|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
3-887 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1608.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 3 FNNLIRNLAIGDNvYKYFDLNGLNDARYNELPISIKYLLEAAVRHCDEFHVLKKDVETILDWKNSQRNQAEIPFKPARVI 82
Cdd:PTZ00092 16 FEKVLKTLKDGGS-YKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPARVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 83 LQDFTGVPAVVDLAAMRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKWGSKAF 162
Cdd:PTZ00092 95 LQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSKAF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 163 DNLLIVPPGSGIVHQVNLEYLARTVFvGKDGVLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVI 242
Cdd:PTZ00092 175 KNLLIVPPGSGIVHQVNLEYLARVVF-NKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 243 GYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQT 322
Cdd:PTZ00092 254 GFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 323 GRDTDYTQRVEQYLKSVGMFVNFTDDsyrPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKGLTDKISFKAFG 402
Cdd:PTZ00092 334 GRSEEKVELIEKYLKANGLFRTYAEQ---IEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGFG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 403 LKPEDATKSVTITNHGRTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGSGVVTKYLE 482
Cdd:PTZ00092 411 IPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 483 ASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPPLAVLYSII 562
Cdd:PTZ00092 491 ASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALA 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 563 GNVNVDI-NGVLAVTPDGKEIRLADIWPTRKEVAKFEEEFVKPQFFREVYANIELGSTEWQQLECPAVKLYPWDDASTYI 641
Cdd:PTZ00092 571 GRVNIDFeTEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTYI 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 642 KKVPFFDGMTSELPSQSDIVNAHVLLNLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGNDEIMARGT 721
Cdd:PTZ00092 651 HNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRGT 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 722 FANIRLVNKLASKVGPITLHVPSGEELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERI 801
Cdd:PTZ00092 731 FANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERI 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 802 HRSNLIGMGIIPFQYQAGQNADSLGLTGKEQFSIGVP-DDLKPGQLIDVNVSNGSVFQVICRFDTEVELTYYRNGGILQY 880
Cdd:PTZ00092 811 HRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNsGELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGILQY 890
|
....*..
gi 17568399 881 MIRKLIQ 887
Cdd:PTZ00092 891 VLRKLVK 897
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
8-887 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1531.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 8 RNLAIGDNVYKYFDLNGLNDAR---YNELPISIKYLLEAAVRHCDEFHVLKKDVETILDWKNSQRNQAEIPFKPARVILQ 84
Cdd:PRK09277 11 KTLEVGGKSYDYYSLRALEAKGlgdISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIPFRPARVVMQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 85 DFTGVPAVVDLAAMRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKWGSKAFDN 164
Cdd:PRK09277 91 DFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFLKWGQKAFDN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 165 LLIVPPGSGIVHQVNLEYLARTVFVGKDG--VLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVI 242
Cdd:PRK09277 171 FRVVPPGTGICHQVNLEYLAPVVWTREDGelVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 243 GYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQT 322
Cdd:PRK09277 251 GVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 323 GRDTDYTQRVEQYLKSVGMFvnfTDDSYRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKglTDKISFKAFG 402
Cdd:PRK09277 331 GRDEEQVALVEAYAKAQGLW---RDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK--SAELGVQGFG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 403 LKPEDAtksvtitnhGRTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGSGVVTKYLE 482
Cdd:PRK09277 406 LDEAEE---------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 483 ASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPPLAVLYSII 562
Cdd:PRK09277 477 KAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 563 GNVNVDI-NGVLAVTPDGKEIRLADIWPTRKEVAKFEEEFVKPQFFREVYANIELGSTEWQQLECPAVKLYPWDDASTYI 641
Cdd:PRK09277 557 GTVDIDLeKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 642 KKVPFFDGMTSELPSQSDIVNAHVLLNLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGNDEIMARGT 721
Cdd:PRK09277 637 RNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGT 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 722 FANIRLVNKLASKV-GPITLHVPSGEELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFER 800
Cdd:PRK09277 717 FANIRIRNEMVPGVeGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFER 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 801 IHRSNLIGMGIIPFQYQAGQNADSLGLTGKEQFSIGVPDDLKPGQLIDVNV--SNGSV--FQVICRFDTEVELTYYRNGG 876
Cdd:PRK09277 797 IHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGATVTVVItrADGEVveFPVLCRIDTAVEVDYYRNGG 876
|
890
....*....|.
gi 17568399 877 ILQYMIRKLIQ 887
Cdd:PRK09277 877 ILQYVLRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
8-887 |
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: 1501.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 8 RNLAIGDNVYKYFDLNGLNDARYN--ELPISIKYLLEAAVRHCDEFHVLKKDVETILDWKNSQRNQAEIPFKPARVILQD 85
Cdd:COG1048 9 KTLTVGGKPYTYYSLPALEEAGGDisRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVLMQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 86 FTGVPAVVDLAAMRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKWGSKAFDNL 165
Cdd:COG1048 89 FTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAFDNF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 166 LIVPPGSGIVHQVNLEYLARTVFVGKDG---VLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVI 242
Cdd:COG1048 169 RVVPPGTGIVHQVNLEYLAFVVWTREEDgetVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 243 GYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQT 322
Cdd:COG1048 249 GVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 323 GRDTDYTQRVEQYLKSVGMFvnFTDDSYRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKGLTDkisfkafg 402
Cdd:COG1048 329 GRSEEQIELVEAYAKAQGLW--RDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAA-------- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 403 LKPEDATKSVTITNHGRTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGSGVVTKYLE 482
Cdd:COG1048 399 PVGEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 483 ASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPPLAVLYSII 562
Cdd:COG1048 479 RAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 563 GNVNVDI-NGVLAVTPDGKEIRLADIWPTRKEVAKFEEEFVKPQFFREVYANIELGSTEWQQLECPAVKLYPWDDASTYI 641
Cdd:COG1048 559 GTVDIDLtTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYI 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 642 KKVPFFDGMTSELPSQSDIVNAHVLLNLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGNDEIMARGT 721
Cdd:COG1048 639 RRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGT 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 722 FANIRLVNKLASKV-GPITLHVPSGEELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFER 800
Cdd:COG1048 719 FANIRIKNLLAPGTeGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFER 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 801 IHRSNLIGMGIIPFQYQAGQNADSLGLTGKEQFSI-GVPDDLKPGQLIDVNV--SNGSV--FQVICRFDTEVELTYYRNG 875
Cdd:COG1048 799 IHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIeGLDEGLAPGKTVTVTAtrADGSTeeFPVLHRIDTPVEVEYYRAG 878
|
890
....*....|..
gi 17568399 876 GILQYMIRKLIQ 887
Cdd:COG1048 879 GILQYVLRQLLA 890
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
18-887 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1327.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 18 KYFDLNGLNDARYNELPISIKYLLEAAVRHCDEFHVLKKDVETILDWKNSQRNQAEIPFKPARVILQDFTGVPAVVDLAA 97
Cdd:PLN00070 62 KYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKPARVLLQDFTGVPAVVDLAC 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 98 MRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKWGSKAFDNLLIVPPGSGIVHQ 177
Cdd:PLN00070 142 MRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 178 VNLEYLARTVFvGKDGVLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVIGYELVGTLSDTVTST 257
Cdd:PLN00070 222 VNLEYLGRVVF-NTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTAT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 258 DLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQTGRDTDYTQRVEQYLK 337
Cdd:PLN00070 301 DLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 338 SVGMFVNFTDDSYRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKGLTDKISFKAFGLKPEDATKSVTITNH 417
Cdd:PLN00070 381 ANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVAKFSFH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 418 GRTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGSGVVTKYLEASGLLPYLEKIGFNI 497
Cdd:PLN00070 461 GQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHI 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 498 AGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPPLAVLYSIIGNVNVDING-VLAVT 576
Cdd:PLN00070 541 VGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKePIGTG 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 577 PDGKEIRLADIWPTRKEVAKFEEEFVKPQFFREVYANIELGSTEWQQLECPAVKLYPWDDASTYIKKVPFFDGMTSELPS 656
Cdd:PLN00070 621 KDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPG 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 657 QSDIVNAHVLLNLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGNDEIMARGTFANIRLVNK-LASKV 735
Cdd:PLN00070 701 PHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKlLKGEV 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 736 GPITLHVPSGEELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQ 815
Cdd:PLN00070 781 GPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLC 860
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17568399 816 YQAGQNADSLGLTGKEQFSIGVPDDL---KPGQLIDVNVSNGSVFQVICRFDTEVELTYYRNGGILQYMIRKLIQ 887
Cdd:PLN00070 861 FKSGEDADTLGLTGHERYTIDLPSNIseiKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFDHGGILPYVIRNLIK 935
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-887 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1320.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 1 MAFNNLiRNLAIGDNVYKYFDL---NGLNDARYNELPISIKYLLEAAVRHCDEFHVLKKDVETILDWKNSQRNQAEIPFK 77
Cdd:PRK12881 4 NLHKTL-KEFDVGGKTYKFYSLpalGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIPFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 78 PARVILQDFTGVPAVVDLAAMRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKW 157
Cdd:PRK12881 83 PARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 158 GSKAFDNLLIVPPGSGIVHQVNLEYLARTVFV---GKDGVLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPI 234
Cdd:PRK12881 163 GMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTkedDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 235 SMVIPEVIGYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSR 314
Cdd:PRK12881 243 YMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 315 TIDYLTQTGRDTDYTQRVEQYLKSVGMFvnfTDDSYRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKGLTD 394
Cdd:PRK12881 323 TLDYLRLTGRTEAQIALVEAYAKAQGLW---GDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 395 KISFKAFGLKPEDATksvtitnhgrTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGS 474
Cdd:PRK12881 400 PVAENGFAKKAQTSN----------GVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 475 GVVTKYLEASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPP 554
Cdd:PRK12881 470 KVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPP 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 555 LAVLYSIIGNVNVDIN-GVLAVTPDGKEIRLADIWPTRKEVAKFEEEFVKPQFFREVYANIELGSTEWQQLECPAVKLYP 633
Cdd:PRK12881 550 LVVAYALAGTVRRDLMtEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYD 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 634 WDDASTYIKKVPFFDGMTSELPSQSDIVNAHVLLNLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGN 713
Cdd:PRK12881 630 WDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGN 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 714 DEIMARGTFANIRLVNKLASKV-GPITLHVPSGEELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKA 792
Cdd:PRK12881 710 HEVMMRGTFANVRIKNLMIPGKeGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKA 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 793 VIAESFERIHRSNLIGMGIIPFQYQAGQNADSLGLTGKEQFSI-GVPDDLKPGQLIDVNV--SNGSV--FQVICRFDTEV 867
Cdd:PRK12881 790 VIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIeGLPGEIKPRQDVTLVIhrADGSTerVPVLCRIDTPI 869
|
890 900
....*....|....*....|
gi 17568399 868 ELTYYRNGGILQYMIRKLIQ 887
Cdd:PRK12881 870 EVDYYKAGGILPYVLRQLLA 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
17-886 |
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: 1286.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 17 YKYFDLNGLNDA--RYNELPISIKYLLEAAVRHCDEFHVLKKDVETILDWKNSQRNQAEIPFKPARVILQDFTGVPAVVD 94
Cdd:TIGR01341 3 YYYYSLKALEESggKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 95 LAAMRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKWGSKAFDNLLIVPPGSGI 174
Cdd:TIGR01341 83 LAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGTGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 175 VHQVNLEYLARTVFVGK---DGVLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVIGYELVGTLS 251
Cdd:TIGR01341 163 IHQVNLEYLATVVFKAEvdgELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 252 DTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQTGRDTDYTQR 331
Cdd:TIGR01341 243 EGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 332 VEQYLKSVGMFVnftDDSYRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKGLTDKISFKAFGLKPEDATKS 411
Cdd:TIGR01341 323 VEKYARAQGLFY---DDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 412 VtitnHGRTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGSGVVTKYLEASGLLPYLE 491
Cdd:TIGR01341 400 V----NGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 492 KIGFNIAGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPPLAVLYSIIGNVNVDING 571
Cdd:TIGR01341 476 ELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 572 -VLAVTPDGKEIRLADIWPTRKEVAKFEEEFVKPQFFREVYANIELGSTEWQQLECPAVKLYPWDDASTYIKKVPFFDGM 650
Cdd:TIGR01341 556 ePIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEM 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 651 TSELPSQSDIVNAHVLLNLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGNDEIMARGTFANIRLVNK 730
Cdd:TIGR01341 636 KQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 731 LA-SKVGPITLHVPSGEELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGM 809
Cdd:TIGR01341 716 MVkGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGM 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 810 GIIPFQYQAGQNADSLGLTGKEQFSIGVPDDLKPGQLIDVNVSNG----SVFQVICRFDTEVELTYYRNGGILQYMIRKL 885
Cdd:TIGR01341 796 GVIPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSkgekITFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
.
gi 17568399 886 I 886
Cdd:TIGR01341 876 L 876
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
80-565 |
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: 809.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 80 RVILQDFTGVPAVVDLAAMRDAVQNMGADPAKINPVCPVDLVIDHSVQVDHYGNLEALAKNQSIEFERNRERFNFLKWGS 159
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 160 KAFDNLLIVPPGSGIVHQVNLEYLARTVFVGK---DGVLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISM 236
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEedgDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 237 VIPEVIGYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTI 316
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 317 dyltqtgrdtdytqrveqylksvgmfvnftddsyrptytttlKLDLGSVVPSVSGPKRPHDRVELaslaqdfskgltdki 396
Cdd:cd01586 241 ------------------------------------------ELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 397 sfkafglkpedatksvtitnhgrtaeltHGSVVIAAITSCTNTSNPSVMLAAGLVAKKAVELGLNVQPYVKTSLSPGSGV 476
Cdd:cd01586 264 ----------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 477 VTKYLEASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKAIEENNLVVAGVLSGNRNFEGRIHPHVRANYLASPPLA 556
Cdd:cd01586 316 VTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLV 395
|
....*....
gi 17568399 557 VLYSIIGNV 565
Cdd:cd01586 396 VAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
59-563 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 656.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 59 ETILDWKNSQRNQAEIPFKPARVILQDFTGVPAVVDLAAMRDAVQNMGADPAKINPVCPVDLVIDHSvqvdhygnLEALA 138
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 139 KNQSIEFERNRERFNFLKWGSKAFdNLLIVPPGSGIVHQVNLEYlartvfvgkdGVLYPD-SVVGTDSHTTMIDGSGVLG 217
Cdd:pfam00330 73 KNIEDEISRNKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEY----------GLALPGmTIVGTDSHTTTHGGLGALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 218 WGVGGIEAEAVMLGQPISMVIPEVIGYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIAN 297
Cdd:pfam00330 142 FGVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 298 MCPEYGATIGFFPVDSRTIDYLTQTGRdtDYTQRVEQYLKSVGMFVNFTDDSyrPTYTTTLKLDLGSVVPSVSGPKRPHD 377
Cdd:pfam00330 222 MAIEYGATAGLFPPDETTFEYLRATGR--PEAPKGEAYDKAVAWKTLASDPG--AEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 378 RVELASLAQD-FSKGLTDKISFKAfglkpedatksVTITNHGRTAELTHGSVVIAAITSCTNTSNPSVMLAAGLVaKKAV 456
Cdd:pfam00330 298 AVPLSELVPDpFADAVKRKAAERA-----------LEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 457 ELGLNVQPYVKTSLSPGSGVVTKYLEASGLLPYLEKIGFNIAGYGCMTCIGNSGPLdepvtkaiEENNlvvAGVLSGNRN 536
Cdd:pfam00330 366 EKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRL--------PPGE---RCVSSSNRN 434
|
490 500
....*....|....*....|....*..
gi 17568399 537 FEGRIHPHVRAnYLASPPLAVLYSIIG 563
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, ... |
668-835 |
2.30e-113 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 343.49 E-value: 2.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 668 NLGDSVTTDHISPAGSISKTSPAARFLAGRGVTPRDFNTYGARRGNDEIMARGTFANIRLVNKLASKVGPITLHVPS-GE 746
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPtGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 747 ELDIFDAAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQYQAGQNADSLG 826
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
....*....
gi 17568399 827 LTGKEQFSI 835
Cdd:cd01580 161 LTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
80-565 |
1.98e-96 |
|
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: 307.50 E-value: 1.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 80 RVILQDFTGVPAVVDLAAMRDAVqnmgadpaKINPVCPVDLVIDHSVQvdhygnlealaknqsIEFERNRERFNFLKWGS 159
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALG--------KVADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 160 KAFdNLLIVPPGSGIVHQVNLEYLArtvfvgkdgvLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIP 239
Cdd:cd01351 58 ALQ-GIAFYRPGVGIIHQIMVENLA----------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 240 EVIGYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYL 319
Cdd:cd01351 127 EVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 320 TQTGRdtdytqrvEQYLKSVGMFVNFTDDSYRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELaslaqdfskgltdkisfk 399
Cdd:cd01351 207 EATGR--------PLLKNLWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSV------------------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 400 afglkpedatksvtitnhgrtAELTHGSVVIAAITSCTNtSNPSVMLAAGLVAKKAVelglnVQPYVKTSLSPGSGVVTK 479
Cdd:cd01351 261 ---------------------SEVEGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 480 YLEASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKaieennlvvaGVLSGNRNFEGRIHPHVRANYLASPPLAVLY 559
Cdd:cd01351 314 TLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEV----------GVSSGNRNFPGRLGTYERHVYLASPELAAAT 383
|
....*.
gi 17568399 560 SIIGNV 565
Cdd:cd01351 384 AIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
73-885 |
1.86e-85 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 286.66 E-value: 1.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 73 EIPFKPARVILQDFTGVPAVVDLAAM-RDAVQnmgadpakinpvcpVDLvidhSVQ-VDHygNLEalaknQSIEfeRNRE 150
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgLDRVK--------------TEL----SVQyVDH--NLL-----QADF--ENAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 151 RFNFLKWGSKAFdNLLIVPPGSGIVHQVNLEYLArtvFVGKdgvlypdSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVML 230
Cdd:PRK07229 77 DHRFLQSVAAKY-GIYFSKPGNGICHQVHLERFA---FPGK-------TLLGSDSHTPTAGGLGMLAIGAGGLDVALAMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 231 GQPISMVIPEVIGYELVGTLSDTVTSTDLVLTItknLRDLGV---VGKFVEFFGTGVASLSIADRATIANMCPEYGATIG 307
Cdd:PRK07229 146 GGPYYLKMPKVVGVKLTGKLPPWVSAKDVILEL---LRRLTVkggVGKIIEYFGPGVATLSVPERATITNMGAELGATTS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 308 FFPVDSRTIDYLTQTGRDTDYTQrveqylksvgmfVNFTDDSYrptYTTTLKLDLGSVVPSVSGPKRPhDRVelaslaqd 387
Cdd:PRK07229 223 IFPSDERTREFLKAQGREDDWVE------------LLADPDAE---YDEVIEIDLSELEPLIAGPHSP-DNV-------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 388 fskgltdkisfkafglkpedatksVTITNHGRTAelthgsVVIAAITSCTNTSNPSVMLAAGLVAKKavelglNVQPYVK 467
Cdd:PRK07229 279 ------------------------VPVSEVAGIK------VDQVLIGSCTNSSYEDLMRAASILKGK------KVHPKVS 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 468 TSLSPGSGVVTKYLEASGLLPYLEKIGFNIAGYGCMTCIGNSgplDEPVTKAIEennlvvagVLSGNRNFEGRI-HP--H 544
Cdd:PRK07229 323 LVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMG---QAPATGNVS--------LRTFNRNFPGRSgTKdaQ 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 545 VranYLASPPLAVLYSIIGnvnvdingvlavtpdgkeiRLADiwPTrkEVAKFEEEFVKPQFFREVYANIELgstewqql 624
Cdd:PRK07229 392 V---YLASPETAAASALTG-------------------VITD--PR--TLALENGEYPKLEEPEGFAVDDAG-------- 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 625 ecpavKLYPWDDASTY-------IKKVPFFDgmtsELPsqsDIVNAHVLLNLGDSVTTDHISPAGsisktspaARFLAgr 697
Cdd:PRK07229 438 -----IIAPAEDGSDVevvrgpnIKPLPLLE----PLP---DLLEGKVLLKVGDNITTDHIMPAG--------AKWLP-- 495
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 698 gvtprdfntYgarRGNDEIMARGTFanIRLVNklaskvgpitlhvpsgeeldifDAAQKYKDAGiPAIILAGKEYGCGSS 777
Cdd:PRK07229 496 ---------Y---RSNIPNISEFVF--EGVDN----------------------TFPERAKEQG-GGIVVGGENYGQGSS 538
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 778 RDWAAKGP-FLqGVKAVIAESFERIHRSNLIGMGIIP--FQ----YQAGQNADSLGLTgkeqfsiGVPDDLKPGQLIDVN 850
Cdd:PRK07229 539 REHAALAPrYL-GVKAVLAKSFARIHKANLINFGILPltFAdpadYDKIEEGDVLEIE-------DLREFLPGGPLTVVN 610
|
810 820 830
....*....|....*....|....*....|....*
gi 17568399 851 VSNGSVFQVICRFdTEVELTYYRNGGILQYMIRKL 885
Cdd:PRK07229 611 VTKDEEIEVRHTL-SERQIEILLAGGALNLIKKKL 644
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
170-565 |
2.73e-49 |
|
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: 179.18 E-value: 2.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 170 PGSGIVHQVNLEYLARTvfvGKdgvlypdSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVIGYELVGT 249
Cdd:cd01585 66 PGNGICHQVHLERFAVP---GK-------TLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 250 LSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQTGRDTDyt 329
Cdd:cd01585 136 LPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDD-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 330 qrveqylksvgmFVNFTDDSyRPTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAqdfskgltdkisfkafGLKpedat 409
Cdd:cd01585 214 ------------WVELAADA-DAEYDEEIEIDLSELEPLIARPHSPDNVVPVREVA----------------GIK----- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 410 ksvtitnhgrtaelthgsVVIAAITSCTNTSNPSVMLAAGLVAkkavelGLNVQPYVKTSLSPGSGVVTKYLEASGLLPY 489
Cdd:cd01585 260 ------------------VDQVAIGSCTNSSYEDLMTVAAILK------GRRVHPHVSMVVAPGSKQVLEMLARNGALAD 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17568399 490 LEKIGFNIAGYGCMTCIGNSGpldEPVTKAIEennlvvagVLSGNRNFEGRIHPHVRANYLASPPLAVLYSIIGNV 565
Cdd:cd01585 316 LLAAGARILESACGPCIGMGQ---APPTGGVS--------VRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
690-819 |
2.44e-45 |
|
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: 159.07 E-value: 2.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 690 AARFLAGRGVTPRDFNTYGARRGNDEIMARGTFANIRLVNKLA-SKVGPITLHVPSGEELDIFDAAQKYKDAGIPAIILA 768
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17568399 769 GKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQYQAG 819
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
97-563 |
3.38e-44 |
|
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: 165.31 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 97 AMRDA------VQNMGADPAKinPVCPVDLVIDHSVQVdHYGNLEALAKNQSIeferNRERFNFLKWGSKAFdNLLIVPP 170
Cdd:cd01584 3 AMQDAtaqmalLQFMSSGLPK--VAVPSTIHCDHLIEA-QVGGEKDLKRAKDI----NKEVYDFLASAGAKY-GIGFWKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 171 GSGIVHQVNLEYLARTvfvgkdGVLypdsVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVIGYELVGTL 250
Cdd:cd01584 75 GSGIIHQIVLENYAFP------GLL----MIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 251 SDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQTGRD--TDY 328
Cdd:cd01584 145 SGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAeiADL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 329 TQrveqylksvgmfvNFTDDSYRPT----YTTTLKLDLGSVVPSVSGPKRPhdrvelaSLAQDFSKgltdkisFKafglk 404
Cdd:cd01584 225 AD-------------EFKDDLLVADegaeYDQLIEINLSELEPHINGPFTP-------DLATPVSK-------FK----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 405 pEDATKsvtitnHGRTAELTHGsvviaAITSCTNTSNPSVMLAAGlVAKKAVELGLNVQpyVKTSLSPGSGVVTKYLEAS 484
Cdd:cd01584 273 -EVAEK------NGWPLDLRVG-----LIGSCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTITPGSEQIRATIERD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 485 GLLPYLEKIGFNIAGYGCMTCIGNsgpLDEPVTKAIEENNLVVagvlSGNRNFEGR--IHPHVRAnYLASPPLAVLYSII 562
Cdd:cd01584 338 GLLQTFRDAGGIVLANACGPCIGQ---WDRKDIKKGEKNTIVT----SYNRNFTGRndANPATHA-FVASPEIVTAMAIA 409
|
.
gi 17568399 563 G 563
Cdd:cd01584 410 G 410
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
80-553 |
7.13e-44 |
|
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: 163.51 E-value: 7.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 80 RVILQDFTGVPAVVDL-AAMRDAVqnmgADPAKINpvcpvdLVIDHSVQVDHYgnleaLAKNQSIEFERNRERFnflkwG 158
Cdd:cd01583 1 LHLVHDVTSPQAFEGLrEAGREKV----WDPEKIV------AVFDHNVPTPDI-----KAAEQVKTLRKFAKEF-----G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 159 SKAFDnllivPPGSGIVHQVNLE-YLARtvfvgkdgvlyP-DSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISM 236
Cdd:cd01583 61 INFFD-----VGRQGICHVILPEkGLTL-----------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 237 VIPEVIGYELVGTLSDTVTSTDLVLTItknLRDLGV---VGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDS 313
Cdd:cd01583 125 RVPETMRVNVEGKLPPGVTAKDVILYI---IGKIGVdgaTYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 314 RTIDYLTQTGRdtdytqRVEQYLKSvgmfvnfTDDSyrpTYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAqdfskglt 393
Cdd:cd01583 202 TTFEYLKGRGK------AYWKELKS-------DEDA---EYDKVVEIDASELEPQVAWPHSPDNVVPVSEVE-------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 394 dkisfkafglkpedatkSVTITnhgrtaelthgsvvIAAITSCTNTSNPSVMLAAGLVAKKavelglNVQPYVKTSLSPG 473
Cdd:cd01583 258 -----------------GIKID--------------QVFIGSCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPA 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 474 SGVVTKYLEASGLLPYLEKIGFNIAGYGCMTCIG-NSGPLDEPVTkaieennlvvaGVLSGNRNFEGRI-HPHVRaNYLA 551
Cdd:cd01583 301 SQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAPGER-----------CVSTSNRNFKGRMgSPGAR-IYLA 368
|
..
gi 17568399 552 SP 553
Cdd:cd01583 369 SP 370
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
80-553 |
2.23e-43 |
|
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: 162.89 E-value: 2.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 80 RVILQDFTGVPAVVDLAAM-RDAVqnmgADPAKInpvcpVdLVIDHSVQVDHygnleALAKNQSIEFERNRERFnflkwG 158
Cdd:COG0065 30 LHLVHDVTSPQAFEGLREAgGRKV----WDPDRI-----V-AVFDHNVPTKD-----PKSAEQVKTLREFAKEF-----G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 159 SKAFDnllivpPGS-GIVHQVNLEylartvfvgkDGVLYP-DSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISM 236
Cdd:COG0065 90 ITFFD------VGDpGICHVVLPE----------QGLVLPgMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 237 VIPEVIGYELVGTLSDTVTSTDLVLTItknLRDLGV---VGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDS 313
Cdd:COG0065 154 KVPETMRIEVTGKLPPGVTAKDLILAI---IGKIGAdgaTGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 314 RTIDYLTQTGRdtdytqRVEQYLKSvgmfvnftDDSYRptYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAqdfskglt 393
Cdd:COG0065 231 TTFEYLKGRPF------APWRTLKS--------DEDAV--YDKEVEIDASDLEPQVAWPHSPDNVVPVSELE-------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 394 dkisfkafGLKpedatksvtitnhgrtaelthgsVVIAAITSCTNtSNPSVMLAAGLVAKkavelGLNVQPYVKTSLSPG 473
Cdd:COG0065 287 --------GIK-----------------------IDQVFIGSCTN-GRIEDLRAAAEILK-----GRKVAPGVRAIVVPG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 474 SGVVTKYLEASGLLPYLEKIGFNIAGYGCMTCIG-NSGPLdepvtkaiEENNLVVAgvlSGNRNFEGRI-HPHVRAnYLA 551
Cdd:COG0065 330 SQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVL--------APGERCAS---TSNRNFEGRMgSPGSRT-YLA 397
|
..
gi 17568399 552 SP 553
Cdd:COG0065 398 SP 399
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
89-556 |
1.45e-29 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 122.21 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 89 VPAVVDLAAMRD-----AVQ---NMGA----DPAKINpvcpvdLVIDHSVQVDhygNLEAlAKNQSI--EFERNRERFNF 154
Cdd:PRK00402 24 VEAKVDLVMAHDitgplAIKefeKIGGdkvfDPSKIV------IVFDHFVPAK---DIKS-AEQQKIlrEFAKEQGIPNF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 155 lkwgskaFDNllivppGSGIVHQVNLEylartvfvgKDGVLYPDSVVGTDSHTTMIDGSGVLGWGVGGIEAEAVM-LGQp 233
Cdd:PRK00402 94 -------FDV------GEGICHQVLPE---------KGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMaTGK- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 234 ISMVIPEVIGYELVGTLSDTVTSTDLVLTItknLRDLGVVG---KFVEFFGTGVASLSIADRATIANMCPEYGATIGFFP 310
Cdd:PRK00402 151 TWFKVPETIKVVLEGKLPPGVTAKDVILHI---IGDIGVDGatyKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 311 VDSRTIDYLTQ-TGRDtdytqrveqylksvgmFVNFTDDSyRPTYTTTLKLDLGSVVPSVSGPKRPhdrvelaslaqdfs 389
Cdd:PRK00402 228 PDEKTLEYLKErAGRD----------------YKPWKSDE-DAEYEEVYEIDLSKLEPQVAAPHLP-------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 390 kgltdkisfkafglkpeDATKSVTitnhgrtaELTHGSVVIAAITSCTNtSNPSVMLAAGLVAKkavelGLNVQPYVKTS 469
Cdd:PRK00402 277 -----------------DNVKPVS--------EVEGTKVDQVFIGSCTN-GRLEDLRIAAEILK-----GRKVAPGVRLI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 470 LSPGSGVVtkYLEA--SGLLPYLEKIGFNIAGYGCMTCIGNSGpldepvtkaieennlvvaGVL--------SGNRNFEG 539
Cdd:PRK00402 326 VIPASQKI--YLQAlkEGLIEIFVDAGAVVSTPTCGPCLGGHM------------------GVLapgevclsTTNRNFKG 385
|
490 500
....*....|....*....|
gi 17568399 540 RI-HP--HVranYLASPPLA 556
Cdd:PRK00402 386 RMgSPesEV---YLASPAVA 402
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
101-565 |
2.08e-28 |
|
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: 117.72 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 101 AVQNMGADPAKINPVCPVDLVIDHSVQ------VDHYGNLEALAKNQSIEFernrerfnflkwgskafdnlliVPPGSGI 174
Cdd:cd01582 12 ALKFMSIGATKIHNPDQIVMTLDHDVQnkseknLKKYKNIESFAKKHGIDF----------------------YPAGRGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 175 VHQVNLEylartvfvgkDGVLYPDSV-VGTDSHTTMIDGSGVLGWGVGGIEAEAVMLGQPISMVIPEVIGYELVGTLSDT 253
Cdd:cd01582 70 GHQIMIE----------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 254 VTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRtidyltqtgrdtdytqrve 333
Cdd:cd01582 140 VTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 334 qylksvgmfvnftddsyrptyttTLKLDLGSVVPSVSGPkrphDRVELASLAQDFSKgltdkisfkafglkpedatKSVT 413
Cdd:cd01582 201 -----------------------HLILDLSTLSPYVSGP----NSVKVSTPLKELEA-------------------QNIK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 414 ITNhgrtaelthgsvviAAITSCTNTSNPSVMLAAGLVAKKAVELGLN-VQPYVKTSLSPGSGVVTKYLEASGLLPYLEK 492
Cdd:cd01582 235 INK--------------AYLVSCTNSRASDIAAAADVVKGKKEKNGKIpVAPGVEFYVAAASSEVQAAAEKNGDWQTLLE 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17568399 493 IGFNIAGYGCMTCIGNSGPLDEPVTkaieennlvvAGVLSGNRNFEGRIHPHVRANYLASPPLAVLYSIIGNV 565
Cdd:cd01582 301 AGATPLPAGCGPCIGLGQGLLEPGE----------VGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
80-556 |
3.53e-28 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 119.24 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 80 RVILQDFTGVPAVVDLAAMRDAVQNMGADPAkinpvcpvdlVIDHSVQVDHYGNLE---ALAKNQSIEFERNRERFnflk 156
Cdd:PRK12466 30 RHLLNEYTSPQAFSGLRARGRTVRRPDLTLA----------VVDHVVPTRPGRDRGitdPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 157 wGSKAFDnllIVPPGSGIVHQVNLEYlartvfvgkdGVLYPDSVVGT-DSHTTMIDGSGVLGWGVGGIEAEAVMLGQPIS 235
Cdd:PRK12466 96 -GIRLFD---VDDPRQGIVHVVAPEL----------GLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 236 MVIPEVIGYELVGTLSDTVTSTDLVLTITKNLRDLGVVGKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRT 315
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 316 IDYLtqtgRDTDYTQRVEQYLKSVGMFVNF-TDDSYRptYTTTLKLDLGSVVPSVSGPKRP------HDRVELASLAQDF 388
Cdd:PRK12466 242 FDYL----RGRPRAPKGALWDAALAYWRTLrSDADAV--FDREVEIDAADIAPQVTWGTSPdqavpiTGRVPDPAAEADP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 389 SKGLTDKISFKAFGLKPEDATKSVTITNhgrtaelthgsvviAAITSCTNTSNPSVMLAAGLVAkkavelGLNVQPYVKT 468
Cdd:PRK12466 316 ARRAAMERALDYMGLTPGTPLAGIPIDR--------------VFIGSCTNGRIEDLRAAAAVLR------GRKVAPGVRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 469 SLSPGSGVVTKYLEASGLLPYLEKIGFNIAGYGCMTCIGNSGPLDEPVTKAIEennlvvagvlSGNRNFEGRIHPHVRAn 548
Cdd:PRK12466 376 MVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCAS----------TTNRNFEGRQGPGART- 444
|
....*...
gi 17568399 549 YLASPPLA 556
Cdd:PRK12466 445 HLMSPAMV 452
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
760-825 |
1.86e-19 |
|
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: 83.67 E-value: 1.86e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17568399 760 AGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQYQAGQNADSL 825
Cdd:cd00404 13 PAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKL 78
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
669-816 |
1.71e-18 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 82.10 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 669 LGDSVTTDHISPAGsisktspaARFLAGRGVTPRdfntygarrgndeiMARGTFanirlvnklaSKVGPitlhvpsgeel 748
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLRSNIPA--------------ISEFVF----------HRVDP----------- 38
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568399 749 difDAAQKYKDAGiPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQY 816
Cdd:cd01579 39 ---TFAERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
674-836 |
1.31e-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: 69.03 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 674 TTDHISPAGsisktsPAARFlagrgvtprdfntygarRGN-DEIMARGTFANIRLVNKLASKVGpitlHVPSGEELDIFD 752
Cdd:cd01578 7 TTDHISAAG------PWLKY-----------------RGHlDNISNNLLIGAINAENGKANSVK----NQVTGEYGPVPD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 753 AAQKYKDAGIPAIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQ------YQAGQNADSLG 826
Cdd:cd01578 60 TARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTfadpadYDKIHPDDKVD 139
|
170
....*....|
gi 17568399 827 LTGKEQFSIG 836
Cdd:cd01578 140 ILGLTDFAPG 149
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
765-880 |
5.13e-13 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 67.91 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 765 IILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQyqagqnadslgltgkeqfSIGVPDDLKPG 844
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFE------------------SEEVVDALEDG 113
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17568399 845 QLIDVNVSNGSV------FQVicRFDTEVELTYYRNGGILQY 880
Cdd:PRK14023 114 DEVELDLETGVLtrggetFQL--RPPPEFLLEALKEGSILEY 153
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
663-815 |
1.49e-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: 67.12 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 663 AHVLLnlGDSVTTDHISPAgsisktspaaRFLagRGVTPrdfntygarrgndEIMARGTFANIRLVNKlaskvgpitlhv 742
Cdd:COG0066 10 AVPLD--GDNIDTDQIIPA----------RFL--KTIDR-------------EGLGKHLFEDWRYDRS------------ 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568399 743 psgEELDIFDAAQKYKDAGIpaiILAGKEYGCGSSRD---WAakgpfLQ--GVKAVIAESFERIHRSNLIGMGIIPFQ 815
Cdd:COG0066 51 ---PDPDFVLNQPRYQGADI---LVAGRNFGCGSSREhapWA-----LKdyGFRAVIAPSFADIFYRNAINNGLLPIE 117
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
759-814 |
1.66e-12 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 64.15 E-value: 1.66e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17568399 759 DAGIPA-----IILAGKEYGCGSSR---DWAAKGpflQGVKAVIAESFERIHRSNLIGMGIIPF 814
Cdd:cd01577 9 DQIIPArflgdIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
765-883 |
6.25e-12 |
|
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: 64.37 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 765 IILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMGIIPFQyqagqnADSLGLTGKEQFSIgvpdDLKPG 844
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEGIKDGDEVTV----DLETG 119
|
90 100 110
....*....|....*....|....*....|....*....
gi 17568399 845 QLIdvnVSNGSVFQviCRFDTEVELTYYRNGGILQYMIR 883
Cdd:TIGR02087 120 EIR---VNGNEEYK--GEPLPDFLLEILREGGLLEYLKK 153
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
765-885 |
8.02e-11 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 61.38 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 765 IILAGKEYGCGSSRD---WAAKGpflQGVKAVIAESFERIHRSNLIGMGIIPFQYQagqnadslgltgkeqfsiGVPDDL 841
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGLPVLECD------------------EAVDKI 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17568399 842 KPGQLIDVNVSNGsvfqVICRFDTEVELTY----------YRNGGILQYMIRKL 885
Cdd:PRK00439 110 EDGDEVEVDLETG----VITNLTTGEEYKFkpipefmleiLKAGGLIEYLKKKG 159
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
168-815 |
9.96e-10 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 62.33 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 168 VPPGSGIVHQVNLEYLARTvfvGKdgvlypdSVVGTDSHTTMidGS-GVLGWGVGGIEAEAVMLGQPISMVIPEVIGYEL 246
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG---GK-------MILGSDSHTRY--GAlGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 247 VGTLSDTVTSTDLVLTITKNLRDLGVV-GKFVEFFGTGVASLSIADRATIANMCPEYGATIGFFPVDSRTIDYLTQTGRD 325
Cdd:PRK11413 191 TGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 326 TDYTQrveqylksvgmfVNFTDDSYrptYTTTLKLDLGSVVPSVSGPKRPHDRVELASLAQDFSKGLtDKISFKAfgLKP 405
Cdd:PRK11413 271 QDYCE------------LNPQPMAY---YDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDIL-REVEIES--ERV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 406 EDATKSVTITNHGRTAELTHGSVVIAAitsCTNTSNPSVMLAAGLVAKKAV---ELGLNVQPyvktSLSP------GSGV 476
Cdd:PRK11413 333 AHGKAKLSLLDKIENGRLKVQQGIIAG---CSGGNYENVIAAANALRGQSCgndTFSLSVYP----SSQPvfmdlaKKGV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 477 VTKYLEASGLLpyleKIGFniagygCMTCIGnSGplDEPVTKAIEennlvvagVLSGNRNFEGRIHPHVRANYLASPPLA 556
Cdd:PRK11413 406 VADLMGAGAII----RTAF------CGPCFG-AG--DTPANNGLS--------IRHTTRNFPNREGSKPANGQMSAVALM 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 557 VLYSIIGNVnvdINGVLaVTPdGKEIrlaDIWPTrkeVAKFeeEFVKPQFFREVYANIELGSTEWQQLECPAVKLYPwdd 636
Cdd:PRK11413 465 DARSIAATA---ANGGY-LTS-ATEL---DCWDN---VPEY--AFDVTPYKNRVYQGFGKGATQQPLIYGPNIKDWP--- 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 637 astyikkvpffdgmtsELPSQSDivnaHVLLNLG----DSV-TTDHISPAGSIS--KTSPA--ARFLAGRgvtpRDFNTY 707
Cdd:PRK11413 529 ----------------EMGALTD----NILLKVCskilDPVtTTDELIPSGETSsyRSNPLglAEFTLSR----RDPGYV 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568399 708 GARRGNDEIMARGTFANIRLVNKLASKVGPItlhvPSGEELDIfdaaqkyKDAGIPAIILAGKEyGCGSSRDWAAKGPFL 787
Cdd:PRK11413 585 GRSKAVAELENQRLAGNVSELTEVFARIKQI----AGQEHIDP-------LQTEIGSMVYAVKP-GDGSAREQAASCQRV 652
|
650 660 670
....*....|....*....|....*....|
gi 17568399 788 QGVKAVIAESF--ERiHRSNLIGMGIIPFQ 815
Cdd:PRK11413 653 LGGLANIAEEYatKR-YRSNVINWGMLPFQ 681
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
757-813 |
5.45e-08 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 53.98 E-value: 5.45e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17568399 757 YKDAgipAIILAGKEYGCGSSRD---WAakgpfLQ--GVKAVIAESFERIHRSNLIGMGIIP 813
Cdd:PRK01641 65 YQGA---SILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
764-810 |
3.60e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.39 E-value: 3.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 17568399 764 AIILAGKEYGCGSSRDWAAKGPFLQGVKAVIAESFERIHRSNLIGMG 810
Cdd:PLN00072 131 SIIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATG 177
|
|
| |
