|
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: 1604.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 3 NPFAHLAEPLDPAQpGKKFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFKPAR 82
Cdd:PTZ00092 14 NPFEKVLKTLKDGG-SYKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 83 VILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQ 162
Cdd:PTZ00092 93 VLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 163 AFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQV 242
Cdd:PTZ00092 173 AFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 243 IGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAYLVQ 322
Cdd:PTZ00092 253 VGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 323 TGREEDKVKHIKRYLQAVGMFRDfsdSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFESCLGAKQGFKGF 402
Cdd:PTZ00092 333 TGRSEEKVELIEKYLKANGLFRT---YAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 403 QVAPDHHNDHKTFIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYL 482
Cdd:PTZ00092 410 GIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 483 RESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAI 562
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYAL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 563 AGTVRIDFEKEPLGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTY 642
Cdd:PTZ00092 570 AGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTY 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 643 IKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARG 722
Cdd:PTZ00092 650 IHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRG 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 723 TFANIRLLNKFLNKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYER 802
Cdd:PTZ00092 730 TFANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFER 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 803 IHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTIHIPE-DLKPRMKVQIKLDTGKTFQAVMRFDTDVELTYFHNGGILN 881
Cdd:PTZ00092 810 IHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGILQ 889
|
....*...
gi 1938523080 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: 1485.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 17 PGKK--FFNLNKLEDSRYG---RLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFKPARVILQDFTGV 91
Cdd:PRK09277 16 GGKSydYYSLRALEAKGLGdisRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIPFRPARVVMQDFTGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 92 PAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFCNMRIIP 171
Cdd:PRK09277 96 PAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFLKWGQKAFDNFRVVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 172 PGSGIIHQVNLEYLARVVF-DQDGC--YYPDSLVGTDSHTTMIDglgvlgwgvggIEAEAVMLGQPISMVLPQVIGYKLM 248
Cdd:PRK09277 176 PGTGICHQVNLEYLAPVVWtREDGElvAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPSSMLIPEVVGVKLT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 249 GKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAYLVQTGREED 328
Cdd:PRK09277 256 GKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 329 KVKHIKRYLQAVGMFRDfsdSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFESCLGAKQGFKGFQVAPdh 408
Cdd:PRK09277 336 QVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQGFGLDEAE-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 409 hndhktfiyNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYLRESGVM 488
Cdd:PRK09277 411 ---------EGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 489 PYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRI 568
Cdd:PRK09277 482 PYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDI 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 569 DFEKEPLGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPF 648
Cdd:PRK09277 562 DLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPY 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 649 FESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIR 728
Cdd:PRK09277 642 FEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIR 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 729 LLNKFLN-KQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSN 807
Cdd:PRK09277 722 IRNEMVPgVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSN 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 808 LVGMGVIPLEYLPGETADSLGLTGRERYTIHIPEDLKPR--MKVQIKLDTG--KTFQAVMRFDTDVELTYFHNGGILNYM 883
Cdd:PRK09277 802 LVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGatVTVVITRADGevVEFPVLCRIDTAVEVDYYRNGGILQYV 881
|
....*.
gi 1938523080 884 IRKMAQ 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: 1473.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 21 FFNLNKLEDSRYG--RLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFKPARVILQDFTGVPAVVDFA 98
Cdd:COG1048 20 YYSLPALEEAGGDisRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVLMQDFTGVPAVVDLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 99 AMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFCNMRIIPPGSGIIH 178
Cdd:COG1048 100 AMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAFDNFRVVPPGTGIVH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 179 QVNLEYLARVVF--DQDG--CYYPDSLVGTDSHTTMIDglgvlgwgvggIEAEAVMLGQPISMVLPQVIGYKLMGKPHPL 254
Cdd:COG1048 180 QVNLEYLAFVVWtrEEDGetVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 255 VTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAYLVQTGREEDKVKHIK 334
Cdd:COG1048 260 VTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIELVE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 335 RYLQAVGMFRDfsDSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFESCLGAKQGfkgfqvapDHHNDHKT 414
Cdd:COG1048 340 AYAKAQGLWRD--PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG--------EELDKPVR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 415 FIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQL 494
Cdd:COG1048 410 VEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEAL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 495 GFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRIDFEKEP 574
Cdd:COG1048 490 GFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLTTDP 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 575 LGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPFFESLTL 654
Cdd:COG1048 570 LGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEGLQL 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 655 DLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIRLLNKFL 734
Cdd:COG1048 650 EPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKNLLA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 735 -NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGV 813
Cdd:COG1048 730 pGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGV 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 814 IPLEYLPGETADSLGLTGRERYTIH-IPEDLKPRMKVQIKLD----TGKTFQAVMRFDTDVELTYFHNGGILNYMIRKMA 888
Cdd:COG1048 810 LPLQFPEGESAESLGLTGDETFDIEgLDEGLAPGKTVTVTATradgSTEEFPVLHRIDTPVEVEYYRAGGILQYVLRQLL 889
|
.
gi 1938523080 889 Q 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: 1359.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 2 KNPFAHLAEPLDPAQPGK--KFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFK 79
Cdd:PLN00070 42 ENPFKGILTSLPKPGGGEfgKYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 80 PARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKW 159
Cdd:PLN00070 122 PARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 160 GSQAFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVL 239
Cdd:PLN00070 202 GSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 240 PQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAY 319
Cdd:PLN00070 282 PGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 320 LVQTGREEDKVKHIKRYLQAVGMFRDFSDSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFESCLGAKQGF 399
Cdd:PLN00070 362 LKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGF 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 400 KGFQVAPDHHNDHKTFIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVT 479
Cdd:PLN00070 442 KGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVT 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 480 YYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:PLN00070 522 KYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVA 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 560 YAIAGTVRIDFEKEPLGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPK 639
Cdd:PLN00070 602 YALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 640 STYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIM 719
Cdd:PLN00070 682 STYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIM 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 720 ARGTFANIRLLNKFLNKQ-APQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAE 798
Cdd:PLN00070 762 ARGTFANIRIVNKLLKGEvGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAK 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 799 SYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTIHIP---EDLKPRMKVQIKLDTGKTFQAVMRFDTDVELTYFH 875
Cdd:PLN00070 842 SFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPsniSEIKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFD 921
|
890
....*....|....
gi 1938523080 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: 1295.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 21 FFNLNKLEDS--RYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFKPARVILQDFTGVPAVVDFA 98
Cdd:TIGR01341 5 YYSLKALEESggKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAVVDLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 99 AMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFCNMRIIPPGSGIIH 178
Cdd:TIGR01341 85 AMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGTGIIH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 179 QVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPL 254
Cdd:TIGR01341 165 QVNLEYLATVVFkaevDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 255 VTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAYLVQTGREEDKVKHIK 334
Cdd:TIGR01341 245 VTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVELVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 335 RYLQAVGMFRDFSDssqDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFESCLGAKQGFKGFQVapdhHNDHKT 414
Cdd:TIGR01341 325 KYARAQGLFYDDSE---EPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTL----RKEPLK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 415 FIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQL 494
Cdd:TIGR01341 398 KKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEEL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 495 GFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRIDFEKEP 574
Cdd:TIGR01341 478 GFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 575 LGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPFFESLTL 654
Cdd:TIGR01341 558 IGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 655 DLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIRLLNKFL 734
Cdd:TIGR01341 638 DPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMV 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 735 -NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGV 813
Cdd:TIGR01341 718 kGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGV 797
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1938523080 814 IPLEYLPGETADSLGLTGRERYTIHIPEDLKPRMKVQIKLDTGK----TFQAVMRFDTDVELTYFHNGGILNYMIRKM 887
Cdd:TIGR01341 798 IPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-889 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1281.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 1 MKNPFAHLAEpLDPAQPGKKFFNLNKLE---DSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVP 77
Cdd:PRK12881 2 AHNLHKTLKE-FDVGGKTYKFYSLPALGkelGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 78 FKPARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFL 157
Cdd:PRK12881 81 FVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 158 KWGSQAFCNMRIIPPGSGIIHQVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQ 233
Cdd:PRK12881 161 KWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHtkedDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 234 PISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVD 313
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 314 NVSIAYLVQTGREEDKVKHIKRYLQAVGMFRDfsdSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFESCL 393
Cdd:PRK12881 321 EQTLDYLRLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 394 GAKQGFKGFQVAPDHHNDHktfiyndsefTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSP 473
Cdd:PRK12881 398 SKPVAENGFAKKAQTSNGV----------DLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 474 GSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLAS 553
Cdd:PRK12881 468 GSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLAS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 554 PPLVIAYAIAGTVRIDFEKEPLGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKL 633
Cdd:PRK12881 548 PPLVVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 634 YAWNPKSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRR 713
Cdd:PRK12881 628 YDWDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRR 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 714 GNDAIMARGTFANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGI 792
Cdd:PRK12881 708 GNHEVMMRGTFANVRIKNLMIpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 793 KAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTIH-IPEDLKPRM--KVQIKLDTGKT--FQAVMRFDT 867
Cdd:PRK12881 788 KAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRQdvTLVIHRADGSTerVPVLCRIDT 867
|
890 900
....*....|....*....|..
gi 1938523080 868 DVELTYFHNGGILNYMIRKMAQ 889
Cdd:PRK12881 868 PIEVDYYKAGGILPYVLRQLLA 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: 791.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 82 RVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGS 161
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 162 QAFCNMRIIPPGSGIIHQVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISM 237
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 238 VLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDnvsi 317
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 318 aylvqtgreedkvkhikrylqavgmfrdfsdssqdpdfTQVVELDLKTVVPCCSGPKRPQDKVAVsemkrdfesclgakq 397
Cdd:cd01586 237 --------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 398 gfkgfqvapdhhndhktfiyndseftlaHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGV 477
Cdd:cd01586 264 ----------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 478 VTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLV 557
Cdd:cd01586 316 VTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLV 395
|
....*....
gi 1938523080 558 IAYAIAGTV 566
Cdd:cd01586 396 VAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
70-564 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 628.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 70 QHKSIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSiqvdfnrrADSLQKNQDLEFER 149
Cdd:pfam00330 10 EELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 150 NRERFEFLKWGSQAFcNMRIIPPGSGIIHQVNLEYlarvvfdqdGCYYPD-SLVGTDSHTTM----------IDGlgvlg 218
Cdd:pfam00330 82 NKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEY---------GLALPGmTIVGTDSHTTThgglgalafgVGG----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 219 wgvggIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIAN 298
Cdd:pfam00330 147 -----SEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 299 MCPEYGATAAFFPVDNVSIAYLVQTGREEDKVkhIKRYLQAVGMFRDFSDSsqDPDFTQVVELDLKTVVPCCSGPKRPQD 378
Cdd:pfam00330 222 MAIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDP--GAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 379 KVAVSEMKRD-FESCLGAKQGFKGFQvapdhhndhktFIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLaKKAV 457
Cdd:pfam00330 298 AVPLSELVPDpFADAVKRKAAERALE-----------YMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 458 EAGLNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEpvveaitqGDlvaVGVLSGNRN 537
Cdd:pfam00330 366 EKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--------GE---RCVSSSNRN 434
|
490 500
....*....|....*....|....*..
gi 1938523080 538 FEGRVHPNTRAnYLASPPLVIAYAIAG 564
Cdd:pfam00330 435 FEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
670-837 |
2.19e-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: 341.18 E-value: 2.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 670 NLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIRLLNKFLNKQAPQ-TVHLPSGE 748
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGtTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 749 TLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLG 828
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
....*....
gi 1938523080 829 LTGRERYTI 837
Cdd:cd01580 161 LTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
82-566 |
1.34e-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: 313.28 E-value: 1.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 82 RVILQDFTGVPAVVDFAAMRDAVKklggnpekINPVCPADLVIDHSIQvdfnrradslqknqdLEFERNRERFEFLKWgS 161
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 162 QAFCNMRIIPPGSGIIHQVNLEYLArvvfdqdgcYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENLA---------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 242 VIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAYLV 321
Cdd:cd01351 128 VVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 322 QTGREEDKVKhikrylqaVGMFRDFSDSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRdfesclgakqgfkg 401
Cdd:cd01351 208 ATGRPLLKNL--------WLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 402 fqvapdhhndhktfiyndseftlahGSVVIAAITSCTNtSNPSVMLGAGLLAKKAVeaglnVKPYVKTSLSPGSGVVTYY 481
Cdd:cd01351 266 -------------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYAT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 482 LRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPepvveaitqgDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYA 561
Cdd:cd01351 315 LSREGYYEILVDSGARILPPGCGPCMGNGARLV----------ADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATA 384
|
....*
gi 1938523080 562 IAGTV 566
Cdd:cd01351 385 IAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
75-889 |
1.47e-83 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 281.65 E-value: 1.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 75 EVPFKPARVILQDFTGVPAVVDFAAM-RDAVK-KLggnpekinpvcpADLVIDHS-IQVDFnrradslqknqdlefeRNR 151
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgLDRVKtEL------------SVQYVDHNlLQADF----------------ENA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 152 ERFEFLKWGSQAFcNMRIIPPGSGIIHQVNLEYLARvvfdqdgcyyP-DSLVGTDSHTT------MIdglgvlgwgvgGI 224
Cdd:PRK07229 76 DDHRFLQSVAAKY-GIYFSKPGNGICHQVHLERFAF----------PgKTLLGSDSHTPtagglgML-----------AI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 225 -----EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGV---VGKFVEFFGPGVAQLSIADRATI 296
Cdd:PRK07229 134 gagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILEL---LRRLTVkggVGKIIEYFGPGVATLSVPERATI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 297 ANMCPEYGATAAFFPVDNVSIAYLVQTGREEDKVKhikryLQAvgmfrdfsdssqDPD--FTQVVELDLKTVVPCCSGPK 374
Cdd:PRK07229 211 TNMGAELGATTSIFPSDERTREFLKAQGREDDWVE-----LLA------------DPDaeYDEVIEIDLSELEPLIAGPH 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 375 RPQDKVAVSEMKrdfesclGAKqgfkgfqvapdhhndhktfiyndseftlahgsVVIAAITSCTNTSNPSVMLGAGLLAK 454
Cdd:PRK07229 274 SPDNVVPVSEVA-------GIK--------------------------------VDQVLIGSCTNSSYEDLMRAASILKG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 455 KaveaglNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGplpEPVVEAITqgdlvavgVLSG 534
Cdd:PRK07229 315 K------KVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNVS--------LRTF 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 535 NRNFEGRV-HPNTRAnYLASPPLVIAYAIAGtvRIDfekEPLGvnaqgqqvfLKDIWPTRDEIQEVERKYVIPGMF---K 610
Cdd:PRK07229 378 NRNFPGRSgTKDAQV-YLASPETAAASALTG--VIT---DPRT---------LALENGEYPKLEEPEGFAVDDAGIiapA 442
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 611 EVYQKIETVnkswnalaapseklyawnpKSTYIKSPPffesltlDLQPPKSIVDAYVLLNLGDSVTTDHISPAGniarns 690
Cdd:PRK07229 443 EDGSDVEVV-------------------RGPNIKPLP-------LLEPLPDLLEGKVLLKVGDNITTDHIMPAG------ 490
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 691 paARYLtnrgltprdfnSYgsrRGN-DAImARGTFanIRLLNKFlnkqapqtvhlpsgetldvfdaAERYQQAGlPLIVL 769
Cdd:PRK07229 491 --AKWL-----------PY---RSNiPNI-SEFVF--EGVDNTF----------------------PERAKEQG-GGIVV 528
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 770 AGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLgltgRERYTIHIP--EDLKPRM 847
Cdd:PRK07229 529 GGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKI----EEGDVLEIEdlREFLPGG 604
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1938523080 848 KVQIKLDT-GKTFQAVMRFdTDVELTYFHNGGILNYMIRKMAQ 889
Cdd:PRK07229 605 PLTVVNVTkDEEIEVRHTL-SERQIEILLAGGALNLIKKKLAA 646
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
692-821 |
1.69e-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: 182.18 E-value: 1.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 692 AARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLA 770
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1938523080 771 GKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPG 821
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
84-566 |
2.32e-46 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 170.71 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 84 ILQDFTGVPAVVDFAAMrdavkklgGNPEKINPVCPAdlVIDHS-IQVDFnrradslqknqdlefeRNRERFEFLKWGSQ 162
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--------GVDRVRTELSVS--YVDHNtLQTDF----------------ENADDHRFLQTVAA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 163 AFcNMRIIPPGSGIIHQVNLEYLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQ 241
Cdd:cd01585 58 RY-GIYFSRPGNGICHQVHLERFAV----------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 242 VIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIAYLV 321
Cdd:cd01585 127 VVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 322 QTGREEDKVKhikryLQAvgmfrdfsdssqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEMkrdfesclgakQGF 399
Cdd:cd01585 207 AQGREDDWVE-----LAA------------DADaeYDEEIEIDLSELEPLIARPHSPDNVVPVREV-----------AGI 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 400 KGFQVapdhhndhktfiyndseftlahgsvviaAITSCTNTSNPSVMLGAGLLakkaveAGLNVKPYVKTSLSPGSGVVT 479
Cdd:cd01585 259 KVDQV----------------------------AIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAPGSKQVL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 480 YYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPvveaitqgdlvAVGVLSGNRNFEGRVHPNTRANYLASPPLVIA 559
Cdd:cd01585 305 EMLARNGALADLLAAGARILESACGPCIGMGQAPPTG-----------GVSVRTFNRNFEGRSGTKDDLVYLASPEVAAA 373
|
....*..
gi 1938523080 560 YAIAGTV 566
Cdd:cd01585 374 AALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
82-565 |
3.71e-46 |
|
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: 171.08 E-value: 3.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 82 RVILQDFTGVPAVVDFAAmrdavkklGGNPEkinPVCPADLVIDHSIQVdfnrradSLQKNQDLEF--ERNRERFEFLKW 159
Cdd:cd01584 1 RVAMQDATAQMALLQFMS--------SGLPK---VAVPSTIHCDHLIEA-------QVGGEKDLKRakDINKEVYDFLAS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 160 GSQAFcNMRIIPPGSGIIHQVNLEYLArvvfdqdgcyYPDSL-VGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMV 238
Cdd:cd01584 63 AGAKY-GIGFWKPGSGIIHQIVLENYA----------FPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 239 LPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSIA 318
Cdd:cd01584 132 CPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 319 YLVQTGREEdkvkhIKRYLQAVGMFRDFSDSSQDPDftQVVELDLKTVVPCCSGPKRPQDKVAVSEMKRDFEsclgaKQG 398
Cdd:cd01584 212 YLKATGRAE-----IADLADEFKDDLLVADEGAEYD--QLIEINLSELEPHINGPFTPDLATPVSKFKEVAE-----KNG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 399 FkgfqvaPDhhndhktfiyndseftlahgSVVIAAITSCTNTSNPSvMLGAGLLAKKAVEAGLNVKpyVKTSLSPGSGVV 478
Cdd:cd01584 280 W------PL--------------------DLRVGLIGSCTNSSYED-MGRAASIAKQALAHGLKCK--SIFTITPGSEQI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 479 TYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPlpepvvEAITQGDLVAVgVLSGNRNFEGR--VHPNTRAnYLASPPL 556
Cdd:cd01584 331 RATIERDGLLQTFRDAGGIVLANACGPCIGQWDR------KDIKKGEKNTI-VTSYNRNFTGRndANPATHA-FVASPEI 402
|
....*....
gi 1938523080 557 VIAYAIAGT 565
Cdd:cd01584 403 VTAMAIAGT 411
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
82-566 |
7.67e-41 |
|
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: 154.65 E-value: 7.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 82 RVILQDFTGVPAvvdFAAMRDAVKKLGGNPEKINpvcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNRERF--EFLKW 159
Cdd:cd01583 1 LHLVHDVTSPQA---FEGLREAGREKVWDPEKIV------AVFDHNVPTP-----DIKAAEQVKTLRKFAKEFgiNFFDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 160 GSQafcnmriippgsGIIHQVNLE-YLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISM 237
Cdd:cd01583 67 GRQ------------GICHVILPEkGLTL----------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 238 VLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSI 317
Cdd:cd01583 125 RVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 318 AYLVqtGREEDKVKHIKrylqavgmfrdfsdSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEmkrdfesclgakq 397
Cdd:cd01583 205 EYLK--GRGKAYWKELK--------------SDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSE------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 398 gfkgfqvapdhhndhktfiyndseftLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKaveaglNVKPYVKTSLSPGSGV 477
Cdd:cd01583 256 --------------------------VEGIKIDQVFIGSCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPASQR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 478 VTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEPVVEAITQgdlvavgvlsgNRNFEGRVHPNTRANYLASPPL 556
Cdd:cd01583 304 VYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAPGERCVSTS-----------NRNFKGRMGSPGARIYLASPAT 372
|
490
....*....|
gi 1938523080 557 VIAYAIAGTV 566
Cdd:cd01583 373 AAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
82-566 |
3.00e-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: 142.09 E-value: 3.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 82 RVILQDFTGVPAvvdFAAMRdavkKLGG----NPEKInpVcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNRERFefl 157
Cdd:COG0065 30 LHLVHDVTSPQA---FEGLR----EAGGrkvwDPDRI--V----AVFDHNVPTK-----DPKSAEQVKTLREFAKEF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 158 kwgsqafcNMRIIPPGS-GIIHQVNLEY-LARvvfdqdgcyyP-DSLVGTDSHTTM----------IDGLgvlgwgvggi 224
Cdd:COG0065 89 --------GITFFDVGDpGICHVVLPEQgLVL----------PgMTIVGGDSHTCThgafgafafgIGTT---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 225 EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYG 304
Cdd:COG0065 141 DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 305 ATAAFFPVDNVSIAYLVQTGREEDKVKHikrylqavgmfrdfSDSsqDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSE 384
Cdd:COG0065 221 AKAGIIAPDETTFEYLKGRPFAPWRTLK--------------SDE--DAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 385 MKrdfesclgakqgfkgfQVAPDHhndhktfiyndseftlahgsvviAAITSCTNtsnpsvmlgaG----LLAKKAVEAG 460
Cdd:COG0065 285 LE----------------GIKIDQ-----------------------VFIGSCTN----------GriedLRAAAEILKG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 461 LNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDlvaVGVLSGNRNFE 539
Cdd:COG0065 316 RKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAP--------GE---RCASTSNRNFE 384
|
490 500
....*....|....*....|....*...
gi 1938523080 540 GRV-HPNTRAnYLASPPLVIAYAIAGTV 566
Cdd:COG0065 385 GRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
83-564 |
2.22e-28 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 118.74 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 83 VILQDFTGVPAVVDFaamrdavKKLGG----NPEKINpvcpadLVIDHSIQVDfNRRADSLQKnqdleFERnrerfEFLK 158
Cdd:PRK00402 31 VMAHDITGPLAIKEF-------EKIGGdkvfDPSKIV------IVFDHFVPAK-DIKSAEQQK-----ILR-----EFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 159 wgSQAFCNMRIIppGSGIIHQVNLEY-LARvvfdqdgcyyP-DSLVGTDSHTT----------------Midglgvlgwg 220
Cdd:PRK00402 87 --EQGIPNFFDV--GEGICHQVLPEKgLVR----------PgDVVVGADSHTCtygalgafatgmgstdM---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 221 vggieAEAVMLGQpISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGVVG---KFVEFFGPGVAQLSIADRATIA 297
Cdd:PRK00402 143 -----AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHI---IGDIGVDGatyKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 298 NMCPEYGATAAFFPVDNVSIAYLVQTGREEDKVKHikrylqavgmfrdfsdSSQDPDFTQVVELDLKTVVPCCSGPKRPQ 377
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLKERAGRDYKPWK----------------SDEDAEYEEVYEIDLSKLEPQVAAPHLPD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 378 DKVAVSEMKRdfesclgakqgfkgfqVAPDHhndhktfiyndseftlahgsVVIAaitSCTNtsnpsvmlgaGLLAKKAV 457
Cdd:PRK00402 278 NVKPVSEVEG----------------TKVDQ--------------------VFIG---SCTN----------GRLEDLRI 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 458 EA----GLNVKPYVKTSLSPGSGVVtyYLR--ESGVMPYLSQLGFdVVGY-GCMTCIGNS-GPLPEpvveaitqGDlvaV 529
Cdd:PRK00402 309 AAeilkGRKVAPGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHmGVLAP--------GE---V 374
|
490 500 510
....*....|....*....|....*....|....*.
gi 1938523080 530 GVLSGNRNFEGRV-HPNTRAnYLASPPLVIAYAIAG 564
Cdd:PRK00402 375 CLSTTNRNFKGRMgSPESEV-YLASPAVAAASAVTG 409
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
110-566 |
5.24e-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: 101.92 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 110 NPEKInpVCpadlVIDHSIQvdfNRRADSLQKNQDLEFERNRERFEFLkwgsqafcnmriiPPGSGIIHQVNLEylarvv 189
Cdd:cd01582 25 NPDQI--VM----TLDHDVQ---NKSEKNLKKYKNIESFAKKHGIDFY-------------PAGRGIGHQIMIE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 190 fdqDGCYYPDSL-VGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHL 268
Cdd:cd01582 77 ---EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 269 RQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDnvsiaylvqtgreedkVKHIKrylqavgmfrdfsd 348
Cdd:cd01582 154 NKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD----------------AKHLI-------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 349 ssqdpdftqvveLDLKTVVPCCSGPkrpqDKVAVSEMKRDFEsclgaKQGFKgfqvapdhhndhktfiyndseftlahgs 428
Cdd:cd01582 204 ------------LDLSTLSPYVSGP----NSVKVSTPLKELE-----AQNIK---------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 429 VVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLN-VKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCI 507
Cdd:cd01582 235 INKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIpVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCI 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1938523080 508 GNSGPLPEPvveaitqGDlvaVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTV 566
Cdd:cd01582 315 GLGQGLLEP-------GE---VGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
73-564 |
4.92e-22 |
|
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: 99.84 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 73 SIEVpfKPARVILQDFTGVPAvvdFAAMRDAVKKLGGNPEKINpvcpadLVIDHSIQVDFNRRAdslqknqdlefERNRE 152
Cdd:TIGR02086 21 IVEV--EVDLAMTHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNVPPPTVEAA-----------EMQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 153 RFEFLKwgsqafcNMRI--IPPGSGIIHQVnleyLARVVFDQDGcyypDSLVGTDSHTTMIDGLGVLGWGVGGIE-AEAV 229
Cdd:TIGR02086 79 IREFAK-------RHGIknFDVGEGICHQI----LAEEGYALPG----MVVVGGDSHTCTSGAFGAFATGMGATDmAIAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 230 MLGQPISMVlPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAF 309
Cdd:TIGR02086 144 ATGKTWIKV-PETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 310 FPVDNVSIAYLVQTGREEdkvkhikrylqavgmfrdFSDSSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEMkr 387
Cdd:TIGR02086 223 IEPDEETYEYLKKRRGLE------------------FRILVPDPGanYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDV-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 388 dfesclgakQGFKGFQVapdhhndhktfiyndseFtlahgsvviaaITSCTNTSNPSVMLGAGLLAkkaveaGLNVKPYV 467
Cdd:TIGR02086 283 ---------EGTEIDQV-----------------F-----------IGSCTNGRLEDLRIAAEILK------GRRVHPDV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 468 KTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDLVavgVLSGNRNFEGRV-HPN 545
Cdd:TIGR02086 320 RLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGaHMGVLGD--------GEVC---LSTTNRNFKGRMgSPN 388
|
490
....*....|....*....
gi 1938523080 546 TRAnYLASPPLVIAYAIAG 564
Cdd:TIGR02086 389 AEI-YLASPATAAASAVEG 406
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
82-564 |
4.75e-21 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 97.28 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 82 RVILQDFTGVPAvvdFAAMRDAVKKLGgNPEKinpvcpADLVIDHSIQVDFNRRA---DSLQKNQDLEFERNRERFeflk 158
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTVR-RPDL------TLAVVDHVVPTRPGRDRgitDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 159 wGSQAFcnmRIIPPGSGIIHqvnleylarVVFDQDGCYYPDSLVGT-DSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISM 237
Cdd:PRK12466 96 -GIRLF---DVDDPRQGIVH---------VVAPELGLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLVY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 238 VLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDNVSI 317
Cdd:PRK12466 163 RKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 318 AYLvqTGREEDKVKHikRYLQAVGMFRDFSdSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVS------EMKRDFES 391
Cdd:PRK12466 243 DYL--RGRPRAPKGA--LWDAALAYWRTLR-SDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpAAEADPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 392 CLGAKQGFKGFQVAPDHHndhktfiyndseftLAHGSVVIAAITSCTNtsnpsvmlgaG----LLAKKAVEAGLNVKPYV 467
Cdd:PRK12466 318 RAAMERALDYMGLTPGTP--------------LAGIPIDRVFIGSCTN----------GriedLRAAAAVLRGRKVAPGV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 468 KTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGnsgplpepvveaiTQGDLVAVG---VLSGNRNFEGRVHP 544
Cdd:PRK12466 374 RAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA-------------MNDDVLAPGercASTTNRNFEGRQGP 440
|
490 500
....*....|....*....|
gi 1938523080 545 NTRAnYLASPPLVIAYAIAG 564
Cdd:PRK12466 441 GART-HLMSPAMVAAAAVAG 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
762-837 |
7.64e-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: 7.64e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938523080 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 |
1.10e-19 |
|
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: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 671 LGDSVTTDHISPAGniarnspaARYLTNRgltprdfnsygsrrgndaimargtfANIRLLNKFlnkqapqtvhlpsgeTL 750
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLR-------------------------SNIPAISEF---------------VF 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 751 DVFDA--AERYQQAGlPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEY 818
Cdd:cd01579 34 HRVDPtfAERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
676-830 |
1.02e-13 |
|
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: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 676 TTDHISPAGniarnsPAARYltnrgltprdfnsygsrrgndaimaRGTFANIRllNKFL-------NKQAPQTVHLPSGE 748
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIS--NNLLigainaeNGKANSVKNQVTGE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 749 TLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYL--------- 819
Cdd:cd01578 54 YGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAdpadydkih 133
|
170
....*....|.
gi 1938523080 820 PGETADSLGLT 830
Cdd:cd01578 134 PDDKVDILGLT 144
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
225-566 |
1.21e-13 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 74.39 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 225 EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGV---VGKFVEFFGPGVAQLSIADRATIANMCP 301
Cdd:PRK05478 148 EVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 302 EYGATAAFFPVDNVSIAYLvqTGRE-----EDkvkhikrYLQAVGMFRDF-SDSsqDPDFTQVVELDLKTVVPCCSGPKR 375
Cdd:PRK05478 225 EAGARAGLVAPDETTFEYL--KGRPfapkgED-------WDKAVAYWKTLkSDE--DAVFDKVVTLDAADIEPQVTWGTN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 376 PQDKVAVSEMKRDFESclgakqgfkgFQVAPDHHNDHKTFIYNDseftLAHG------SVVIAAITSCTNtsnpsvmlga 449
Cdd:PRK05478 294 PGQVISIDGKVPDPED----------FADPVKRASAERALAYMG----LKPGtpitdiKIDKVFIGSCTN---------- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 450 G----LLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqG 524
Cdd:PRK05478 350 SriedLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLPP--------G 421
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938523080 525 DLVAVgvlSGNRNFEGRVHPNTRaNYLASPPLVIAYAIAGTV 566
Cdd:PRK05478 422 ERCAS---TSNRNFEGRQGKGGR-THLVSPAMAAAAAITGHF 459
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
672-861 |
1.00e-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: 67.89 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 672 GDSVTTDHISPAgniarnspaaRYLTnrgLTPRDfnsygsrrgndaIMARGTFANIRLLNK-----FLNkqapqtvhlps 746
Cdd:COG0066 15 GDNIDTDQIIPA----------RFLK---TIDRE------------GLGKHLFEDWRYDRSpdpdfVLN----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 747 getldvfdaAERYQQAGlplIVLAGKEYGSGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEyLPGET 823
Cdd:COG0066 59 ---------QPRYQGAD---ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEA 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1938523080 824 ADSL--GLTGRERYTIHIpeDLKPRmkvQIKLDTGKTFQA 861
Cdd:COG0066 123 VDALfaAIEANPGDELTV--DLEAG---TVTNGTGETYPF 157
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
764-833 |
2.47e-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: 2.47e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938523080 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 |
4.94e-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: 55.89 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 767 IVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEylpgetADSLGLTGRERYTIhipeDLKpr 846
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEGIKDGDEVTV----DLE-- 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 1938523080 847 mKVQIKLDTGKTFqaVMRFDTDVELTYFHNGGILNYMIR 885
Cdd:TIGR02087 118 -TGEIRVNGNEEY--KGEPLPDFLLEILREGGLLEYLKK 153
|
|
| 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 1938523080 767 IVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLE 817
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFE 102
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
170-328 |
1.23e-08 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 58.87 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 170 IPPGSGIIHQVNLEYLArvvfdqdGCyyPDSLVGTDSHT------TMidglgvlgwgvggieaeAV----------MLGQ 233
Cdd:PRK11413 123 VPPHIAVIHQYMREMMA-------GG--GKMILGSDSHTrygalgTM-----------------AVgegggelvkqLLND 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 234 PISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVV-GKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPV 312
Cdd:PRK11413 177 TYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQT 256
|
170
....*....|....*.
gi 1938523080 313 DNVSIAYLVQTGREED 328
Cdd:PRK11413 257 DEEVHNWLALHGRGQD 272
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
767-889 |
1.34e-07 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 52.14 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938523080 767 IVLAGKEYGSGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEYlpGETADSLGlTGRErytihIPEDL 843
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGLPVLEC--DEAVDKIE-DGDE-----VEVDL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1938523080 844 KprMKVQIKLDTGKTFQA-----VMRfdtdvELtyFHNGGILNYMIRKMAQ 889
Cdd:PRK00439 120 E--TGVITNLTTGEEYKFkpipeFML-----EI--LKAGGLIEYLKKKGRF 161
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
757-827 |
4.60e-06 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 48.20 E-value: 4.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938523080 757 ERYQQAGlplIVLAGKEYGSGSSRD---WAakgpfLL--GIKAVLAESYERIHRSNLVGMGVIPLEyLPGETADSL 827
Cdd:PRK01641 63 PRYQGAS---ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDEL 129
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
767-817 |
2.70e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.78 E-value: 2.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1938523080 767 IVLAGKEYGSGSSRDWAakgPFLLG---IKAVLAESYERIHRSNLVGMG-VIPLE 817
Cdd:PLN00072 132 IIIGGENFGCGSSREHA---PVALGaagAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| |
