivTLDLSSIKACIAGPKrpqdrvelSYLTSTFNQFLTENNRTEEKeksfit 469
Cdd:cd01582 199 -----------AK--------HL--------ILDLSTLSPYVSGPN--------SVKVSTPLKELEAQNIKINK------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 470 dsnfemhhgdvviAAITSCTNTSNPNVLVAAGLLAKKAVEKGITRK-PWVKTSFAPGSQVVTRYLEETNLQKYLNELGFT 548
Cdd:cd01582 238 -------------AYLVSCTNSRASDIAAAADVVKGKKEKNGKIPVaPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGAT 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179981458 549 LVGYGCTTCIGNSGPLLESVEktviehdLIVSAVlsgNRNFEGRIHPLVKANWLASPPLVVAFALAG 615
Cdd:cd01582 305 PLPAGCGPCIGLGQGLLEPGE-------VGISAT---NRNFKGRMGSTEALAYLASPAVVAASAISG 361
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
143-615 |
1.72e-26 |
|
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: 113.31 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 143 VLMQDFTGVPAIvdlaamrAAIKKLGGNSeqinPLSP--VDLIIDHSIQvdeflTPNAFTVNAQMEMernherYEFLRwg 220
Cdd:TIGR01343 28 AMVHDITAPLAI-------KTLEEYGIDK----VWNPekIVIVFDHQVP-----ADTIKAAEMQKLA------REFVK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 221 QKAFKNFRvvPPDTGICHQINLEylaktvwtqqingKIYAYP-DTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPI 299
Cdd:TIGR01343 84 KQGIKYFY--DVGEGICHQVLPE-------------KGLVKPgDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 300 SLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEI 379
Cdd:TIGR01343 149 WFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 380 TLDYLRLSGREEQDIALVEAYAKtqglwhnphlepvYTDIVTLDLSSIKACIAGPKRPQDRVELSyltstfnqfltennr 459
Cdd:TIGR01343 229 TIQYLKERRKEPFRVYKSDEDAE-------------YAKEIEIDASQIEPVVACPHNVDNVKPVS--------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 460 teekeksfitdsnfEMHHGDVVIAAITSCTNTSNPNVLVAAGLLAKKAVekgitrKPWVKTSFAPGSQVVtrYLEEtnLQ 539
Cdd:TIGR01343 281 --------------EVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKV------APDVRLIVIPASRAV--YLQA--LK 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1179981458 540 KYLNElgfTLVGYGCTTCIGNSGPLLESVEKTVIEHDLIVSavlSGNRNFEGRIHPLVKANWLASPPLVVAFALAG 615
Cdd:TIGR01343 337 EGLIE---IFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCIS---TSNRNFKGRMGHPNAEIYLASPATAAASAVKG 406
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
304-615 |
9.98e-23 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 102.51 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 304 PEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITLDY 383
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEY 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 384 LRlsGR------EEQDIALveAYaktqglWHNPHLEP--VYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTSTFNQFLT 455
Cdd:PRK05478 243 LK--GRpfapkgEDWDKAV--AY------WKTLKSDEdaVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFAD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 456 ENNRtEEKEKSF----------ITDSNFemhhgDVVIaaITSCTNTSNPNVLVAAGLLAKKAVEKGItrKPWVktsfAPG 525
Cdd:PRK05478 313 PVKR-ASAERALaymglkpgtpITDIKI-----DKVF--IGSCTNSRIEDLRAAAAVVKGRKVAPGV--RALV----VPG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 526 SQVVTRYLEETNLQKYLNELGFTLVGYGCTTCIG-NsgpllesvEKTVIEHDLIVSavlSGNRNFEGR------IHplvk 598
Cdd:PRK05478 379 SGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmN--------PDKLPPGERCAS---TSNRNFEGRqgkggrTH---- 443
|
330
....*....|....*..
gi 1179981458 599 anwLASPPLVVAFALAG 615
Cdd:PRK05478 444 ---LVSPAMAAAAAITG 457
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
815-890 |
4.49e-22 |
|
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: 91.38 E-value: 4.49e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1179981458 815 TALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPegVTRKTLQITGSELIDIVG 890
Cdd:cd00404 15 GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFA--DPEDYLKLHTGDELDIYP 88
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
289-615 |
4.83e-21 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 97.67 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 289 EAEAAMLGQPISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVVGKFVEYFGDGLRYLSIADRATIGNMSPEYG 368
Cdd:PRK12466 150 EVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 369 ATCGFFPIDEITLDYLRLSGREEQDIALVEAYAKTQGLWHNPhlEPVYTDIVTLDLSSIKACIAGPKRPQDRVELSYLTS 448
Cdd:PRK12466 230 ARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDA--DAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 449 TFNQFLTENNRTEEKEKSFITDSNFEMHHGDVVI--AAITSCTNTSNPNVLVAAGLLAKKAVEKGITrkPWVktsfAPGS 526
Cdd:PRK12466 308 DPAAEADPARRAAMERALDYMGLTPGTPLAGIPIdrVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVR--AMV----VPGS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 527 QVVTRYLEETNLQKYLNELGFTLVGYGCTTCIGNSGPLLESVEKtviehdlivsAVLSGNRNFEGRIHPLVKANwLASPP 606
Cdd:PRK12466 382 GAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGER----------CASTTNRNFEGRQGPGARTH-LMSPA 450
|
....*....
gi 1179981458 607 LVVAFALAG 615
Cdd:PRK12466 451 MVAAAAVAG 459
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
722-871 |
1.57e-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: 82.10 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 722 GDSITTDHISPAGSikpdspagKYLqskgvsikdfnsygSRRGNHEVMMRGTFANIRirnemtpdveggftkhipnneil 801
Cdd:cd01579 3 GDNITTDHIMPAGA--------KVL--------------PLRSNIPAISEFVFHRVD----------------------- 37
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 802 PIYDAAMrykKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPE 871
Cdd:cd01579 38 PTFAERA---KAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFAD 104
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
726-892 |
1.44e-15 |
|
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: 74.81 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 726 TTDHISPAGsikpdsPAGKYlqskgvsikdfnsygsrRGNHEV----MMRGTfanIRIRNEMTPDVEGGFTkhipnNEIL 801
Cdd:cd01578 7 TTDHISAAG------PWLKY-----------------RGHLDNisnnLLIGA---INAENGKANSVKNQVT-----GEYG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 802 PIYDAAMRYKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGVTRKtlQIT 881
Cdd:cd01578 56 PVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYD--KIH 133
|
170
....*....|.
gi 1179981458 882 GSELIDIVGLT 892
Cdd:cd01578 134 PDDKVDILGLT 144
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
707-876 |
2.33e-15 |
|
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: 75.59 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 707 EKIKEIKGaRILALFGDSITTDHISPAgsikpdspagKYLqsKGVSIKDFnsygsrrGNHevmmrgTFANIRIRNEMTPD 786
Cdd:COG0066 1 EKFTTLTG-RAVPLDGDNIDTDQIIPA----------RFL--KTIDREGL-------GKH------LFEDWRYDRSPDPD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 787 veggftkHIPNNEilpiydaamRYKKertALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILP 866
Cdd:COG0066 55 -------FVLNQP---------RYQG---ADILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLP 115
|
170
....*....|
gi 1179981458 867 LEFPEGVTRK 876
Cdd:COG0066 116 IELPEEAVDA 125
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
818-887 |
3.68e-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: 62.99 E-value: 3.68e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179981458 818 VIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGVTRKTLQITGSEL-ID 887
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDEVeVD 90
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
810-941 |
1.51e-11 |
|
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: 63.21 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 810 YKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPegvtrkTLQITGSELIDIV 889
Cdd:TIGR02087 42 AKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIEAK------TEGIKDGDEVTVD 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1179981458 890 GLTHEmkprmqvkvIIHNEDKtqneihlILRIDTLNE--LDYYKNGGILHYVLR 941
Cdd:TIGR02087 116 LETGE---------IRVNGNE-------EYKGEPLPDflLEILREGGLLEYLKK 153
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
230-508 |
1.72e-11 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 68.11 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 230 VPPDTGICHQINLEYLAKTvwtqqinGKIyaypdtLVGTDSHT------TMinglgvlgwgvgGI-----EAEAAMLGQP 298
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG-------GKM------ILGSDSHTrygalgTM------------AVgegggELVKQLLNDT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 299 ISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVV-GKFVEYFGDGLRYLSIADRATIGNMSPEygATC--GFFP 375
Cdd:PRK11413 178 YDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 376 IDEITLDYLRLSGREeqdialvEAYAKTqglwhNPHlEPVYTD-IVTLDLSSIKACIAGPKRPQDrvelSYLTSTFNQFL 454
Cdd:PRK11413 256 TDEEVHNWLALHGRG-------QDYCEL-----NPQ-PMAYYDgCISVDLSAIKPMIALPFHPSN----VYEIDELNQNL 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1179981458 455 TENNRTEEKEKSFITDSNFEMHHGDVVI--------AAITSCTNTSNPNVLVAAGLLAKKAV 508
Cdd:PRK11413 319 TDILREVEIESERVAHGKAKLSLLDKIEngrlkvqqGIIAGCSGGNYENVIAAANALRGQSC 380
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
721-873 |
2.67e-11 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 62.92 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 721 FGDSITTDHISPagsikpdspaGKYLQSKgvsikdfnsygsrrgNHEVMMRGTFANIRirnemtPDveggFTKHIPNNEI 800
Cdd:PRK00439 7 FGDNIDTDVIIP----------ARYLNTS---------------DPQELAKHCMEDLD------PE----FAKKVKPGDI 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1179981458 801 lpiydaamrykkertalvIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGV 873
Cdd:PRK00439 52 ------------------IVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAV 106
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
715-871 |
3.48e-11 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 62.51 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 715 ARILAlFGDSITTDHISPagsikpdspaGKYLQSKgVSIKDFNSYgsrrgnhevmmrgtfANIRIRNEMTPDVeggftkh 794
Cdd:PRK14023 2 ARVWK-FGDNINTDDILP----------GKYAPFM-VGEDRFHNY---------------AFAHLRPEFASTV------- 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179981458 795 ipnneilpiydaamrykkeRTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPE 871
Cdd:PRK14023 48 -------------------RPGDILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEE 105
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
707-871 |
4.30e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 51.28 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 707 EKIKEIKGaRILALFGDSITTDHISPAgsikpdspagKYLQSkgvsIKdFNSYGsrrgnhevmmRGTFANIRIRNEMTPD 786
Cdd:PRK01641 2 EKFTTHTG-LAVPLDRANVDTDQIIPK----------QFLKR----IT-RTGFG----------KGLFDDWRYLDDGQPN 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 787 VEggftkHIPNNEilpiydaamRYKKertALVIIAGKEYGTGSSRD---WAakgpkLQ--GVVAVIAESFERIHRSNLIG 861
Cdd:PRK01641 56 PD-----FVLNQP---------RYQG---ASILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFK 113
|
170
....*....|
gi 1179981458 862 MGILPLEFPE 871
Cdd:PRK01641 114 NGLLPIVLPE 123
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
818-897 |
5.24e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.01 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 818 VIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMG-ILPLEFPEGVTRK-------TLQITGSELID-I 888
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLESEVRICEEcktgdvvTVELGNSVLINhT 211
|
....*....
gi 1179981458 889 VGLTHEMKP 897
Cdd:PLN00072 212 TGKEYKLKP 220
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
262-617 |
1.05e-04 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 45.95 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 262 PDTL-VGTDSHTTMinGLGVLGWGVGGIEAEAAMLGQpISLLIPEVIGVKLVGQLQEGITATDLVLSITHLLREKGVV-- 338
Cdd:cd01581 106 PDTVgTGGDSHTRF--PIGISFPAGSGLVAFAAATGV-MPLDMPESVLVRFKGKMQPGITLRDLVNAIPYYAIQQGLLtv 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 339 ----------GKFVEYfgDGLRYLSIADRATIGNMSPEYGATCGFFPIDEITL-DYLRlSGREEQDIALVEAY------- 400
Cdd:cd01581 183 ekkgkknvfnGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLE-SNVVLMKIMIANGYddartll 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 401 ----AKTQGLWHNPHLEP----VYTDIVTLDLSSIK-ACIAGPKRPQDRVELSYLtstfnqfltennrteekeksfitds 471
Cdd:cd01581 260 rriiAMEEWLANPPLLEPdadaEYAAVIEIDLDDIKePILACPNDPDDVKLLSEV------------------------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981458 472 nfemhHGDVV-IAAITSCTnTSNPNVLVAAGLLAKKAVEKGITrkpWVktsfAPGSQVVTRYLEETNLQKYLNELGFTLV 550
Cdd:cd01581 315 -----AGKKIdEVFIGSCM-TNIGHFRAAAKILRGKEFKPTRL---WV----APPTRMDWAILQEEGYYSIFGDAGARTE 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179981458 551 GYGCTTCIGNsgpllesvEKTVIEHDLIVSavlSGNRNFEGRIHPLVKAnWLASPPLVVAFALAGTT 617
Cdd:cd01581 382 MPGCSLCMGN--------QARVADGATVFS---TSTRNFDNRVGKGAEV-YLGSAELAAVCALLGRI 436
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
804-875 |
2.34e-04 |
|
Homoaconitase swivel domain. This family includes 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. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238837 [Multi-domain] Cd Length: 129 Bit Score: 41.89 E-value: 2.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1179981458 804 YDAAMRyKKERTALVIIAGKEYGTGSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGVTR 875
Cdd:cd01674 35 YDSEFS-TKTKQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGNIFSRNSINNALLSIELPFLVQK 105
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
828-888 |
3.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 38.16 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179981458 828 GSSRDWAAKGPKLQGVVAVIAESFERIHRSNLIGMGILPLEFPEGVTRKTLQITGSELIDI 888
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTV 63
|
|
| |
