|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
2-889 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1639.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 2 SNPFAHLAEPLdPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPA 81
Cdd:PTZ00092 13 PNPFEKVLKTL-KDGGSYKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGS 161
Cdd:PTZ00092 92 RVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 162 QAFHNMRIIPPGSGIIHQVNLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:PTZ00092 172 KAFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 242 VIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLV 321
Cdd:PTZ00092 252 VVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 322 QTGRDEEKLKYIKKYLQAVGMFRDFNDpsqDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKG 401
Cdd:PTZ00092 332 QTGRSEEKVELIEKYLKANGLFRTYAE---QIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 402 FQVAPEHHNDHKTFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTYY 481
Cdd:PTZ00092 409 FGIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKY 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 482 LQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYA 561
Cdd:PTZ00092 489 LEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYA 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 562 IAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKST 641
Cdd:PTZ00092 569 LAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKST 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 642 YIKSPPFFENLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMAR 721
Cdd:PTZ00092 649 YIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVR 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 722 GTFANIRLLNRFLNKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYE 801
Cdd:PTZ00092 729 GTFANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFE 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 802 RIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIPE-NLKPQMKVQVKLDTGKTFQAVMRFDTDVELTYFLNGGIL 880
Cdd:PTZ00092 809 RIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGIL 888
|
....*....
gi 1384865994 881 NYMIRKMAK 889
Cdd:PTZ00092 889 QYVLRKLVK 897
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
17-889 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1524.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 17 PGKK--FFNLNKLEDSRYG---RLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGV 91
Cdd:PRK09277 16 GGKSydYYSLRALEAKGLGdisRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIPFRPARVVMQDFTGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 92 PAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIP 171
Cdd:PRK09277 96 PAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFLKWGQKAFDNFRVVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 172 PGSGIIHQVNLEYLARVVF-DQDG--YYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLM 248
Cdd:PRK09277 176 PGTGICHQVNLEYLAPVVWtREDGelVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 249 GKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLVQTGRDEE 328
Cdd:PRK09277 256 GKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 329 KLKYIKKYLQAVGMFRDfndPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEh 408
Cdd:PRK09277 336 QVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQGFGLDEAEE- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 409 hndhktfiydNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVM 488
Cdd:PRK09277 412 ----------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 489 PYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRI 568
Cdd:PRK09277 482 PYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDI 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 569 DFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPF 648
Cdd:PRK09277 562 DLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPY 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 649 FENLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIR 728
Cdd:PRK09277 642 FEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIR 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 729 LLNRFLN-KQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSN 807
Cdd:PRK09277 722 IRNEMVPgVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSN 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 808 LVGMGVIPLEYLPGENADALGLTGQERYTIIIPENLKPQMKVQVKL--DTG--KTFQAVMRFDTDVELTYFLNGGILNYM 883
Cdd:PRK09277 802 LVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGATVTVVItrADGevVEFPVLCRIDTAVEVDYYRNGGILQYV 881
|
....*.
gi 1384865994 884 IRKMAK 889
Cdd:PRK09277 882 LRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
21-889 |
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: 1511.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 21 FFNLNKLEDSRYG--RLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFA 98
Cdd:COG1048 20 YYSLPALEEAGGDisRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVLMQDFTGVPAVVDLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 99 AMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIPPGSGIIH 178
Cdd:COG1048 100 AMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAFDNFRVVPPGTGIVH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 179 QVNLEYLARVVF--DQDG--YYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPL 254
Cdd:COG1048 180 QVNLEYLAFVVWtrEEDGetVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 255 VTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLVQTGRDEEKLKYIK 334
Cdd:COG1048 260 VTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIELVE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 335 KYLQAVGMFRDfnDPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGfkgfqvapEHHNDHKT 414
Cdd:COG1048 340 AYAKAQGLWRD--PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG--------EELDKPVR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 415 FIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQL 494
Cdd:COG1048 410 VEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEAL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 495 GFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRIDFEKEP 574
Cdd:COG1048 490 GFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLTTDP 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 575 LGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFENLTL 654
Cdd:COG1048 570 LGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEGLQL 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 655 DLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIRLLNRFL 734
Cdd:COG1048 650 EPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKNLLA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 735 -NKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGV 813
Cdd:COG1048 730 pGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGV 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 814 IPLEYLPGENADALGLTGQERYTII-IPENLKPQMKVQVKLD----TGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMA 888
Cdd:COG1048 810 LPLQFPEGESAESLGLTGDETFDIEgLDEGLAPGKTVTVTATradgSTEEFPVLHRIDTPVEVEYYRAGGILQYVLRQLL 889
|
.
gi 1384865994 889 K 889
Cdd:COG1048 890 A 890
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
2-889 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1384.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 2 SNPFAHLAEPLDPVQPGK--KFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFK 79
Cdd:PLN00070 42 ENPFKGILTSLPKPGGGEfgKYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 80 PARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKW 159
Cdd:PLN00070 122 PARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 160 GSQAFHNMRIIPPGSGIIHQVNLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVL 239
Cdd:PLN00070 202 GSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 240 PQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITY 319
Cdd:PLN00070 282 PGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 320 LVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGF 399
Cdd:PLN00070 362 LKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGF 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 400 KGFQVAPEHHNDHKTFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVT 479
Cdd:PLN00070 442 KGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVT 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 480 YYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:PLN00070 522 KYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVA 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 560 YAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSK 639
Cdd:PLN00070 602 YALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 640 STYIKSPPFFENLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVM 719
Cdd:PLN00070 682 STYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIM 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 720 ARGTFANIRLLNRFLNKQ-APQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAE 798
Cdd:PLN00070 762 ARGTFANIRIVNKLLKGEvGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAK 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 799 SYERIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIPENL---KPQMKVQVKLDTGKTFQAVMRFDTDVELTYFL 875
Cdd:PLN00070 842 SFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNIseiKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFD 921
|
890
....*....|....
gi 1384865994 876 NGGILNYMIRKMAK 889
Cdd:PLN00070 922 HGGILPYVIRNLIK 935
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
21-887 |
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: 1329.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 21 FFNLNKLEDS--RYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFA 98
Cdd:TIGR01341 5 YYSLKALEESggKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAVVDLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 99 AMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIPPGSGIIH 178
Cdd:TIGR01341 85 AMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGTGIIH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 179 QVNLEYLARVVF----DQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPL 254
Cdd:TIGR01341 165 QVNLEYLATVVFkaevDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 255 VTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLVQTGRDEEKLKYIK 334
Cdd:TIGR01341 245 VTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVELVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 335 KYLQAVGMFRDFndpSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHhndhKT 414
Cdd:TIGR01341 325 KYARAQGLFYDD---SEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEP----LK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 415 FIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQL 494
Cdd:TIGR01341 398 KKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEEL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 495 GFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRIDFEKEP 574
Cdd:TIGR01341 478 GFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 575 LGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFENLTL 654
Cdd:TIGR01341 558 IGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 655 DLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIRLLNRFL 734
Cdd:TIGR01341 638 DPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMV 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 735 -NKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGV 813
Cdd:TIGR01341 718 kGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGV 797
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865994 814 IPLEYLPGENADALGLTGQERYTIIIPENLKPQMKVQVKLDTGK----TFQAVMRFDTDVELTYFLNGGILNYMIRKM 887
Cdd:TIGR01341 798 IPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
11-889 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1308.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 11 PLDPVQPGKK---FFNLNKLE---DSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPARVI 84
Cdd:PRK12881 8 TLKEFDVGGKtykFYSLPALGkelGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIPFVPARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 85 LQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAF 164
Cdd:PRK12881 88 MQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 165 HNMRIIPPGSGIIHQVNLEYLARVVF----DQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLP 240
Cdd:PRK12881 168 DNFRVVPPGTGIMHQVNLEYLARVVHtkedDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 241 QVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYL 320
Cdd:PRK12881 248 DVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 321 VQTGRDEEKLKYIKKYLQAVGMFRDfndPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFK 400
Cdd:PRK12881 328 RLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAEN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 401 GFQVAPEHHNDHktfiydntefTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTY 480
Cdd:PRK12881 405 GFAKKAQTSNGV----------DLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 481 YLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAY 560
Cdd:PRK12881 475 YLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAY 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 561 AIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKS 640
Cdd:PRK12881 555 ALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKS 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 641 TYIKSPPFFENLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMA 720
Cdd:PRK12881 635 TYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMM 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 721 RGTFANIRLLNRFL-NKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAES 799
Cdd:PRK12881 715 RGTFANVRIKNLMIpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAES 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 800 YERIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTII-IPENLKPQMKVQVKLDTG----KTFQAVMRFDTDVELTYF 874
Cdd:PRK12881 795 FERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRQDVTLVIHRAdgstERVPVLCRIDTPIEVDYY 874
|
890
....*....|....*
gi 1384865994 875 LNGGILNYMIRKMAK 889
Cdd:PRK12881 875 KAGGILPYVLRQLLA 889
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
82-566 |
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: 830.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGS 161
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 162 QAFHNMRIIPPGSGIIHQVNLEYLARVVF----DQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISM 237
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 238 VLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDevsi 317
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 318 tylvqtgrdeeklkyikkylqavgmfrdfndpsqdpdfTQVVELDLKTVVPCCSGPKRPQDKVAVsdmkkdfesclgakq 397
Cdd:cd01586 237 --------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 398 gfkgfqvapehhndhktfiydnteftlaHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGV 477
Cdd:cd01586 264 ----------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 478 VTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLV 557
Cdd:cd01586 316 VTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLV 395
|
....*....
gi 1384865994 558 IAYAIAGTI 566
Cdd:cd01586 396 VAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
61-564 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 668.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 61 ENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSiqvdfnrrADSLQ 140
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 141 KNQDLEFERNRERFEFLKWGSQAFhNMRIIPPGSGIIHQVNLEYlarvvfdqdGYYYPD-SLVGTDSHTTMIDGLGILGW 219
Cdd:pfam00330 73 KNIEDEISRNKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEY---------GLALPGmTIVGTDSHTTTHGGLGALAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 220 GVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANM 299
Cdd:pfam00330 143 GVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 300 CPEYGATAAFFPVDEVSITYLVQTGRDEEKLkyIKKYLQAVGMFRDFNDPsqDPDFTQVVELDLKTVVPCCSGPKRPQDK 379
Cdd:pfam00330 223 AIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDP--GAEYDKVVEIDLSTIEPMVTGPTRPQDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 380 VAVSDMKKD-FESCLGAKQGFKGFQvapehhndhktFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLaKKAVD 458
Cdd:pfam00330 299 VPLSELVPDpFADAVKRKAAERALE-----------YMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 459 AGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEpvveaitqGDlvaVGVLSGNRNF 538
Cdd:pfam00330 367 KGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--------GE---RCVSSSNRNF 435
|
490 500
....*....|....*....|....*.
gi 1384865994 539 EGRVHPNTRAnYLASPPLVIAYAIAG 564
Cdd:pfam00330 436 EGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
670-839 |
4.59e-111 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 337.71 E-value: 4.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 670 NLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIRLLNRFLNKQAPQTIHLPS-GE 748
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPtGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 749 ILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALG 828
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|.
gi 1384865994 829 LTGQERYTIII 839
Cdd:cd01580 161 LTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
82-566 |
1.43e-108 |
|
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: 339.47 E-value: 1.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAVVDFAAMRDAVKklggdpekINPVCPADLVIDHSIQvdfnrradslqknqdLEFERNRERFEFLKWgS 161
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 162 QAFHNMRIIPPGSGIIHQVNLEYLArvvfdqdgyYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENLA---------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 242 VIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLV 321
Cdd:cd01351 128 VVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 322 QTGRDEEKLKyikkylqaVGMFRDFNDPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKdfesclgakqgfkg 401
Cdd:cd01351 208 ATGRPLLKNL--------WLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 402 fqvapehhndhktfiydnteftlahGSVVIAAITSCTNtSNPSVMLGAGLLAKKAVdaglnVMPYIKTSLSPGSGVVTYY 481
Cdd:cd01351 266 -------------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYAT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 482 LQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPepvveaitqgDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYA 561
Cdd:cd01351 315 LSREGYYEILVDSGARILPPGCGPCMGNGARLV----------ADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATA 384
|
....*
gi 1384865994 562 IAGTI 566
Cdd:cd01351 385 IAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
75-889 |
3.90e-91 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 302.07 E-value: 3.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 75 EVPFKPARVILQDFTGVPAVVDFAAM-RDAVK-KLggdpekinpvcpADLVIDHS-IQVDFnrradslqknqdlefeRNR 151
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgLDRVKtEL------------SVQYVDHNlLQADF----------------ENA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 152 ERFEFLKWGSQAFhNMRIIPPGSGIIHQVNLEYLARvvfdqdgyyyP-DSLVGTDSHTTMIDGLGILGWGVGGIEAEAVM 230
Cdd:PRK07229 76 DDHRFLQSVAAKY-GIYFSKPGNGICHQVHLERFAF----------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 231 LGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTItkhLRQVGV---VGKFVEFFGPGVAQLSIADRATIANMCPEYGATA 307
Cdd:PRK07229 145 AGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILEL---LRRLTVkggVGKIIEYFGPGVATLSVPERATITNMGAELGATT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 308 AFFPVDEVSITYLVQTGRDEeklkyikkylqavgmfrDFNDPSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSDM 385
Cdd:PRK07229 222 SIFPSDERTREFLKAQGRED-----------------DWVELLADPDaeYDEVIEIDLSELEPLIAGPHSPDNVVPVSEV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 386 KkdfesclGAKqgfkgfqvapehhndhktfiydnteftlahgsVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAglnvmp 465
Cdd:PRK07229 285 A-------GIK--------------------------------VDQVLIGSCTNSSYEDLMRAASILKGKKVHP------ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 466 yiKTSL--SPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGplpEPVVEAITqgdlvavgVLSGNRNFEGRV- 542
Cdd:PRK07229 320 --KVSLviNPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNVS--------LRTFNRNFPGRSg 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 543 HPNTRAnYLASPPLVIAYAIAGTIR--IDFEKEPLGvnakgqqvflkdiWPtrdEIQAVERQYVIPGMF---KEVYQKIE 617
Cdd:PRK07229 387 TKDAQV-YLASPETAAASALTGVITdpRTLALENGE-------------YP---KLEEPEGFAVDDAGIiapAEDGSDVE 449
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 618 TVneswnalatpsdklffwnsKSTYIKSPPffenltlDLQPPKSIVDAYVLLNLGDSVTTDHISPAGniarnspaARYLt 697
Cdd:PRK07229 450 VV-------------------RGPNIKPLP-------LLEPLPDLLEGKVLLKVGDNITTDHIMPAG--------AKWL- 494
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 698 nrgltprefnSYgsrRGNDAVMARGTFanIRLLNRFlnkqapqtihlpsgeildvfdaAERYQQAGlPLIVLAGKEYGAG 777
Cdd:PRK07229 495 ----------PY---RSNIPNISEFVF--EGVDNTF----------------------PERAKEQG-GGIVVGGENYGQG 536
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 778 SSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALgltgQERYTIIIpENLKPQMK---VQVKLD 854
Cdd:PRK07229 537 SSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKI----EEGDVLEI-EDLREFLPggpLTVVNV 611
|
810 820 830
....*....|....*....|....*....|....*.
gi 1384865994 855 T-GKTFQAVMRFdTDVELTYFLNGGILNYMIRKMAK 889
Cdd:PRK07229 612 TkDEEIEVRHTL-SERQIEILLAGGALNLIKKKLAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
82-566 |
1.67e-56 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 200.36 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAVVDFAAmrdavkklGGDPEkinPVCPADLVIDHSIQVdfnrradSLQKNQDLEF--ERNRERFEFLKW 159
Cdd:cd01584 1 RVAMQDATAQMALLQFMS--------SGLPK---VAVPSTIHCDHLIEA-------QVGGEKDLKRakDINKEVYDFLAS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 160 GSqAFHNMRIIPPGSGIIHQVNLEylarvvfdqdGYYYPDSL-VGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMV 238
Cdd:cd01584 63 AG-AKYGIGFWKPGSGIIHQIVLE----------NYAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 239 LPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIT 318
Cdd:cd01584 132 CPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 319 YLVQTGRDEeklkyIKKYLQAVGMFRDFNDPSQDPDftQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFEsclgaKQG 398
Cdd:cd01584 212 YLKATGRAE-----IADLADEFKDDLLVADEGAEYD--QLIEINLSELEPHINGPFTPDLATPVSKFKEVAE-----KNG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 399 FkgfqvaPEhhndhktfiydnteftlahgSVVIAAITSCTNTSNPSvMLGAGLLAKKAVDAGLNvmPYIKTSLSPGSGVV 478
Cdd:cd01584 280 W------PL--------------------DLRVGLIGSCTNSSYED-MGRAASIAKQALAHGLK--CKSIFTITPGSEQI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 479 TYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPlpepvvEAITQGDLVAVgVLSGNRNFEGR--VHPNTRAnYLASPPL 556
Cdd:cd01584 331 RATIERDGLLQTFRDAGGIVLANACGPCIGQWDR------KDIKKGEKNTI-VTSYNRNFTGRndANPATHA-FVASPEI 402
|
490
....*....|
gi 1384865994 557 VIAYAIAGTI 566
Cdd:cd01584 403 VTAMAIAGTL 412
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
84-566 |
2.33e-54 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 193.43 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 84 ILQDFTGVPAVVDFAAMrdavkklgGDPEKINPVCPAdlVIDHS-IQVDFnrradslqknqdlefeRNRERFEFLKwGSQ 162
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--------GVDRVRTELSVS--YVDHNtLQTDF----------------ENADDHRFLQ-TVA 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 163 AFHNMRIIPPGSGIIHQVNLEYLARvvfdqdgyyyP-DSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:cd01585 57 ARYGIYFSRPGNGICHQVHLERFAV----------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 242 VIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLV 321
Cdd:cd01585 127 VVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 322 QTGRDEeklkyikkylqavgmfrDFNDPSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSDMkkdfesclgakQGF 399
Cdd:cd01585 207 AQGRED-----------------DWVELAADADaeYDEEIEIDLSELEPLIARPHSPDNVVPVREV-----------AGI 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 400 KGFQVapehhndhktfiydnteftlahgsvviaAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMpyiktsLSPGSGVVT 479
Cdd:cd01585 259 KVDQV----------------------------AIGSCTNSSYEDLMTVAAILKGRRVHPHVSMV------VAPGSKQVL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 480 YYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPvveaitqgdlvAVGVLSGNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:cd01585 305 EMLARNGALADLLAAGARILESACGPCIGMGQAPPTG-----------GVSVRTFNRNFEGRSGTKDDLVYLASPEVAAA 373
|
....*..
gi 1384865994 560 YAIAGTI 566
Cdd:cd01585 374 AALTGVI 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
692-821 |
5.85e-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: 183.34 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 692 AARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIRLLNRFL-NKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLA 770
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1384865994 771 GKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPG 821
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
82-566 |
1.19e-49 |
|
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: 180.08 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAvvdFAAMRDAVKKLGGDPEKINpvcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNRERFeflkwGS 161
Cdd:cd01583 1 LHLVHDVTSPQA---FEGLREAGREKVWDPEKIV------AVFDHNVPTP-----DIKAAEQVKTLRKFAKEF-----GI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 162 QAFHNMRiippgSGIIHQVNLEylarvvfdqDGYYYP-DSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLP 240
Cdd:cd01583 62 NFFDVGR-----QGICHVILPE---------KGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 241 QVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYL 320
Cdd:cd01583 128 ETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 321 VqtGRDEEKLKYIKkylqavgmfrdfndPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSdmkkdfesclgakqgfk 400
Cdd:cd01583 208 K--GRGKAYWKELK--------------SDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVS----------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 401 gfQVAPEhhndhktfiydnteftlahgSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMpyiktsLSPGSGVVTY 480
Cdd:cd01583 255 --EVEGI--------------------KIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLI------VVPASQRVYK 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 481 YLQESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEPVVEAITQgdlvavgvlsgNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:cd01583 307 QAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAPGERCVSTS-----------NRNFKGRMGSPGARIYLASPATAAA 375
|
....*..
gi 1384865994 560 YAIAGTI 566
Cdd:cd01583 376 SAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
82-566 |
1.26e-44 |
|
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: 166.74 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAvvdFAAMRdavkKLGG----DPEKInpVcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNRERFefl 157
Cdd:COG0065 30 LHLVHDVTSPQA---FEGLR----EAGGrkvwDPDRI--V----AVFDHNVPTK-----DPKSAEQVKTLREFAKEF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 158 kwgsqafhNMRIIPPGS-GIIHQVNLEylarvvfdqDGYYYP-DSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPI 235
Cdd:COG0065 89 --------GITFFDVGDpGICHVVLPE---------QGLVLPgMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 236 SMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEV 315
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 316 SITYLVQTGRDEEklkyikKYLQAvgmfrdfnDPsqDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKkdfesclGA 395
Cdd:COG0065 232 TFEYLKGRPFAPW------RTLKS--------DE--DAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELE-------GI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 396 K--QGFkgfqvapehhndhktfiydnteftlahgsvviaaITSCTNtsnpsvmlG--------AGLLAKKAVDAGLNVMp 465
Cdd:COG0065 289 KidQVF----------------------------------IGSCTN--------GriedlraaAEILKGRKVAPGVRAI- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 466 yiktsLSPGSGVVtyYLQ--ESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDlvaVGVLSGNRNFEGRV 542
Cdd:COG0065 326 -----VVPGSQEV--YRQaeAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAP--------GE---RCASTSNRNFEGRM 387
|
490 500
....*....|....*....|....*
gi 1384865994 543 -HPNTRAnYLASPPLVIAYAIAGTI 566
Cdd:COG0065 388 gSPGSRT-YLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
83-566 |
3.66e-35 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 139.16 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 83 VILQDFTGVPAVVDFaamrdavKKLGG----DPEKINpvcpadLVIDHSIQVDfNRRADSLQKnqdleFERnrerfEFLK 158
Cdd:PRK00402 31 VMAHDITGPLAIKEF-------EKIGGdkvfDPSKIV------IVFDHFVPAK-DIKSAEQQK-----ILR-----EFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 159 wgSQAFHNMRIIppGSGIIHQVNLEYlarvvfdqdGYYYP-DSLVGTDSHTTMIDGLGILGWGVGGIEAEAVM-LGQpIS 236
Cdd:PRK00402 87 --EQGIPNFFDV--GEGICHQVLPEK---------GLVRPgDVVVGADSHTCTYGALGAFATGMGSTDMAAAMaTGK-TW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 237 MVLPQVIGYRLMGKPHPLVTSTDIVLTItkhLRQVGVVG---KFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVD 313
Cdd:PRK00402 153 FKVPETIKVVLEGKLPPGVTAKDVILHI---IGDIGVDGatyKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 314 EVSITYLVQ-TGRDEEKLKyikkylqavgmfrdfndPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKkdfesc 392
Cdd:PRK00402 230 EKTLEYLKErAGRDYKPWK-----------------SDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVE------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 393 lgakqGFKGFQVapehhndhktFIydnteftlahGsvviaaitSCTNtsnpsvmlG--------AGLLAKKAVDaglnvm 464
Cdd:PRK00402 287 -----GTKVDQV----------FI----------G--------SCTN--------GrledlriaAEILKGRKVA------ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 465 PYIKTSLSPGSGVVtyYLQ--ESGVMPYLSQLGFdVVGY-GCMTCIGNS-GPLPEpvveaitqGDlvaVGVLSGNRNFEG 540
Cdd:PRK00402 320 PGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHmGVLAP--------GE---VCLSTTNRNFKG 385
|
490 500
....*....|....*....|....*..
gi 1384865994 541 RV-HPNTRAnYLASPPLVIAYAIAGTI 566
Cdd:PRK00402 386 RMgSPESEV-YLASPAVAAASAVTGKI 411
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
79-566 |
1.28e-31 |
|
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: 128.34 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 79 KPARVILQDFTGVPAvvdFAAMRDAVKKLGGDPEKINpvcpadLVIDHSIQVDfNRRADSLQKnqdlefernrerfEFLK 158
Cdd:TIGR02086 25 EVDLAMTHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNVPPP-TVEAAEMQK-------------EIRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 159 WGSQafHNMRIIPPGSGIIHQVNLEylarvvfdqDGYYYP-DSLVGTDSHTTMIDGLGILGWGVGGIE-AEAVMLGQPIS 236
Cdd:TIGR02086 82 FAKR--HGIKNFDVGEGICHQILAE---------EGYALPgMVVVGGDSHTCTSGAFGAFATGMGATDmAIALATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 237 MVlPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVS 316
Cdd:TIGR02086 151 KV-PETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 317 ITYLVQTGRDEEKLKYikkylqavgmfrdfndPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMkkdfesclgak 396
Cdd:TIGR02086 230 YEYLKKRRGLEFRILV----------------PDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDV----------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 397 QGFKGFQVapehhndhktfiydnteFtlahgsvviaaITSCTNTSNPSVMLGAGLLAkkavdaGLNVMPYIKTSLSPGSG 476
Cdd:TIGR02086 283 EGTEIDQV-----------------F-----------IGSCTNGRLEDLRIAAEILK------GRRVHPDVRLIVIPASR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 477 VVTYYLQESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDLVavgVLSGNRNFEGRV-HPNTRAnYLASP 554
Cdd:TIGR02086 329 KVYLRALEEGIILTLVRAGAMICPPGCGPCLGaHMGVLGD--------GEVC---LSTTNRNFKGRMgSPNAEI-YLASP 396
|
490
....*....|..
gi 1384865994 555 PLVIAYAIAGTI 566
Cdd:TIGR02086 397 ATAAASAVEGYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
82-566 |
3.95e-30 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 125.02 E-value: 3.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 82 RVILQDFTGVPAvvdFAAMRDAVKKLGgDPEKinpvcpADLVIDHSIQVDFNRRA---DSLQKNQDLEFERNRERFeflk 158
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTVR-RPDL------TLAVVDHVVPTRPGRDRgitDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 159 wgsqAFHNMRIIPPGSGIIHqvnleylarVVFDQDGYYYPDSLVGT-DSHTTMIDGLGILGWGVGGIEAEAVMLGQPISM 237
Cdd:PRK12466 96 ----GIRLFDVDDPRQGIVH---------VVAPELGLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLVY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 238 VLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSI 317
Cdd:PRK12466 163 RKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 318 TYLvqTGR----DEEKLKyikkylQAVGMFRDFndPSqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSD------M 385
Cdd:PRK12466 243 DYL--RGRprapKGALWD------AALAYWRTL--RS-DADavFDREVEIDAADIAPQVTWGTSPDQAVPITGrvpdpaA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 386 KKDFESCLGAKQGFKGFQVAPEHHndhktfiydnteftLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMp 465
Cdd:PRK12466 312 EADPARRAAMERALDYMGLTPGTP--------------LAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAM- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 466 yiktsLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGnsgplpepvveaiTQGDLVAVG---VLSGNRNFEGRV 542
Cdd:PRK12466 377 -----VVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA-------------MNDDVLAPGercASTTNRNFEGRQ 438
|
490 500
....*....|....*....|....
gi 1384865994 543 HPNTRAnYLASPPLVIAYAIAGTI 566
Cdd:PRK12466 439 GPGART-HLMSPAMVAAAAVAGHI 461
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
124-566 |
3.96e-29 |
|
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: 120.03 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 124 IDHSIQvdfNRRADSLQKNQDLEfernrerfEFLKWgsqafHNMRIIPPGSGIIHQVNLEylarvvfdqDGYYYPDSL-V 202
Cdd:cd01582 33 LDHDVQ---NKSEKNLKKYKNIE--------SFAKK-----HGIDFYPAGRGIGHQIMIE---------EGYAFPGTLaV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 203 GTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFG 282
Cdd:cd01582 88 ASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 283 PGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITylvqtgrdeeklkyikkylqavgmfrdfndpsqdpdftqvveLD 362
Cdd:cd01582 168 SGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLI------------------------------------------LD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 363 LKTVVPCCSGPkrpqDKVAVSDMKKDFEsclgaKQGFKgfqvapehhndhktfiydnteftlahgsVVIAAITSCTNTSN 442
Cdd:cd01582 206 LSTLSPYVSGP----NSVKVSTPLKELE-----AQNIK----------------------------INKAYLVSCTNSRA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 443 PSVMLGAGLLAKKAVDAGLN-VMPYIKTSLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPvveai 521
Cdd:cd01582 249 SDIAAAADVVKGKKEKNGKIpVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEP----- 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1384865994 522 tqGDlvaVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTI 566
Cdd:cd01582 324 --GE---VGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
762-838 |
5.28e-21 |
|
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: 87.91 E-value: 5.28e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1384865994 762 AGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGEnaDALGLTGQERYTII 838
Cdd:cd00404 13 PAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE--DYLKLHTGDELDIY 87
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
671-818 |
7.84e-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: 85.95 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 671 LGDSVTTDHISPAGniarnspaARYLTNRgltprefnsygsrrgndavmargtfANIRLLNRFLNKQAPQTIHlpsgeil 750
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLR-------------------------SNIPAISEFVFHRVDPTFA------- 41
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865994 751 dvfdaaERYQQAGlPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEY 818
Cdd:cd01579 42 ------ERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
123-566 |
1.23e-16 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 83.63 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 123 VIDHSIQVDfNRR---ADSLQKNQDLEFERNRERFeflkwgsqafhNMRIIPPGS---GIIHqvnleylarVVFDQDGYY 196
Cdd:PRK05478 60 TMDHNVPTT-DRDlpiADPVSRIQVETLEKNCKEF-----------GITLFDLGDprqGIVH---------VVGPEQGLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 197 YPD-SLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTItkhLRQVGV-- 273
Cdd:PRK05478 119 LPGmTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAI---IGKIGTag 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 274 -VGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYL-----VQTGRDEEklkyikkylQAVGMFRDFn 347
Cdd:PRK05478 196 gTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLkgrpfAPKGEDWD---------KAVAYWKTL- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 348 dPSqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESclgakqgfkgFQVAPEHHNDHKTFIYDNteftLA 425
Cdd:PRK05478 266 -KS-DEDavFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPED----------FADPVKRASAERALAYMG----LK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 426 HG------SVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMpyiktsLSPGSGVVTYYLQESGVMPYLSQLGFDVV 499
Cdd:PRK05478 330 PGtpitdiKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRAL------VVPGSGLVKAQAEAEGLDKIFIEAGFEWR 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384865994 500 GYGCMTCIG-NSGPLPEpvveaitqGDLVAVgvlSGNRNFEGRVHPNTRaNYLASPPLVIAYAIAGTI 566
Cdd:PRK05478 404 EPGCSMCLAmNPDKLPP--------GERCAS---TSNRNFEGRQGKGGR-THLVSPAMAAAAAITGHF 459
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
676-830 |
9.86e-14 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 69.42 E-value: 9.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 676 TTDHISPAGniarnsPAARYltnrgltprefnsygsrrgndavmaRGTFANIRllNRFL-------NKQAPQTIHLPSGE 748
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIS--NNLLigainaeNGKANSVKNQVTGE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 749 ILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYL--------- 819
Cdd:cd01578 54 YGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAdpadydkih 133
|
170
....*....|.
gi 1384865994 820 PGENADALGLT 830
Cdd:cd01578 134 PDDKVDILGLT 144
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
672-861 |
1.02e-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: 67.50 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 672 GDSVTTDHISPAgniarnspaaRYLtnRGLTPREFnsygsrrgndavmARGTFANIRllnrFLNKQAPqtihlpsgeilD 751
Cdd:COG0066 15 GDNIDTDQIIPA----------RFL--KTIDREGL-------------GKHLFEDWR----YDRSPDP-----------D 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 752 VFDAAERYQQAGlplIVLAGKEYGAGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEyLPGENADAL- 827
Cdd:COG0066 55 FVLNQPRYQGAD---ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALf 127
|
170 180 190
....*....|....*....|....*....|....*
gi 1384865994 828 -GLTGQERYTIIIpeNLKPQmkvQVKLDTGKTFQA 861
Cdd:COG0066 128 aAIEANPGDELTV--DLEAG---TVTNGTGETYPF 157
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
764-833 |
6.07e-11 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 59.52 E-value: 6.07e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384865994 764 LPLIVLAGKEYGAGSSR---DWAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALGLTGQE 833
Cdd:cd01577 17 LGDIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE 86
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
170-328 |
6.99e-11 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 66.19 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 170 IPPGSGIIHQVNLEYLArvvfdQDGyyypDSLVGTDSHTTMiDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMG 249
Cdd:PRK11413 123 VPPHIAVIHQYMREMMA-----GGG----KMILGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 250 KPHPLVTSTDIVLTITKHLRQVGVV-GKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLVQTGRDEE 328
Cdd:PRK11413 193 KPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQD 272
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
767-817 |
4.85e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 56.35 E-value: 4.85e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1384865994 767 IVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLE 817
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFE 102
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
767-885 |
2.10e-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: 54.35 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 767 IVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEylpgenADALGLTGQERYTIiipeNLKpq 846
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEGIKDGDEVTV----DLE-- 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 1384865994 847 mKVQVKLDTGKTFqaVMRFDTDVELTYFLNGGILNYMIR 885
Cdd:TIGR02087 118 -TGEIRVNGNEEY--KGEPLPDFLLEILREGGLLEYLKK 153
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
767-817 |
1.58e-06 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 49.05 E-value: 1.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1384865994 767 IVLAGKEYGAGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLE 817
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGLPVLE 101
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
624-817 |
8.99e-06 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 47.93 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 624 NALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPKSIVDA---------YVLlnlGDSVTTDHISPAGniarnspaar 694
Cdd:PLN00072 23 SSSATPRPFLRFSSTSSIFPFKPLTTSSGTSSPTISDSAESTssttfhglcFVV---GDNIDTDQIIPAE---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384865994 695 YLTNRGLTPREFNSYGSrrgndavmargtFANIRLlnrflnKQAPQTIHLPSGEIldvfdaAERYQqaglplIVLAGKEY 774
Cdd:PLN00072 90 YLTLVPSKPDEYEKLGS------------YALIGL------PAFYKTRFVEPGEM------KTKYS------IIIGGENF 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1384865994 775 GAGSSRDWAakgPFLLG---IKAVLAESYERIHRSNLVGMG-VIPLE 817
Cdd:PLN00072 140 GCGSSREHA---PVALGaagAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
757-827 |
1.18e-05 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 47.04 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1384865994 757 ERYQQAGlplIVLAGKEYGAGSSRD---WAakgpfLL--GIKAVLAESYERIHRSNLVGMGVIPLEyLPGENADAL 827
Cdd:PRK01641 63 PRYQGAS---ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDEL 129
|
|
| |
