|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00070 |
PLN00070 |
aconitate hydratase |
59-990 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 2100.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 59 WSHSFHSKPSPFRFTSQIRAVSPVLDRLQRTFSSMASEHPFKGIFTTLPKPGGGEFGKFYSLPALNDPRVDKLPYSIRIL 138
Cdd:PLN00070 5 SSSLSSSSSSPFSLRAQIRAASPVIERFQRKFASMASENPFKGILTSLPKPGGGEFGKYYSLPALNDPRIDKLPYSIRIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 139 LESAIRNCDNFQVTKEDVEKIIDWEKTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDL 218
Cdd:PLN00070 85 LESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 219 VIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTKGLLYPDSVV 298
Cdd:PLN00070 165 VIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 299 GTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYG 378
Cdd:PLN00070 245 GTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 379 NGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANNMFVDYNEPQQDRVYSSYLELN 458
Cdd:PLN00070 325 EGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 459 LDDVEPCISGPKRPHDRVTLKEMKADWHSCLDSKVGFKGFAIPKEAQEKVVNFSFDGQPAELKHGSVVIAAITSCTNTSN 538
Cdd:PLN00070 405 LEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSN 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 539 PSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAIT 618
Cdd:PLN00070 485 PSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAIT 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 619 ENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNIDFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQS 698
Cdd:PLN00070 565 ENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQS 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 699 SVLPDMFRATYESITKGNPMWNKLSVPENTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISP 778
Cdd:PLN00070 645 SVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISP 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 779 AGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKS 858
Cdd:PLN00070 725 AGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKS 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 859 SGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIHLPT 938
Cdd:PLN00070 805 EGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPS 884
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 30678219 939 DISEIRPGQDVTVTTDNGKSFTCTVRFDTEVELAYFNHGGILPYVIRNLSKQ 990
Cdd:PLN00070 885 NISEIKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFDHGGILPYVIRNLIKQ 936
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
87-990 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1707.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 87 QRTFSSMASEHPFKGIFTTLPkpGGGEFgKFYSLPALNDPRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTS 166
Cdd:PTZ00092 4 QQLRMSSSRPNPFEKVLKTLK--DGGSY-KYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 167 PKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRN 246
Cdd:PTZ00092 81 KKQIEIPFKPARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 247 KERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTKGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATM 326
Cdd:PTZ00092 161 LERFEFLKWGSKAFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 327 LGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFF 406
Cdd:PTZ00092 241 LGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 407 PVDHVTLQYLKLTGRSDETVAMIEAYLRANNMFVDYNEpqqDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWH 486
Cdd:PTZ00092 321 PIDEKTLDYLKQTGRSEEKVELIEKYLKANGLFRTYAE---QIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 487 SCLDSKVGFKGFAIPKEAQEKVVNFSFDGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTS 566
Cdd:PTZ00092 398 ACLSAPVGFKGFGIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 567 LAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANY 646
Cdd:PTZ00092 478 LSPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANY 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 647 LASPPLVVAYALAGTVNIDFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPE 726
Cdd:PTZ00092 558 LASPPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 727 NTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYG 806
Cdd:PTZ00092 638 GKLYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 807 SRRGNDEIMARGTFANIRIVNKLMnGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPML 886
Cdd:PTZ00092 718 ARRGNDEVMVRGTFANIRLINKLC-GKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 887 QGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIHLPTDisEIRPGQDVTVTTDNGKSFTCTVRFD 966
Cdd:PTZ00092 797 QGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSG--ELKPGQDVTVKTDTGKTFDTILRID 874
|
890 900
....*....|....*....|....
gi 30678219 967 TEVELAYFNHGGILPYVIRNLSKQ 990
Cdd:PTZ00092 875 TEVEVEYFKHGGILQYVLRKLVKG 898
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
93-990 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1593.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 93 MASEHPFKGIfTTLPKPGGGefGKFYSLPALND---PRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTSPKQ 169
Cdd:PRK09277 1 MSSTDSFKAR-KTLEVGGKS--YDYYSLRALEAkglGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 170 VEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKER 249
Cdd:PRK09277 78 REIPFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 250 FAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTKG---LLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATM 326
Cdd:PRK09277 158 YQFLKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTREDgelVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 327 LGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFF 406
Cdd:PRK09277 238 LGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 407 PVDHVTLQYLKLTGRSDETVAMIEAYLRANNMFVDynePQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWH 486
Cdd:PRK09277 318 PIDEETLDYLRLTGRDEEQVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 487 SCLDskVGFKGFAIPKEAQekvvnfsfdGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTS 566
Cdd:PRK09277 395 KSAE--LGVQGFGLDEAEE---------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 567 LAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANY 646
Cdd:PRK09277 464 LAPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANY 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 647 LASPPLVVAYALAGTVNIDFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPE 726
Cdd:PRK09277 544 LASPPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPE 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 727 NTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYG 806
Cdd:PRK09277 624 GPLYDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYG 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 807 SRRGNDEIMARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPML 886
Cdd:PRK09277 704 SRRGNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 887 QGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIhlpTDISEIRPGQDVTV--TTDNG--KSFTCT 962
Cdd:PRK09277 784 LGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDI---EGLEDLKPGATVTVviTRADGevVEFPVL 860
|
890 900
....*....|....*....|....*...
gi 30678219 963 VRFDTEVELAYFNHGGILPYVIRNLSKQ 990
Cdd:PRK09277 861 CRIDTAVEVDYYRNGGILQYVLRDLLAS 888
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
111-990 |
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: 1580.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 111 GGEFGKFYSLPALND--PRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTSPKQVEIPFKPARVLLQDFTGVP 188
Cdd:COG1048 14 GGKPYTYYSLPALEEagGDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVLMQDFTGVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 189 AVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPP 268
Cdd:COG1048 94 AVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAFDNFRVVPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 269 GSGIVHQVNLEYLGRVVF----NTKGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLA 344
Cdd:COG1048 174 GTGIVHQVNLEYLAFVVWtreeDGETVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 345 GKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDE 424
Cdd:COG1048 254 GKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 425 TVAMIEAYLRANNMFvdYNEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWHSCLDSKVGfkgfaipkEA 504
Cdd:COG1048 334 QIELVEAYAKAQGLW--RDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG--------EE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 505 QEKVVNFSFDGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGVVTKYLLKSGLQ 584
Cdd:COG1048 404 LDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 585 EYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNI 664
Cdd:COG1048 484 PYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDI 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 665 DFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPENTLYSWDPNSTYIHEPPY 744
Cdd:COG1048 564 DLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPF 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 745 FKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIR 824
Cdd:COG1048 644 FEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIR 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 825 IVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSN 904
Cdd:COG1048 724 IKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSN 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 905 LVGMGIIPLCFKSGEDADTLGLTGHERYTIhlpTDISE-IRPGQDVTV--TTDNG--KSFTCTVRFDTEVELAYFNHGGI 979
Cdd:COG1048 804 LVGMGVLPLQFPEGESAESLGLTGDETFDI---EGLDEgLAPGKTVTVtaTRADGstEEFPVLHRIDTPVEVEYYRAGGI 880
|
890
....*....|.
gi 30678219 980 LPYVIRNLSKQ 990
Cdd:COG1048 881 LQYVLRQLLAA 891
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
113-987 |
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: 1560.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 113 EFGKFYSLPALND--PRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTSPKQVEIPFKPARVLLQDFTGVPAV 190
Cdd:TIGR01341 1 KTYYYYSLKALEEsgGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 191 VDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGS 270
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 271 GIVHQVNLEYLGRVVFNT----KGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGK 346
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAevdgELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 347 MRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETV 426
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 427 AMIEAYLRANNMFVDYNEPQQdrvYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWHSCLDSKVGFKGFAIPKEAQE 506
Cdd:TIGR01341 321 ELVEKYARAQGLFYDDSEEPR---YTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 507 KVVNfsfdGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGVVTKYLLKSGLQEY 586
Cdd:TIGR01341 398 KKVN----GQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 587 LNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNIDF 666
Cdd:TIGR01341 474 LEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 667 ETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPENTLYSWDPNSTYIHEPPYFK 746
Cdd:TIGR01341 554 YTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 747 DMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIV 826
Cdd:TIGR01341 634 EMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIK 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 827 NKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLV 906
Cdd:TIGR01341 714 NLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLV 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 907 GMGIIPLCFKSGEDADTLGLTGHEryTIHLPtDISEIRPGQDVTVTTDNGK----SFTCTVRFDTEVELAYFNHGGILPY 982
Cdd:TIGR01341 794 GMGVIPLQFPQGEDAETLGLTGDE--TIDID-GIKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHGGILQY 870
|
....*
gi 30678219 983 VIRNL 987
Cdd:TIGR01341 871 VLRKF 875
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
102-987 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1385.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 102 IFTTLPK-PGGGEFGKFYSLPAL---NDPRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTSPKQVEIPFKPA 177
Cdd:PRK12881 5 LHKTLKEfDVGGKTYKFYSLPALgkeLGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIPFVPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 178 RVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGS 257
Cdd:PRK12881 85 RVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 258 TAFQNMLVVPPGSGIVHQVNLEYLGRVVF----NTKGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSM 333
Cdd:PRK12881 165 QAFDNFRVVPPGTGIMHQVNLEYLARVVHtkedDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 334 VLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTL 413
Cdd:PRK12881 245 LIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 414 QYLKLTGRSDETVAMIEAYLRANNMFVDynePQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWHSCLDSKV 493
Cdd:PRK12881 325 DYLRLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 494 GFKGFAIPKEaqekvvnfsfDGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGV 573
Cdd:PRK12881 402 AENGFAKKAQ----------TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 574 VTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLV 653
Cdd:PRK12881 472 VTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 654 VAYALAGTVNIDFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPENTLYSWD 733
Cdd:PRK12881 552 VAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 734 PNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDE 813
Cdd:PRK12881 632 PKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 814 IMARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVI 893
Cdd:PRK12881 712 VMMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVI 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 894 AKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIHLPTDisEIRPGQDVTVTT--DNG--KSFTCTVRFDTEV 969
Cdd:PRK12881 792 AESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPG--EIKPRQDVTLVIhrADGstERVPVLCRIDTPI 869
|
890
....*....|....*...
gi 30678219 970 ELAYFNHGGILPYVIRNL 987
Cdd:PRK12881 870 EVDYYKAGGILPYVLRQL 887
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
178-662 |
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: 800.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 178 RVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGS 257
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 258 TAFQNMLVVPPGSGIVHQVNLEYLGRVVF----NTKGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSM 333
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 334 VLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDhvtl 413
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 414 qylkltgrsdetvamieaylrannmfvdynepqqdrvySSYLELNLDDVEPCISGPKRPHDRVTLkemkadwhscldskv 493
Cdd:cd01586 237 --------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 494 gfkgfaipkeaqekvvnfsfdgqpaelkHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGV 573
Cdd:cd01586 264 ----------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 574 VTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLV 653
Cdd:cd01586 316 VTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLV 395
|
....*....
gi 30678219 654 VAYALAGTV 662
Cdd:cd01586 396 VAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
157-660 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 659.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 157 EKIIDWEKTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSvqvdvarsENAVQ 236
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 237 ANMELEFQRNKERFAFLKWGSTAFqNMLVVPPGSGIVHQVNLEYlgrvvfntkGLLYPD-SVVGTDSHTTMIDGLGVAGW 315
Cdd:pfam00330 73 KNIEDEISRNKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEY---------GLALPGmTIVGTDSHTTTHGGLGALAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 316 GVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANM 395
Cdd:pfam00330 143 GVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 396 SPEYGATMGFFPVDHVTLQYLKLTGRSDETVamIEAYLRANNMFVDYNEPqqDRVYSSYLELNLDDVEPCISGPKRPHDR 475
Cdd:pfam00330 223 AIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDP--GAEYDKVVEIDLSTIEPMVTGPTRPQDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 476 VTLKEMKADwhscldskvGFKGfAIPKEAQEKVVNFSFDGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVaKKACDL 555
Cdd:pfam00330 299 VPLSELVPD---------PFAD-AVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 556 GLQVKPWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEinesvgaaITENDivaAAVLSGNRNFE 635
Cdd:pfam00330 368 GLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDR--------LPPGE---RCVSSSNRNFE 436
|
490 500
....*....|....*....|....*
gi 30678219 636 GRVHPLTRAnYLASPPLVVAYALAG 660
Cdd:pfam00330 437 GRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
766-934 |
9.40e-109 |
|
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: 333.86 E-value: 9.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 766 NFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLMNGEVGPKTVHIPSGE 845
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 846 KLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLG 925
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
....*....
gi 30678219 926 LTGHERYTI 934
Cdd:cd01580 161 LTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
178-662 |
9.68e-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: 307.89 E-value: 9.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 178 RVLLQDFTGVPAVVDLACMRDAmnklgsdsNKINPLVPVDLVIDHSVQvdvarsenavqanmeLEFQRNKERFAFLKWgS 257
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAAL--------GKVADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 258 TAFQNMLVVPPGSGIVHQVNLEYLgrvvfntkgLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPG 337
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENL---------ALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 338 VVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLK 417
Cdd:cd01351 128 VVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 418 LTGRSDETVAMIEaylrannmFVDYNEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLkemkadwhscldskvgfkg 497
Cdd:cd01351 208 ATGRPLLKNLWLA--------FPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSV------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 498 faipkeaqekvvnfsfdgqpAELKHGSVVIAAITSCTNtSNPSVMLGAGLVAKKAcdlglQVKPWIKTSLAPGSGVVTKY 577
Cdd:cd01351 261 --------------------SEVEGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLIVTPGSRMVYAT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 578 LLKSGLQEYLNEQGFNIVGYGCTTCIGNsgeinesvGAAITENDIVaaAVLSGNRNFEGRVHPLTRANYLASPPLVVAYA 657
Cdd:cd01351 315 LSREGYYEILVDSGARILPPGCGPCMGN--------GARLVADGEV--GVSSGNRNFPGRLGTYERHVYLASPELAAATA 384
|
....*
gi 30678219 658 LAGTV 662
Cdd:cd01351 385 IAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
156-983 |
4.90e-93 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 309.00 E-value: 4.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 156 VEKIID---WEKTSPKQVEIPFKPARVLLQDFTGVPAVVDLacmrDAMNKlgsdsnkinPLVPVDLvidhSVQ-VDvars 231
Cdd:PRK07229 6 TEKILYahlVEGELEPGEEIAIRIDQTLTQDATGTMAYLQF----EAMGL---------DRVKTEL----SVQyVD---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 232 ENAVQANmelefQRNKERFAFLK--------WGStafqnmlvvPPGSGIVHQVNLEYLGRvvfntkgllyP-DSVVGTDS 302
Cdd:PRK07229 65 HNLLQAD-----FENADDHRFLQsvaakygiYFS---------KPGNGICHQVHLERFAF----------PgKTLLGSDS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 303 HTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTvtqMLRKHGV---VGKFVEFYGN 379
Cdd:PRK07229 121 HTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILE---LLRRLTVkggVGKIIEYFGP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 380 GMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMieaylrannmfvdynEPQQDRVYSSYLELNL 459
Cdd:PRK07229 198 GVATLSVPERATITNMGAELGATTSIFPSDERTREFLKAQGREDDWVEL---------------LADPDAEYDEVIEIDL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 460 DDVEPCISGPKRPhDRVT----LKEMKADWhscldskvgfkgfaipkeaqekvvnfsfdgqpaelkhgsvviAAITSCTN 535
Cdd:PRK07229 263 SELEPLIAGPHSP-DNVVpvseVAGIKVDQ------------------------------------------VLIGSCTN 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 536 TSNPSVMLGAGLVAKKacdlglQVKPwiKTSL--APGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNsgeinesv 613
Cdd:PRK07229 300 SSYEDLMRAASILKGK------KVHP--KVSLviNPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM-------- 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 614 GAAITENDIvaaAVLSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAGTVnidfeTEPIG-KGKNGKDVFLRDiwPTTEE 691
Cdd:PRK07229 364 GQAPATGNV---SLRTFNRNFPGRSgTKDAQV-YLASPETAAASALTGVI-----TDPRTlALENGEYPKLEE--PEGFA 432
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 692 IAEvvqSSVLPDMFRATYESITKGnpmwnklsvpentlyswdPNstyIHEPPyfkdmTMDPPGphNVKDAYCLLNFGDSI 771
Cdd:PRK07229 433 VDD---AGIIAPAEDGSDVEVVRG------------------PN---IKPLP-----LLEPLP--DLLEGKVLLKVGDNI 481
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 772 TTDHISPAGniqkdspaAKFLMergvdrkdfnsYgsrRGNDEIMARGTFanIRIVNklmngevgpktvhipsgeklsvfD 851
Cdd:PRK07229 482 TTDHIMPAG--------AKWLP-----------Y---RSNIPNISEFVF--EGVDN-----------------------T 514
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 852 AAMRYKSSGeDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGltghER 931
Cdd:PRK07229 515 FPERAKEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIE----EG 589
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 30678219 932 YTIHLPtDISEIRPGQDVTVT-TDNGKSFTCTVRFdTEVELAYFNHGGILPYV 983
Cdd:PRK07229 590 DVLEIE-DLREFLPGGPLTVVnVTKDEEIEVRHTL-SERQIEILLAGGALNLI 640
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
268-662 |
8.21e-54 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 192.66 E-value: 8.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 268 PGSGIVHQVNLEYLGRvvfntkgllyP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGK 346
Cdd:cd01585 66 PGNGICHQVHLERFAV----------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 347 MRNGVTATDLVLtvtQMLRKHGV---VGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSD 423
Cdd:cd01585 136 LPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRED 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 424 ETVAMieaylrannmfvdynEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMkadwhscldskvgfkgfAIPKE 503
Cdd:cd01585 213 DWVEL---------------AADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREV-----------------AGIKV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 504 AQekvvnfsfdgqpaelkhgsvviAAITSCTNTSNPSVMLGAGLVAkkacdlGLQVKPWIKTSLAPGSGVVTKYLLKSGL 583
Cdd:cd01585 261 DQ----------------------VAIGSCTNSSYEDLMTVAAILK------GRRVHPHVSMVVAPGSKQVLEMLARNGA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30678219 584 QEYLNEQGFNIVGYGCTTCIGnsgeinesVGAAITENdivAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTV 662
Cdd:cd01585 313 LADLLAAGARILESACGPCIG--------MGQAPPTG---GVSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
178-661 |
9.61e-54 |
|
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: 193.43 E-value: 9.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 178 RVLLQDFTGVPAVvdLACMRDAMNKlgsdsnkinPLVPVDLVIDHSVQVDVARSENAVQANMElefqrNKERFAFLKwGS 257
Cdd:cd01584 1 RVAMQDATAQMAL--LQFMSSGLPK---------VAVPSTIHCDHLIEAQVGGEKDLKRAKDI-----NKEVYDFLA-SA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 258 TAFQNMLVVPPGSGIVHQVNLEYlgrvvFNTKGLLypdsVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPG 337
Cdd:cd01584 64 GAKYGIGFWKPGSGIIHQIVLEN-----YAFPGLL----MIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 338 VVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLK 417
Cdd:cd01584 135 VIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 418 LTGRSDetvamIEAYlrANNMFVDYNEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKadwhscldskvgfkg 497
Cdd:cd01584 215 ATGRAE-----IADL--ADEFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFK--------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 498 faipKEAQEKvvnfsfdGQPAELKHGsvviaAITSCTNTSNPSvMLGAGLVAKKACDLGLQVKpwIKTSLAPGSGVVTKY 577
Cdd:cd01584 273 ----EVAEKN-------GWPLDLRVG-----LIGSCTNSSYED-MGRAASIAKQALAHGLKCK--SIFTITPGSEQIRAT 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 578 LLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGaaiTENDIVAaavlSGNRNFEGR--VHPLTRAnYLASPPLVVA 655
Cdd:cd01584 334 IERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKG---EKNTIVT----SYNRNFTGRndANPATHA-FVASPEIVTA 405
|
....*.
gi 30678219 656 YALAGT 661
Cdd:cd01584 406 MAIAGT 411
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
788-918 |
2.17e-47 |
|
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: 165.23 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 788 AAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILA 867
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30678219 868 GAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSG 918
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
178-662 |
5.12e-47 |
|
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: 173.14 E-value: 5.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 178 RVLLQDFTGVPAVVDLacmRDAMNKLGSDSNKINplvpvdLVIDHSVQVDvaRSENAVQANMELEFQRnkerfaflKWGS 257
Cdd:cd01583 1 LHLVHDVTSPQAFEGL---REAGREKVWDPEKIV------AVFDHNVPTP--DIKAAEQVKTLRKFAK--------EFGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 258 TAFQnmlvvPPGSGIVHQVNLEylgrvvfntKGLLYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLP 336
Cdd:cd01583 62 NFFD-----VGRQGICHVILPE---------KGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 337 GVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYL 416
Cdd:cd01583 128 ETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 417 KLTGRSDETVAmieaylrannmfvdynEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEmkadwhscldskvgfk 496
Cdd:cd01583 208 KGRGKAYWKEL----------------KSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSE---------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 497 gfAIPKEaqekvvnfsfdgqpaelkhgsVVIAAITSCTNTSNPSVMLGAGLVAKKacdlglQVKPWIKTSLAPGSGVVTK 576
Cdd:cd01583 256 --VEGIK---------------------IDQVFIGSCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPASQRVYK 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 577 YLLKSGLQEYLNEQGFNIVGYGCTTCIG-NSGEINesvgaaitENDIVAAavlSGNRNFEGRVHPLTRANYLASPPLVVA 655
Cdd:cd01583 307 QAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLA--------PGERCVS---TSNRNFKGRMGSPGARIYLASPATAAA 375
|
....*..
gi 30678219 656 YALAGTV 662
Cdd:cd01583 376 SAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
156-662 |
1.87e-46 |
|
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: 172.52 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 156 VEKIidWEKTSPKQV---EIPF-KPARVLLQDFTGVPAVvdlacmrDAMNKLGS----DSNKInplvpVdLVIDHSVQVD 227
Cdd:COG0065 6 AEKI--LARHAGREVepgEIVLlYIDLHLVHDVTSPQAF-------EGLREAGGrkvwDPDRI-----V-AVFDHNVPTK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 228 VARSENAVQANmelefqrnkERFAfLKWGSTAFqnmlvvPPGS-GIVHQVNLEylgrvvfntKGLLYP-DSVVGTDSHTT 305
Cdd:COG0065 71 DPKSAEQVKTL---------REFA-KEFGITFF------DVGDpGICHVVLPE---------QGLVLPgMTIVGGDSHTC 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 306 MIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLS 385
Cdd:COG0065 126 THGAFGAFAFGIGTTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 386 LADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRsdetvamieAYLRANNMFVDynepqQDRVYSSYLELNLDDVEPC 465
Cdd:COG0065 206 MEERMTLCNMAIEAGAKAGIIAPDETTFEYLK--GR---------PFAPWRTLKSD-----EDAVYDKEVEIDASDLEPQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 466 ISGPKRPHDRVTLKEMkadwhscldskvgfKGFAIpkeaqekvvnfsfDgqpaelkhgsvvIAAITSCTNtsnpsvmlG- 544
Cdd:COG0065 270 VAWPHSPDNVVPVSEL--------------EGIKI-------------D------------QVFIGSCTN--------Gr 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 545 ------AGLVAKkacdlGLQVKPWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEInesvgaaIT 618
Cdd:COG0065 303 iedlraAAEILK-----GRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGV-------LA 370
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 30678219 619 ENDIVAAavlSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAGTV 662
Cdd:COG0065 371 PGERCAS---TSNRNFEGRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
179-660 |
7.82e-32 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 129.53 E-value: 7.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 179 VLLQDFTGVPAVvdlacmrDAMNKLGS----DSNKINplvpvdLVIDHsvQVDVARSENAVQANMELEFQRnkerfaflk 254
Cdd:PRK00402 31 VMAHDITGPLAI-------KEFEKIGGdkvfDPSKIV------IVFDH--FVPAKDIKSAEQQKILREFAK--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 255 wgSTAFQNMLVVppGSGIVHQVNLEylgrvvfntKGLLYP-DSVVGTDSHTTMIDGLGVAGWGVGGIE-AEATMLGQPMS 332
Cdd:PRK00402 87 --EQGIPNFFDV--GEGICHQVLPE---------KGLVRPgDVVVGADSHTCTYGALGAFATGMGSTDmAAAMATGKTWF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 333 MVlPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVT 412
Cdd:PRK00402 154 KV-PETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 413 LQYLKltGRSDETVAMIEAYlrannmfvdynepqQDRVYSSYLELNLDDVEPCISGPKRPhDRVtlkemkadwhscldsk 492
Cdd:PRK00402 233 LEYLK--ERAGRDYKPWKSD--------------EDAEYEEVYEIDLSKLEPQVAAPHLP-DNV---------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 493 vgfkgfaipkeaqeKVVnfsfdgqpAELKHGSVVIAAITSCTNtsnpsvmlGaglvakKACDL--------GLQVKPWIK 564
Cdd:PRK00402 280 --------------KPV--------SEVEGTKVDQVFIGSCTN--------G------RLEDLriaaeilkGRKVAPGVR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 565 TSLAPGSGVVTKYLLKSGLQEYLNEQGFnIVGY-GCTTCIGNSGEInesvgaaITENDIVAAavlSGNRNFEGRVHPLTR 643
Cdd:PRK00402 324 LIVIPASQKIYLQALKEGLIEIFVDAGA-VVSTpTCGPCLGGHMGV-------LAPGEVCLS---TTNRNFKGRMGSPES 392
|
490
....*....|....*..
gi 30678219 644 ANYLASPPLVVAYALAG 660
Cdd:PRK00402 393 EVYLASPAVAAASAVTG 409
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
179-662 |
1.87e-30 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 125.25 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 179 VLLQDFTGVPAVvdlacmrDAMNKLGSDSNKiNPlVPVDLVIDHSVQVDvaRSENAVQANMELEFQRnkerfaflKWGST 258
Cdd:TIGR01343 28 AMVHDITAPLAI-------KTLEEYGIDKVW-NP-EKIVIVFDHQVPAD--TIKAAEMQKLAREFVK--------KQGIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 259 AFQnmlvvPPGSGIVHQVNLEylgrvvfntKGLLYP-DSVVGTDSHTTMIDGLGVAGWGVGGIE-AEATMLGQPMSMVlP 336
Cdd:TIGR01343 89 YFY-----DVGEGICHQVLPE---------KGLVKPgDLVVGADSHTCTYGAFGAFATGMGSTDmAYAIATGKTWFKV-P 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 337 GVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYL 416
Cdd:TIGR01343 154 ETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 417 KLTGRSDETVAmieaylrannmfvdynEPQQDRVYSSYLELNLDDVEPCISGPKRPhDRVTlkemkadwhscldskvgfk 496
Cdd:TIGR01343 234 KERRKEPFRVY----------------KSDEDAEYAKEIEIDASQIEPVVACPHNV-DNVK------------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 497 gfaipkeaqekvvnfsfdgQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKacdlglQVKPWIKTSLAPGSGVVTK 576
Cdd:TIGR01343 278 -------------------PVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGR------KVAPDVRLIVIPASRAVYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 577 YLLKSGLQEYLNEQGFNIVGYGCTTCIGnsgeINESVGAaitENDIvaaAVLSGNRNFEGRVHPLTRANYLASPPLVVAY 656
Cdd:TIGR01343 333 QALKEGLIEIFVKAGAVVSTPGCGPCLG----SHQGVLA---PGEV---CISTSNRNFKGRMGHPNAEIYLASPATAAAS 402
|
....*.
gi 30678219 657 ALAGTV 662
Cdd:TIGR01343 403 AVKGYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
268-660 |
8.22e-28 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 118.47 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 268 PGSGIVHqvnleylgrVVFNTKGLLYPDSVVGT-DSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGK 346
Cdd:PRK12466 105 PRQGIVH---------VVAPELGLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 347 MRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRS-DET 425
Cdd:PRK12466 176 LPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLR--GRPrAPK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 426 VAMIE---AYLRAnnMFVDynepqQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEmkadwhscldskvgfkgfAIPK 502
Cdd:PRK12466 254 GALWDaalAYWRT--LRSD-----ADAVFDREVEIDAADIAPQVTWGTSPDQAVPITG------------------RVPD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 503 EAQEKVVNFSFDGQPA----ELKHG----SVVI--AAITSCTNTSNPSVMLGAGLVAkkacdlGLQVKPWIKTSLAPGSG 572
Cdd:PRK12466 309 PAAEADPARRAAMERAldymGLTPGtplaGIPIdrVFIGSCTNGRIEDLRAAAAVLR------GRKVAPGVRAMVVPGSG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 573 VVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGeinesvgaaitenDIVAA---AVLSGNRNFEGRVHPLTRAnYLAS 649
Cdd:PRK12466 383 AVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMND-------------DVLAPgerCASTTNRNFEGRQGPGART-HLMS 448
|
410
....*....|.
gi 30678219 650 PPLVVAYALAG 660
Cdd:PRK12466 449 PAMVAAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
220-662 |
3.09e-26 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 111.55 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 220 IDHSVQvdvarseNAVQANmeLEFQRNKERFAflkwgstAFQNMLVVPPGSGIVHQVNLEylgrvvfntKGLLYPDSV-V 298
Cdd:cd01582 33 LDHDVQ-------NKSEKN--LKKYKNIESFA-------KKHGIDFYPAGRGIGHQIMIE---------EGYAFPGTLaV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 299 GTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYG 378
Cdd:cd01582 88 ASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 379 NGMSGLSLADRATIANMSPEYGATMGFFPVDhvtlqylkltgrsdetvamieaylrannmfvdynepqqdrvySSYLELN 458
Cdd:cd01582 168 SGLNSLSVDTRLTIANMTTEWGALSGLFPTD------------------------------------------AKHLILD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 459 LDDVEPCISGPKRPHDRVTLKEMkadwhscldskvgfkgfaipkEAQEKVVNFSFdgqpaelkhgsvviaaITSCTNTSN 538
Cdd:cd01582 206 LSTLSPYVSGPNSVKVSTPLKEL---------------------EAQNIKINKAY----------------LVSCTNSRA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 539 PSVMLGAGLV-AKKACDLGLQVKPWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGnsgeinesVGAAI 617
Cdd:cd01582 249 SDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG--------LGQGL 320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 30678219 618 TENDIVaaAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTV 662
Cdd:cd01582 321 LEPGEV--GISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
768-922 |
1.80e-21 |
|
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: 90.57 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 768 GDSITTDHISPAGniqkdspaAKFLmergvdrkdfnsygSRRGNDEIMARGTFANirivnklmngeVGPKtvhipsgekl 847
Cdd:cd01579 3 GDNITTDHIMPAG--------AKVL--------------PLRSNIPAISEFVFHR-----------VDPT---------- 39
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30678219 848 svFDAAMRYKSSGedtIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDAD 922
Cdd:cd01579 40 --FAERAKAAGPG---FIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYD 109
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
858-934 |
2.88e-20 |
|
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: 85.98 E-value: 2.88e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30678219 858 SSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDAdtLGLTGHERYTI 934
Cdd:cd00404 12 SPAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDY--LKLHTGDELDI 86
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
271-662 |
7.38e-19 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 90.95 E-value: 7.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 271 GIVHQVNLEylgrvvfntKGLLYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRN 349
Cdd:PRK05478 106 GIVHVVGPE---------QGLTLPGmTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKTMKIEVDGKLPP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 350 GVTATDLVLTVtqmLRKHGV---VGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRS---- 422
Cdd:PRK05478 177 GVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK--GRPfapk 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 423 ----DETVamieAYLR-----ANNMFvdynepqqDRVyssyLELNLDDVEPCIS-GpkrphdrvTLKEMkadwhscldsK 492
Cdd:PRK05478 252 gedwDKAV----AYWKtlksdEDAVF--------DKV----VTLDAADIEPQVTwG--------TNPGQ----------V 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 493 VGFKGfAIPKEAQEK--VVNFSFD----------GQPAELKHGSVVIaaITSCTNtSNPSVMLGAGLVAKkacdlGLQVK 560
Cdd:PRK05478 298 ISIDG-KVPDPEDFAdpVKRASAEralaymglkpGTPITDIKIDKVF--IGSCTN-SRIEDLRAAAAVVK-----GRKVA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 561 PWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGnsgeINesvgaaiteNDIVAA---AVLSGNRNFEGR 637
Cdd:PRK05478 369 PGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLA----MN---------PDKLPPgerCASTSNRNFEGR 435
|
410 420
....*....|....*....|....*
gi 30678219 638 VHPLTRaNYLASPPLVVAYALAGTV 662
Cdd:PRK05478 436 QGKGGR-THLVSPAMAAAAAITGHF 459
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
772-922 |
5.73e-15 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 73.27 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 772 TTDHISPAGniqkdsPAAKFlmergvdrkdfnsygsrRGN-DEIMARGTFANIRIVNKLMNgevgpKTVHIPSGEKLSVF 850
Cdd:cd01578 7 TTDHISAAG------PWLKY-----------------RGHlDNISNNLLIGAINAENGKAN-----SVKNQVTGEYGPVP 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30678219 851 DAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDAD 922
Cdd:cd01578 59 DTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYD 130
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
266-490 |
6.41e-12 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 69.65 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 266 VPPGSGIVHQVNLEYL---GRVVfntkgllypdsvVGTDSHTTMiDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFK 342
Cdd:PRK11413 123 VPPHIAVIHQYMREMMaggGKMI------------LGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVY 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 343 LAGKMRNGVTATDLVLTVTQMLRKHGVV-GKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGR 421
Cdd:PRK11413 190 LTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGR 269
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30678219 422 SDetvamieaylrannmfvDYNE--PQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWHSCLD 490
Cdd:PRK11413 270 GQ-----------------DYCElnPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILR 323
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
768-963 |
2.29e-11 |
|
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: 64.04 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 768 GDSITTDHISPAgniqkdspaaKFLmeRGVDRKDFnsygsrrgndeimARGTFANIRIVNKlmngevgPKTVHipsgekl 847
Cdd:COG0066 15 GDNIDTDQIIPA----------RFL--KTIDREGL-------------GKHLFEDWRYDRS-------PDPDF------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 848 sVFDAAmRYKSSgedTIILAGAEYGSGSSRD---WAakgpmLQ--GVKAVIAKSFERIHRSNLVGMGIIPL-CfkSGEDA 921
Cdd:COG0066 56 -VLNQP-RYQGA---DILVAGRNFGCGSSREhapWA-----LKdyGFRAVIAPSFADIFYRNAINNGLLPIeL--PEEAV 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30678219 922 DTLgltgherytihlpTDISEIRPGQDVTV-------TTDNGKSFTCTV 963
Cdd:COG0066 124 DAL-------------FAAIEANPGDELTVdleagtvTNGTGETYPFEI 159
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
863-913 |
2.06e-10 |
|
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: 57.98 E-value: 2.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 30678219 863 TIILAGAEYGSGSSR---DWAAKGpmlQGVKAVIAKSFERIHRSNLVGMGIIPL 913
Cdd:cd01577 19 DIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
268-660 |
2.29e-10 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 64.06 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 268 PGSGIVHQVnleyLGRvvfntkgLLYPDSV-VGTDSHTTMidGLGVAGWGVGGIEAEATMLGQpMSMVLPGVVGFKLAGK 346
Cdd:cd01581 91 PGDGVIHSW----LNR-------MLLPDTVgTGGDSHTRF--PIGISFPAGSGLVAFAAATGV-MPLDMPESVLVRFKGK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 347 MRNGVTATDLV------------LTVTQMLRKHGVVGKFVEfygngMSGLS--LADRA-TIANMSPEYGATMGFFPVDHV 411
Cdd:cd01581 157 MQPGITLRDLVnaipyyaiqqglLTVEKKGKKNVFNGRILE-----IEGLPdlKVEQAfELTDASAERSAAACTVRLDKE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 412 TL-QYLK--------LTGRSDETVAMIEAYLRANNMFVDYN---EPQQDRVYSSYLELNLDDV-EPCISGPKRPHDRVTL 478
Cdd:cd01581 232 PViEYLEsnvvlmkiMIANGYDDARTLLRRIIAMEEWLANPpllEPDADAEYAAVIEIDLDDIkEPILACPNDPDDVKLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 479 KEmkadwhsCLDSKVGfKGFaipkeaqekvvnfsfdgqpaelkhgsvviaaITSCtntsnpsvMLGAGLVakKACDLGLQ 558
Cdd:cd01581 312 SE-------VAGKKID-EVF-------------------------------IGSC--------MTNIGHF--RAAAKILR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 559 VKPWIKTSL--APGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSgeinesvgAAITENDIVAAavlSGNRNFEG 636
Cdd:cd01581 343 GKEFKPTRLwvAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQ--------ARVADGATVFS---TSTRNFDN 411
|
410 420
....*....|....*....|....
gi 30678219 637 RVHPLTRAnYLASPPLVVAYALAG 660
Cdd:cd01581 412 RVGKGAEV-YLGSAELAAVCALLG 434
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
864-924 |
6.07e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 59.05 E-value: 6.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30678219 864 IILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPlcFKSGEDADTL 924
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDAL 110
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
856-986 |
3.10e-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: 56.66 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 856 YKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLcfksgeDADTLGLTGHERYTIH 935
Cdd:TIGR02087 42 AKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI------EAKTEGIKDGDEVTVD 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30678219 936 LptDISEIRpgqdvtvtTDNGKSFTCtvRFDTEVELAYFNHGGILPYVIRN 986
Cdd:TIGR02087 116 L--ETGEIR--------VNGNEEYKG--EPLPDFLLEILREGGLLEYLKKR 154
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
767-985 |
2.73e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 54.06 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 767 FGDSITTDHISPAGNIQKDSPA--AKFLMErGVDrKDFnsygsrrgndeimargtfaniriVNKLMNGEvgpktvhipsg 844
Cdd:PRK00439 7 FGDNIDTDVIIPARYLNTSDPQelAKHCME-DLD-PEF-----------------------AKKVKPGD----------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 845 eklsvfdaamrykssgedtIILAGAEYGSGSSRD---WAAKGpmlQGVKAVIAKSFERIHRSNLVGMGiIPLcfksgeda 921
Cdd:PRK00439 51 -------------------IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIG-LPV-------- 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30678219 922 dtlgltgherytIHLPTDISEIRPGQDVTVTTDNG--------KSFTCTvRFdTEVELAYFNHGGILPYVIR 985
Cdd:PRK00439 100 ------------LECDEAVDKIEDGDEVEVDLETGvitnlttgEEYKFK-PI-PEFMLEILKAGGLIEYLKK 157
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
268-484 |
3.07e-06 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 51.46 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 268 PGSGIVHQvnleYLGRvvfntkgLLYPDSV-VGTDSHTTMIDGLGV-AGWGVGGIEAEATMLgqPMSMvlPGVVGFKLAG 345
Cdd:PLN00094 537 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAGSGLVAFGAATGVI--PLDM--PESVLVRFTG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 346 KMRNGVTATDLV------------LTVTQMLRKHGVVGKFVEFygNGMSGLSLADRATIANMSPEYGATMGFFPVDH--- 410
Cdd:PLN00094 602 TMQPGITLRDLVhaipytaiqdglLTVEKKGKKNVFSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDKepi 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 411 --------VTLQYLKLTGRSD-----ETVAMIEAYLRANNMFvdynEPQQDRVYSSYLELNLDDV-EPCISGPKRPHDRV 476
Cdd:PLN00094 680 ieylnsnvVMLKWMIAEGYGDrrtleRRIARMQQWLADPELL----EADPDAEYAAVIEIDMDEIkEPILCAPNDPDDAR 755
|
....*...
gi 30678219 477 TLKEMKAD 484
Cdd:PLN00094 756 LLSEVTGD 763
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
855-912 |
2.44e-05 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 46.27 E-value: 2.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30678219 855 RYKSSgedTIILAGAEYGSGSSRD---WAakgpmLQ--GVKAVIAKSFERIHRSNLVGMGIIP 912
Cdd:PRK01641 64 RYQGA---SILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
268-366 |
2.45e-04 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 45.17 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30678219 268 PGSGIVHQVnleyLGRvvfntkgLLYPDSV-VGTDSHTTMidGLGVAGWGVGGIEAEATMLG-QPMSM---VLpgvVGFK 342
Cdd:PRK09238 463 PGDGVIHSW----LNR-------MLLPDTVgTGGDSHTRF--PIGISFPAGSGLVAFAAATGvMPLDMpesVL---VRFK 526
|
90 100
....*....|....*....|....*
gi 30678219 343 laGKMRNGVTATDLV-LTVTQMLRK 366
Cdd:PRK09238 527 --GEMQPGITLRDLVhAIPYYAIKQ 549
|
|
| |
