|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
3-889 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1601.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 3 NPFAHLAEPLdAAQPGKRFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPAR 82
Cdd:PTZ00092 14 NPFEKVLKTL-KDGGSYKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 83 VILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQ 162
Cdd:PTZ00092 93 VLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 163 AFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQV 242
Cdd:PTZ00092 173 AFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 243 IGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLLQ 322
Cdd:PTZ00092 253 VGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 323 TGREEDKVKHIQKYLQAVGMFRDFNDtsqDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGFKGF 402
Cdd:PTZ00092 333 TGRSEEKVELIEKYLKANGLFRTYAE---QIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 403 QVAPDRHNDRKTFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYL 482
Cdd:PTZ00092 410 GIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 483 RESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAI 562
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYAL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 563 AGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTY 642
Cdd:PTZ00092 570 AGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTY 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 643 IKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARG 722
Cdd:PTZ00092 650 IHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRG 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 723 TFANIRLLNKFLNKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYER 802
Cdd:PTZ00092 730 TFANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFER 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 803 IHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTINIPE-DLKPRMTVQIKLDTGKTFQAVMRFDTDVELTYFHNGGILN 881
Cdd:PTZ00092 810 IHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGILQ 889
|
....*...
gi 110347487 882 YMIRKMAQ 889
Cdd:PTZ00092 890 YVLRKLVK 897
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
17-889 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1483.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 17 PGK--RFFNLNKLEDSRYG---RLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVILQDFTGV 91
Cdd:PRK09277 16 GGKsyDYYSLRALEAKGLGdisRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIPFRPARVVMQDFTGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 92 PAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAFCNMRIIP 171
Cdd:PRK09277 96 PAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFLKWGQKAFDNFRVVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 172 PGSGIIHQVNLEYLARVVF-DQDGC--YYPDSLVGTDSHTTMIDglgvlgwgvggIEAEAVMLGQPISMVLPQVIGYKLM 248
Cdd:PRK09277 176 PGTGICHQVNLEYLAPVVWtREDGElvAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPSSMLIPEVVGVKLT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 249 GKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLLQTGREED 328
Cdd:PRK09277 256 GKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 329 KVKHIQKYLQAVGMFRDfndTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGFKGFQVAPDr 408
Cdd:PRK09277 336 QVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQGFGLDEAEE- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 409 hndrktflysNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVM 488
Cdd:PRK09277 412 ----------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 489 PYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRI 568
Cdd:PRK09277 482 PYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDI 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 569 DFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPF 648
Cdd:PRK09277 562 DLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPY 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 649 FESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIR 728
Cdd:PRK09277 642 FEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIR 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 729 LLNKFLN-KQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSN 807
Cdd:PRK09277 722 IRNEMVPgVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSN 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 808 LVGMGVIPLEYLPGETADSLGLTGRERYTINIPEDLKPR--MTVQIKLDTG--KTFQAVMRFDTDVELTYFHNGGILNYM 883
Cdd:PRK09277 802 LVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGatVTVVITRADGevVEFPVLCRIDTAVEVDYYRNGGILQYV 881
|
....*.
gi 110347487 884 IRKMAQ 889
Cdd:PRK09277 882 LRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
20-889 |
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: 1472.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 20 RFFNLNKLEDSRYG--RLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVILQDFTGVPAVVDF 97
Cdd:COG1048 19 TYYSLPALEEAGGDisRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVLMQDFTGVPAVVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 98 AAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAFCNMRIIPPGSGII 177
Cdd:COG1048 99 AAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAFDNFRVVPPGTGIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 178 HQVNLEYLARVVF--DQDG--CYYPDSLVGTDSHTTMIDglgvlgwgvggIEAEAVMLGQPISMVLPQVIGYKLMGKPHP 253
Cdd:COG1048 179 HQVNLEYLAFVVWtrEEDGetVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPVSMLIPEVVGVKLTGKLPE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 254 LVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVKHI 333
Cdd:COG1048 259 GVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIELV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 334 QKYLQAVGMFRDfnDTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGfkgfqvapDRHNDRK 413
Cdd:COG1048 339 EAYAKAQGLWRD--PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG--------EELDKPV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 414 TFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQ 493
Cdd:COG1048 409 RVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 494 LGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRIDFEKE 573
Cdd:COG1048 489 LGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLTTD 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 574 PLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPFFESLT 653
Cdd:COG1048 569 PLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEGLQ 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 654 LDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIRLLNKF 733
Cdd:COG1048 649 LEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKNLL 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 734 L-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMG 812
Cdd:COG1048 729 ApGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMG 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 813 VIPLEYLPGETADSLGLTGRERYTI-NIPEDLKPRMTVQIKLD----TGKTFQAVMRFDTDVELTYFHNGGILNYMIRKM 887
Cdd:COG1048 809 VLPLQFPEGESAESLGLTGDETFDIeGLDEGLAPGKTVTVTATradgSTEEFPVLHRIDTPVEVEYYRAGGILQYVLRQL 888
|
..
gi 110347487 888 AQ 889
Cdd:COG1048 889 LA 890
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
2-889 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1357.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 2 KNPFAHLAEPLDAAQPGK--RFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFK 79
Cdd:PLN00070 42 ENPFKGILTSLPKPGGGEfgKYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 80 PARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKW 159
Cdd:PLN00070 122 PARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 160 GSQAFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVL 239
Cdd:PLN00070 202 GSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 240 PQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAY 319
Cdd:PLN00070 282 PGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 320 LLQTGREEDKVKHIQKYLQAVGMFRDFNDTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGF 399
Cdd:PLN00070 362 LKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGF 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 400 KGFQVAPDRHNDRKTFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVT 479
Cdd:PLN00070 442 KGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVT 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 480 YYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:PLN00070 522 KYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVA 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 560 YAIAGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPK 639
Cdd:PLN00070 602 YALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 640 STYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIM 719
Cdd:PLN00070 682 STYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIM 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 720 ARGTFANIRLLNKFLNKQ-APQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAE 798
Cdd:PLN00070 762 ARGTFANIRIVNKLLKGEvGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAK 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 799 SYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTINIP---EDLKPRMTVQIKLDTGKTFQAVMRFDTDVELTYFH 875
Cdd:PLN00070 842 SFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPsniSEIKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFD 921
|
890
....*....|....
gi 110347487 876 NGGILNYMIRKMAQ 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: 1294.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 21 FFNLNKLEDS--RYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVILQDFTGVPAVVDFA 98
Cdd:TIGR01341 5 YYSLKALEESggKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAVVDLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 99 AMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAFCNMRIIPPGSGIIH 178
Cdd:TIGR01341 85 AMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGTGIIH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 179 QVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPL 254
Cdd:TIGR01341 165 QVNLEYLATVVFkaevDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 255 VTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVKHIQ 334
Cdd:TIGR01341 245 VTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVELVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 335 KYLQAVGMFRDFndtSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGFKGFQVapdrHNDRKT 414
Cdd:TIGR01341 325 KYARAQGLFYDD---SEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTL----RKEPLK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 415 FLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQL 494
Cdd:TIGR01341 398 KKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEEL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 495 GFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRIDFEKEP 574
Cdd:TIGR01341 478 GFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 575 LGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPFFESLTL 654
Cdd:TIGR01341 558 IGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 655 DLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIRLLNKFL 734
Cdd:TIGR01341 638 DPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMV 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 735 -NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGV 813
Cdd:TIGR01341 718 kGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 814 IPLEYLPGETADSLGLTGREryTINIP--EDLKPRMTVQIKLDTGK----TFQAVMRFDTDVELTYFHNGGILNYMIRKM 887
Cdd:TIGR01341 798 IPLQFPQGEDAETLGLTGDE--TIDIDgiKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
11-889 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1277.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 11 PLDAAQPGK---RFFNLNKLE---DSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVI 84
Cdd:PRK12881 8 TLKEFDVGGktyKFYSLPALGkelGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIPFVPARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 85 LQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAF 164
Cdd:PRK12881 88 MQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 165 CNMRIIPPGSGIIHQVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLP 240
Cdd:PRK12881 168 DNFRVVPPGTGIMHQVNLEYLARVVHtkedDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 241 QVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYL 320
Cdd:PRK12881 248 DVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 321 LQTGREEDKVKHIQKYLQAVGMFRDfndTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGFK 400
Cdd:PRK12881 328 RLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAEN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 401 GFQVAPDRHNDrktflysnseFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTY 480
Cdd:PRK12881 405 GFAKKAQTSNG----------VDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 481 YLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAY 560
Cdd:PRK12881 475 YLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAY 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 561 AIAGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKS 640
Cdd:PRK12881 555 ALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKS 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 641 TYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMA 720
Cdd:PRK12881 635 TYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMM 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 721 RGTFANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAES 799
Cdd:PRK12881 715 RGTFANVRIKNLMIpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAES 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 800 YERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTIN-IPEDLKPRM--TVQIKLDTGKT--FQAVMRFDTDVELTYF 874
Cdd:PRK12881 795 FERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRQdvTLVIHRADGSTerVPVLCRIDTPIEVDYY 874
|
890
....*....|....*
gi 110347487 875 HNGGILNYMIRKMAQ 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: 790.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 82 RVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGS 161
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 162 QAFCNMRIIPPGSGIIHQVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISM 237
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 238 VLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDevsi 317
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 318 ayllqtgreedkvkhiqkylqavgmfrdfndtsqdpdfTQVVELDLKTVVPCCSGPKRPQDKVAVsemkkdfesclgakq 397
Cdd:cd01586 237 --------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 398 gfkgfqvapdrhndrktflysnseftlaHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGV 477
Cdd:cd01586 264 ----------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 478 VTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLV 557
Cdd:cd01586 316 VTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLV 395
|
....*....
gi 110347487 558 IAYAIAGTV 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: 629.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 61 ENILNWNVMQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSiqvdfnrrADSLQ 140
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 141 KNQDLEFERNKERFEFLKWGSQAFcNMRIIPPGSGIIHQVNLEYlarvvfdqdGCYYPD-SLVGTDSHTTM--------- 210
Cdd:pfam00330 73 KNIEDEISRNKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEY---------GLALPGmTIVGTDSHTTThgglgalaf 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 211 -IDGlgvlgwgvggIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLS 289
Cdd:pfam00330 143 gVGG----------SEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 290 IADRATIANMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVkhIQKYLQAVGMFRDFNDtsQDPDFTQVVELDLKTVVPC 369
Cdd:pfam00330 213 MEGRATICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASD--PGAEYDKVVEIDLSTIEPM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 370 CSGPKRPQDKVAVSEMKKD-FESCLGAKQGFKGFQVAPDRHNDRktflysnseftLAHGSVVIAAITSCTNTSNPSVMLG 448
Cdd:pfam00330 289 VTGPTRPQDAVPLSELVPDpFADAVKRKAAERALEYMGLGPGTP-----------LSDGKVDIAFIGSCTNSSIEDLRAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 449 AGLLaKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEpvveaitqGDlva 528
Cdd:pfam00330 358 AGLL-KKAVEKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--------GE--- 425
|
490 500 510
....*....|....*....|....*....|....*.
gi 110347487 529 VGVLSGNRNFEGRVHPNTRAnYLASPPLVIAYAIAG 564
Cdd:pfam00330 426 RCVSSSNRNFEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
670-837 |
3.15e-112 |
|
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: 340.79 E-value: 3.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 670 NLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIRLLNKFLNKQAPQ-TVHLPSGE 748
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGtTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 749 TLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLG 828
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
....*....
gi 110347487 829 LTGRERYTI 837
Cdd:cd01580 161 LTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
82-566 |
1.20e-98 |
|
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: 313.66 E-value: 1.20e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 82 RVILQDFTGVPAVVDFAAMRDAVKklggnpekINPVCPADLVIDHSIQvdfnrradslqknqdLEFERNKERFEFLKWgS 161
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 162 QAFCNMRIIPPGSGIIHQVNLEYLArvvfdqdgcYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENLA---------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 242 VIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLL 321
Cdd:cd01351 128 VVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 322 QTGREEDKVKhiqkylqaVGMFRDFNDTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKdfesclgakqgfkg 401
Cdd:cd01351 208 ATGRPLLKNL--------WLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 402 fqvapdrhndrktflysnseftlahGSVVIAAITSCTNtSNPSVMLGAGLLAKKAVeaglsVKPYIKTSLSPGSGVVTYY 481
Cdd:cd01351 266 -------------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYAT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 482 LRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPepvveaitqgDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYA 561
Cdd:cd01351 315 LSREGYYEILVDSGARILPPGCGPCMGNGARLV----------ADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATA 384
|
....*
gi 110347487 562 IAGTV 566
Cdd:cd01351 385 IAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
75-889 |
4.57e-83 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 280.11 E-value: 4.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 75 EVPFKPARVILQDFTGVPAVVDFAAM-RDAVK-KLggnpekinpvcpADLVIDHS-IQVDFnrradslqknqdlefeRNK 151
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgLDRVKtEL------------SVQYVDHNlLQADF----------------ENA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 152 ERFEFLKWGSQAFcNMRIIPPGSGIIHQVNLEYLARvvfdqdgcyyP-DSLVGTDSHTT------MIdglgvlgwgvgGI 224
Cdd:PRK07229 76 DDHRFLQSVAAKY-GIYFSKPGNGICHQVHLERFAF----------PgKTLLGSDSHTPtagglgML-----------AI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 225 -----EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGV---VGKFVEFFGPGVAQLSIADRATI 296
Cdd:PRK07229 134 gagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILEL---LRRLTVkggVGKIIEYFGPGVATLSVPERATI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 297 ANMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVKhiqkyLQAvgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPK 374
Cdd:PRK07229 211 TNMGAELGATTSIFPSDERTREFLKAQGREDDWVE-----LLA------------DPDaeYDEVIEIDLSELEPLIAGPH 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 375 RPQDKVAVSEMKkdfesclGAKqgfkgfqvapdrhndrktflysnseftlahgsVVIAAITSCTNTSNPSVMLGAGLLAK 454
Cdd:PRK07229 274 SPDNVVPVSEVA-------GIK--------------------------------VDQVLIGSCTNSSYEDLMRAASILKG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 455 KAVEAGLSvkpyikTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGplpEPVVEAITqgdlvavgVLSG 534
Cdd:PRK07229 315 KKVHPKVS------LVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNVS--------LRTF 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 535 NRNFEGRV-HPNTRAnYLASPPLVIAYAIAGtvRIDfekEPlgvnaqgRQVFLKDI-WPtrdEIQAVERQHVIPGMF--- 609
Cdd:PRK07229 378 NRNFPGRSgTKDAQV-YLASPETAAASALTG--VIT---DP-------RTLALENGeYP---KLEEPEGFAVDDAGIiap 441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 610 KEVYQKIETVnkswnalaapseklyawnpKSTYIKSPPffesltlDLQPPKSIVDAYVLLNLGDSVTTDHISPAGniarn 689
Cdd:PRK07229 442 AEDGSDVEVV-------------------RGPNIKPLP-------LLEPLPDLLEGKVLLKVGDNITTDHIMPAG----- 490
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 690 spaARYLtnrgltprefnSYgsrRGN-DAImARGTFanIRLLNKFlnkqapqtvhlpsgetldvfdaAERYQQAGlPLIV 768
Cdd:PRK07229 491 ---AKWL-----------PY---RSNiPNI-SEFVF--EGVDNTF----------------------PERAKEQG-GGIV 527
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 769 LAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLgltgRERYTINIP--EDLKPR 846
Cdd:PRK07229 528 VGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKI----EEGDVLEIEdlREFLPG 603
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 110347487 847 MTVQIKLDT-GKTFQAVMRFdTDVELTYFHNGGILNYMIRKMAQ 889
Cdd:PRK07229 604 GPLTVVNVTkDEEIEVRHTL-SERQIEILLAGGALNLIKKKLAA 646
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
692-821 |
6.47e-53 |
|
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: 180.25 E-value: 6.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 692 AARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLA 770
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 110347487 771 GKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPG 821
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
82-565 |
4.02e-48 |
|
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: 176.48 E-value: 4.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 82 RVILQDFTGVPAVVDFAAmrdavkklGGNPEkinPVCPADLVIDHSIQVdfnrradSLQKNQDLEF--ERNKERFEFLKW 159
Cdd:cd01584 1 RVAMQDATAQMALLQFMS--------SGLPK---VAVPSTIHCDHLIEA-------QVGGEKDLKRakDINKEVYDFLAS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 160 GSQAFcNMRIIPPGSGIIHQVNLEYLArvvfdqdgcyYPDSL-VGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMV 238
Cdd:cd01584 63 AGAKY-GIGFWKPGSGIIHQIVLENYA----------FPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 239 LPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIA 318
Cdd:cd01584 132 CPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 319 YLLQTGREEdkvkhIQKYLQAVGMFRDFNDTSQDPDftQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFEsclgaKQG 398
Cdd:cd01584 212 YLKATGRAE-----IADLADEFKDDLLVADEGAEYD--QLIEINLSELEPHINGPFTPDLATPVSKFKEVAE-----KNG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 399 FkgfqvaPDRhndrktflysnseftlahgsVVIAAITSCTNTSNPSvMLGAGLLAKKAVEAGLSVKpyIKTSLSPGSGVV 478
Cdd:cd01584 280 W------PLD--------------------LRVGLIGSCTNSSYED-MGRAASIAKQALAHGLKCK--SIFTITPGSEQI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 479 TYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPlpepvvEAITQGDLVAVgVLSGNRNFEGR--VHPNTRAnYLASPPL 556
Cdd:cd01584 331 RATIERDGLLQTFRDAGGIVLANACGPCIGQWDR------KDIKKGEKNTI-VTSYNRNFTGRndANPATHA-FVASPEI 402
|
....*....
gi 110347487 557 VIAYAIAGT 565
Cdd:cd01584 403 VTAMAIAGT 411
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
84-566 |
9.01e-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: 171.86 E-value: 9.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 84 ILQDFTGVPAVVDFAAMrdavkklgGNPEKINPVCPAdlVIDHS-IQVDFnrradslqknqdlefeRNKERFEFLKWGSQ 162
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--------GVDRVRTELSVS--YVDHNtLQTDF----------------ENADDHRFLQTVAA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 163 AFcNMRIIPPGSGIIHQVNLEYLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:cd01585 58 RY-GIYFSRPGNGICHQVHLERFAV----------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 242 VIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLL 321
Cdd:cd01585 127 VVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 322 QTGREEdkvkhiqkylqavgmfrDFNDTSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEMkkdfesclgakQGF 399
Cdd:cd01585 207 AQGRED-----------------DWVELAADADaeYDEEIEIDLSELEPLIARPHSPDNVVPVREV-----------AGI 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 400 KGFQVapdrhndrktflysnseftlahgsvviaAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVkpyiktSLSPGSGVVT 479
Cdd:cd01585 259 KVDQV----------------------------AIGSCTNSSYEDLMTVAAILKGRRVHPHVSM------VVAPGSKQVL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 480 YYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPvveaitqgdlvAVGVLSGNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:cd01585 305 EMLARNGALADLLAAGARILESACGPCIGMGQAPPTG-----------GVSVRTFNRNFEGRSGTKDDLVYLASPEVAAA 373
|
....*..
gi 110347487 560 YAIAGTV 566
Cdd:cd01585 374 AALTGVI 380
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
82-566 |
1.33e-40 |
|
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: 153.88 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 82 RVILQDFTGVPAvvdFAAMRDAVKKLGGNPEKINpvcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNKERF--EFLKW 159
Cdd:cd01583 1 LHLVHDVTSPQA---FEGLREAGREKVWDPEKIV------AVFDHNVPTP-----DIKAAEQVKTLRKFAKEFgiNFFDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 160 GSQafcnmriippgsGIIHQVNLE-YLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISM 237
Cdd:cd01583 67 GRQ------------GICHVILPEkGLTL----------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 238 VLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSI 317
Cdd:cd01583 125 RVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 318 AYLlqTGREEDKVKHIQKylqavgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKdfesclga 395
Cdd:cd01583 205 EYL--KGRGKAYWKELKS----------------DEDaeYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 396 kqgfkgfqVAPDRhndrktflysnseftlahgsVVIAaitSCTNTSNPSVMLGAGLLAKKaveaglSVKPYIKTSLSPGS 475
Cdd:cd01583 259 --------IKIDQ--------------------VFIG---SCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPAS 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 476 GVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEPVVEAITQgdlvavgvlsgNRNFEGRVHPNTRANYLASP 554
Cdd:cd01583 302 QRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAPGERCVSTS-----------NRNFKGRMGSPGARIYLASP 370
|
490
....*....|..
gi 110347487 555 PLVIAYAIAGTV 566
Cdd:cd01583 371 ATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
82-566 |
1.14e-36 |
|
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: 143.25 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 82 RVILQDFTGVPAvvdFAAMRdavkKLGG----NPEKInpVcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNKERFefl 157
Cdd:COG0065 30 LHLVHDVTSPQA---FEGLR----EAGGrkvwDPDRI--V----AVFDHNVPTK-----DPKSAEQVKTLREFAKEF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 158 kwgsqafcNMRIIPPGS-GIIHQVNLEY-LARvvfdqdgcyyP-DSLVGTDSHTTM----------IDGLgvlgwgvggi 224
Cdd:COG0065 89 --------GITFFDVGDpGICHVVLPEQgLVL----------PgMTIVGGDSHTCThgafgafafgIGTT---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 225 EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYG 304
Cdd:COG0065 141 DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 305 ATAAFFPVDEVSIAYLLQTGREEDKVkhiqkyLQAvgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAV 382
Cdd:COG0065 221 AKAGIIAPDETTFEYLKGRPFAPWRT------LKS------------DEDavYDKEVEIDASDLEPQVAWPHSPDNVVPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 383 SEMKKdfesclgakqgfkgfqVAPDRhndrktflysnseftlahgsvviAAITSCTNtsnpsvmlgaG----LLAKKAVE 458
Cdd:COG0065 283 SELEG----------------IKIDQ-----------------------VFIGSCTN----------GriedLRAAAEIL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 459 AGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDlvaVGVLSGNRN 537
Cdd:COG0065 314 KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAP--------GE---RCASTSNRN 382
|
490 500 510
....*....|....*....|....*....|
gi 110347487 538 FEGRV-HPNTRAnYLASPPLVIAYAIAGTV 566
Cdd:COG0065 383 FEGRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
83-564 |
4.05e-28 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 117.97 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 83 VILQDFTGVPAVVDFaamrdavKKLGG----NPEKINpvcpadLVIDHSIQVDfNRRADSLQKnqdleFERnkerfEFLK 158
Cdd:PRK00402 31 VMAHDITGPLAIKEF-------EKIGGdkvfDPSKIV------IVFDHFVPAK-DIKSAEQQK-----ILR-----EFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 159 wgSQAFCNMRIIppGSGIIHQVNLEY-LARvvfdqdgcyyP-DSLVGTDSHTT----------------Midglgvlgwg 220
Cdd:PRK00402 87 --EQGIPNFFDV--GEGICHQVLPEKgLVR----------PgDVVVGADSHTCtygalgafatgmgstdM---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 221 vggieAEAVMLGQpISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGVVG---KFVEFFGPGVAQLSIADRATIA 297
Cdd:PRK00402 143 -----AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHI---IGDIGVDGatyKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 298 NMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVkhiqkyLQAvgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKR 375
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLKERAGRDYKP------WKS------------DEDaeYEEVYEIDLSKLEPQVAAPHL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 376 PQDKVAVSEMKkdfesclGAKqgfkgfqvapdrhndrktflysnseftlahgsVVIAAITSCTNtsnpsvmlgaGLLAKK 455
Cdd:PRK00402 276 PDNVKPVSEVE-------GTK--------------------------------VDQVFIGSCTN----------GRLEDL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 456 AVEA----GLSVKPYIKTSLSPGSGVVtyYLR--ESGVMPYLSQLGFdVVGY-GCMTCIGNS-GPLPEpvveaitqGDlv 527
Cdd:PRK00402 307 RIAAeilkGRKVAPGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHmGVLAP--------GE-- 373
|
490 500 510
....*....|....*....|....*....|....*...
gi 110347487 528 aVGVLSGNRNFEGRV-HPNTRAnYLASPPLVIAYAIAG 564
Cdd:PRK00402 374 -VCLSTTNRNFKGRMgSPESEV-YLASPAVAAASAVTG 409
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
79-564 |
4.73e-23 |
|
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: 102.92 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 79 KPARVILQDFTGVPAvvdFAAMRDAVKKLGGNPEKINpvcpadLVIDHSIQVDFNRRAdslqknqdlefERNKERFEFLK 158
Cdd:TIGR02086 25 EVDLAMTHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNVPPPTVEAA-----------EMQKEIREFAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 159 wgsqafcNMRI--IPPGSGIIHQVnleyLARVVFDQDGcyypDSLVGTDSHTTMIDGLGVLGWGVGGIE-AEAVMLGQPI 235
Cdd:TIGR02086 85 -------RHGIknFDVGEGICHQI----LAEEGYALPG----MVVVGGDSHTCTSGAFGAFATGMGATDmAIALATGKTW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 236 SMVlPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEV 315
Cdd:TIGR02086 150 IKV-PETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 316 SIAYLLQTGREEdkvkhiqkylqavgmfrdFNDTSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEMkkdfescl 393
Cdd:TIGR02086 229 TYEYLKKRRGLE------------------FRILVPDPGanYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDV-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 394 gakQGFKGFQVapdrhndrktflysnseFtlahgsvviaaITSCTNTSNPSVMLGAGLLAkkaveaGLSVKPYIKTSLSP 473
Cdd:TIGR02086 283 ---EGTEIDQV-----------------F-----------IGSCTNGRLEDLRIAAEILK------GRRVHPDVRLIVIP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 474 GSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDLVavgVLSGNRNFEGRV-HPNTRAnYL 551
Cdd:TIGR02086 326 ASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGaHMGVLGD--------GEVC---LSTTNRNFKGRMgSPNAEI-YL 393
|
490
....*....|...
gi 110347487 552 ASPPLVIAYAIAG 564
Cdd:TIGR02086 394 ASPATAAASAVEG 406
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
110-566 |
5.54e-23 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 101.54 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 110 NPEKInpVCpadlVIDHSIQvdfNRRADSLQKNQDLEFERNKERFEFLkwgsqafcnmriiPPGSGIIHQVNLEylarvv 189
Cdd:cd01582 25 NPDQI--VM----TLDHDVQ---NKSEKNLKKYKNIESFAKKHGIDFY-------------PAGRGIGHQIMIE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 190 fdqDGCYYPDSL-VGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHL 268
Cdd:cd01582 77 ---EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 269 RQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDevsiayllqtgreedkVKHIQkylqavgmfrdfnd 348
Cdd:cd01582 154 NKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD----------------AKHLI-------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 349 tsqdpdftqvveLDLKTVVPCCSGPkrpqDKVAVSEMKKDFEsclgaKQGFKgfqvapdrhndrktflysnseftlahgs 428
Cdd:cd01582 204 ------------LDLSTLSPYVSGP----NSVKVSTPLKELE-----AQNIK---------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 429 VVIAAITSCTNTSNPSVMLGAGLL-AKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCI 507
Cdd:cd01582 235 INKAYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCI 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 110347487 508 GNSGPLPEPvveaitqGDlvaVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTV 566
Cdd:cd01582 315 GLGQGLLEP-------GE---VGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
82-564 |
5.39e-22 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 100.36 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 82 RVILQDFTGVPAvvdFAAMRDAVKKLGgNPEKinpvcpADLVIDHSIQVDFNRRA---DSLQKNQDLEFERNKERFeflk 158
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTVR-RPDL------TLAVVDHVVPTRPGRDRgitDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 159 wGSQAFcnmRIIPPGSGIIHqvnleylarVVFDQDGCYYPDSLVGT-DSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISM 237
Cdd:PRK12466 96 -GIRLF---DVDDPRQGIVH---------VVAPELGLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLVY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 238 VLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSI 317
Cdd:PRK12466 163 RKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 318 AYLlqTGREED-KVKHIQkylQAVGMFRDFndtSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVS------EMKKD 388
Cdd:PRK12466 243 DYL--RGRPRApKGALWD---AALAYWRTL---RSDADavFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpAAEAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 389 FESCLGAKQGFKGFQVAPDRHndrktflysnseftLAHGSVVIAAITSCTNtsnpsvmlgaG----LLAKKAVEAGLSVK 464
Cdd:PRK12466 315 PARRAAMERALDYMGLTPGTP--------------LAGIPIDRVFIGSCTN----------GriedLRAAAAVLRGRKVA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 465 PYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGnsgplpepvveaiTQGDLVAVG---VLSGNRNFEGR 541
Cdd:PRK12466 371 PGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA-------------MNDDVLAPGercASTTNRNFEGR 437
|
490 500
....*....|....*....|...
gi 110347487 542 VHPNTRAnYLASPPLVIAYAIAG 564
Cdd:PRK12466 438 QGPGART-HLMSPAMVAAAAVAG 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
762-837 |
7.57e-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: 87.52 E-value: 7.57e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347487 762 AGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGEtaDSLGLTGRERYTI 837
Cdd:cd00404 13 PAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE--DYLKLHTGDELDI 86
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
671-818 |
9.70e-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: 85.57 E-value: 9.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 671 LGDSVTTDHISPAGniarnspaARYLTNRgltprefnsygsrrgndaimargtfANIRLLNKFlnkqapqtvhlpsgeTL 750
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLR-------------------------SNIPAISEF---------------VF 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 751 DVFDA--AERYQQAGlPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEY 818
Cdd:cd01579 34 HRVDPtfAERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
225-566 |
3.59e-15 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 79.01 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 225 EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGV---VGKFVEFFGPGVAQLSIADRATIANMCP 301
Cdd:PRK05478 148 EVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 302 EYGATAAFFPVDEVSIAYLlqTGREedkvkHIQK---YLQAVGMFRDFNdTSQDPDFTQVVELDLKTVVPCCSGPKRPQD 378
Cdd:PRK05478 225 EAGARAGLVAPDETTFEYL--KGRP-----FAPKgedWDKAVAYWKTLK-SDEDAVFDKVVTLDAADIEPQVTWGTNPGQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 379 KVAVSEMKKDFESclgakqgfkgFQVAPDRHNDRKTFLYSNseftLAHG------SVVIAAITSCTNtsnpsvmlgaG-- 450
Cdd:PRK05478 297 VISIDGKVPDPED----------FADPVKRASAERALAYMG----LKPGtpitdiKIDKVFIGSCTN----------Sri 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 451 --LLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDLV 527
Cdd:PRK05478 353 edLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLPP--------GERC 424
|
330 340 350
....*....|....*....|....*....|....*....
gi 110347487 528 AVgvlSGNRNFEGRVHPNTRaNYLASPPLVIAYAIAGTV 566
Cdd:PRK05478 425 AS---TSNRNFEGRQGKGGR-THLVSPAMAAAAAITGHF 459
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
676-830 |
9.58e-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: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 676 TTDHISPAGniarnsPAARYltnrgltprefnsygsrrgndaimaRGTFANIRllNKFL-------NKQAPQTVHLPSGE 748
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIS--NNLLigainaeNGKANSVKNQVTGE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 749 TLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYL--------- 819
Cdd:cd01578 54 YGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAdpadydkih 133
|
170
....*....|.
gi 110347487 820 PGETADSLGLT 830
Cdd:cd01578 134 PDDKVDILGLT 144
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
672-861 |
2.20e-13 |
|
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: 69.82 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 672 GDSVTTDHISPAgniarnspaaRYLtnRGLTPREFnsygsrrgndaimARGTFANIRLLNK-----FLNkqapqtvhlps 746
Cdd:COG0066 15 GDNIDTDQIIPA----------RFL--KTIDREGL-------------GKHLFEDWRYDRSpdpdfVLN----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 747 getldvfdaAERYQQAGlplIVLAGKEYGSGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEyLPGET 823
Cdd:COG0066 59 ---------QPRYQGAD---ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEA 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110347487 824 ADSL--GLTGRERYTINIpeDLkPRMTvqIKLDTGKTFQA 861
Cdd:COG0066 123 VDALfaAIEANPGDELTV--DL-EAGT--VTNGTGETYPF 157
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
764-833 |
2.45e-11 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 60.68 E-value: 2.45e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347487 764 LPLIVLAGKEYGSGSSR---DWAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRE 833
Cdd:cd01577 17 LGDIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE 86
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
767-885 |
1.18e-09 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 57.82 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 767 IVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEylpgetADSLGLTGRERYTINIpedlkpr 846
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEGIKDGDEVTVDL------- 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 110347487 847 MTVQIKLDTGKTFqaVMRFDTDVELTYFHNGGILNYMIR 885
Cdd:TIGR02087 117 ETGEIRVNGNEEY--KGEPLPDFLLEILREGGLLEYLKK 153
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
170-328 |
3.12e-09 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 60.79 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 170 IPPGSGIIHQVNLEYLArvvfdqdGCyyPDSLVGTDSHT------TMidglgvlgwgvggieaeAV----------MLGQ 233
Cdd:PRK11413 123 VPPHIAVIHQYMREMMA-------GG--GKMILGSDSHTrygalgTM-----------------AVgegggelvkqLLND 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 234 PISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVV-GKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPV 312
Cdd:PRK11413 177 TYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQT 256
|
170
....*....|....*.
gi 110347487 313 DEVSIAYLLQTGREED 328
Cdd:PRK11413 257 DEEVHNWLALHGRGQD 272
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
767-817 |
5.49e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 56.35 E-value: 5.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 110347487 767 IVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLE 817
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFE 102
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
767-889 |
8.06e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 52.52 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 767 IVLAGKEYGSGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEYlpGETADSLGlTGRErytINIpeDL 843
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGLPVLEC--DEAVDKIE-DGDE---VEV--DL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 110347487 844 KprmTVQIK-LDTGKTFQA-----VMRfdtdvELtyFHNGGILNYMIRKMAQ 889
Cdd:PRK00439 120 E---TGVITnLTTGEEYKFkpipeFML-----EI--LKAGGLIEYLKKKGRF 161
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
757-827 |
4.73e-06 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 48.20 E-value: 4.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347487 757 ERYQQAGlplIVLAGKEYGSGSSRD---WAakgpfLL--GIKAVLAESYERIHRSNLVGMGVIPLEyLPGETADSL 827
Cdd:PRK01641 63 PRYQGAS---ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDEL 129
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
671-817 |
2.07e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 47.16 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347487 671 LGDSVTTDHISPAGniarnspaarYLTNRGLTPREFNSYGSrrgndaimargtFANIRLlnkflnKQAPQTVHLPSGETl 750
Cdd:PLN00072 76 VGDNIDTDQIIPAE----------YLTLVPSKPDEYEKLGS------------YALIGL------PAFYKTRFVEPGEM- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347487 751 dvfdaAERYQqaglplIVLAGKEYGSGSSRDWAakgPFLLG---IKAVLAESYERIHRSNLVGMG-VIPLE 817
Cdd:PLN00072 127 -----KTKYS------IIIGGENFGCGSSREHA---PVALGaagAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| |
