|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-927 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1631.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 1 MTDTLPFDAVRELDVDGTTYKMADLRALEEQGLCDLDTLPVSIRILLESVLRNADGETVTAADVKNAAGWKPD-VPDAEV 79
Cdd:PRK09277 1 MSSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKaKPDREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 80 PFSPSRVVLQDLTGVPAVVDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRA 159
Cdd:PRK09277 81 PFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 160 IKWAQNAFENFNVVPPGTGIVHQVNLEHLGRVVHAReQDGENWLLPDTLVGTDSHTPMiggigvvgwgvggiEAEAAMLG 239
Cdd:PRK09277 161 LKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTR-EDGELVAYPDTLVGTDSHTTMinglgvlgwgvggiEAEAAMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 240 QPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPV 319
Cdd:PRK09277 240 QPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 320 DEQTLEYLELTGRDPDHVDLVREYLEAQGLFGE--QEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQSFRGLLHG 397
Cdd:PRK09277 320 DEETLDYLRLTGRDEEQVALVEAYAKAQGLWRDplEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 398 efeddlddvdedalqrwlGEGGAADAETDggvqvepeselhpltkrvevdlDGETVEIGHGDVLVSAITSCTNTSNPSVM 477
Cdd:PRK09277 400 ------------------GVQGFGLDEAE----------------------EGEDYELPDGAVVIAAITSCTNTSNPSVM 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 478 IAAGLLAQNAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDL 557
Cdd:PRK09277 440 IAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 558 WTTSVLSGNRNFEARIHPKIRANYLASPPLVVAYGLAGRMDIDLEHEPLGTDDEGNPVYLADIWPDAADVQAAIHENVSP 637
Cdd:PRK09277 520 VVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKP 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 638 EMFEEKYASVFEGDERWAALDAPTGDVYEWDEDSTYIREPPFFKDFPVEKPGVADIEDARCLLTLGDTVTTDHISPAGPF 717
Cdd:PRK09277 600 EMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAI 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 718 GPDLPAGQWLLDHGVEPHEFNTYGARRGNHEVMMRGTFANVRIENEMLDDVEGGYTIHHPTDEQTTVFEASRRYRDEGIP 797
Cdd:PRK09277 680 KADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTP 759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 798 LVVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEVFTIHGLDDgLD 877
Cdd:PRK09277 760 LVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLED-LK 838
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 499541635 878 VMDELTVIAERADGSTVEFPVTAQVGTPAAVTYIEHGGILHYVLRRLLRQ 927
Cdd:PRK09277 839 PGATVTVVITRADGEVVEFPVLCRIDTAVEVDYYRNGGILQYVLRDLLAS 888
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-927 |
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: 1592.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 3 DTLPFDAVRELDVDGTTYKMADLRALEEQGlCDLDTLPVSIRILLESVLRNADGETVTAADVKNAAGWKPD-VPDAEVPF 81
Cdd:COG1048 1 SMDSFKARKTLTVGGKPYTYYSLPALEEAG-GDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKaRGDDEIPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 82 SPSRVVLQDLTGVPAVVDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRAIK 161
Cdd:COG1048 80 RPARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 162 WAQNAFENFNVVPPGTGIVHQVNLEHLGRVVHAREQDGENWLLPDTLVGTDSHTPMiggigvvgwgvggiEAEAAMLGQP 241
Cdd:COG1048 160 WGQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMinglgvlgwgvggiEAEAAMLGQP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 242 VTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDE 321
Cdd:COG1048 240 VSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 322 QTLEYLELTGRDPDHVDLVREYLEAQGLFGE---QEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQSFRGLLhge 398
Cdd:COG1048 320 ETLDYLRLTGRSEEQIELVEAYAKAQGLWRDpdaPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAAL--- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 399 feddlddvdedalqrwlgeggaadaetdggvqvePESELHPLTKRVEVDLDGETVEIGHGDVLVSAITSCTNTSNPSVMI 478
Cdd:COG1048 397 ----------------------------------AAPVGEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 479 AAGLLAQNAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDLW 558
Cdd:COG1048 443 AAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLV 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 559 TTSVLSGNRNFEARIHPKIRANYLASPPLVVAYGLAGRMDIDLEHEPLGTDDEGNPVYLADIWPDAADVQAAIHENVSPE 638
Cdd:COG1048 523 VAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPE 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 639 MFEEKYASVFEGDERWAALDAPTGDVYEWDEDSTYIREPPFFKDFPVEKPGVADIEDARCLLTLGDTVTTDHISPAGPFG 718
Cdd:COG1048 603 MFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIK 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 719 PDLPAGQWLLDHGVEPHEFNTYGARRGNHEVMMRGTFANVRIENEMLDDVEGGYTIHHPTDEQTTVFEASRRYRDEGIPL 798
Cdd:COG1048 683 ADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPL 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 799 VVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEVFTIHGLDDGLDV 878
Cdd:COG1048 763 VVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAP 842
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 499541635 879 MDELTVIAERADGSTVEFPVTAQVGTPAAVTYIEHGGILHYVLRRLLRQ 927
Cdd:COG1048 843 GKTVTVTATRADGSTEEFPVLHRIDTPVEVEYYRAGGILQYVLRQLLAA 891
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
7-926 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1338.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 7 FDAVRELDVDGTTYKMADLRALEEQGLCDLDTLPVSIRILLESVLRNADGETVTAADVKNAAGWKPD-VPDAEVPFSPSR 85
Cdd:PRK12881 6 HKTLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPErKSDDEIPFVPAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 86 VVLQDLTGVPAVVDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRAIKWAQN 165
Cdd:PRK12881 86 VVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 166 AFENFNVVPPGTGIVHQVNLEHLGRVVHAREQDGENWLLPDTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTMK 245
Cdd:PRK12881 166 AFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYML 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 246 LPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTLE 325
Cdd:PRK12881 246 IPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 326 YLELTGRDPDHVDLVREYLEAQGLFGE--QEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQSFRGLLhgefeddl 403
Cdd:PRK12881 326 YLRLTGRTEAQIALVEAYAKAQGLWGDpkAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLF-------- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 404 ddvdedalqrwlgeggaADAETDGGVQVEPEselhpltkrvevdlDGETVEIGHGDVLVSAITSCTNTSNPSVMIAAGLL 483
Cdd:PRK12881 398 -----------------SKPVAENGFAKKAQ--------------TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 484 AQNAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDLWTTSVL 563
Cdd:PRK12881 447 AKKAVERGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 564 SGNRNFEARIHPKIRANYLASPPLVVAYGLAGRMDIDLEHEPLGTDDEGNPVYLADIWPDAADVQAAIHENVSPEMFEEK 643
Cdd:PRK12881 527 SGNRNFEGRIHPNIKANFLASPPLVVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKN 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 644 YASVFEGDERWAALDAPTGDVYEWDEDSTYIREPPFFKDFPVEKPGVADIEDARCLLTLGDTVTTDHISPAGPFGPDLPA 723
Cdd:PRK12881 607 YAEVFKGSELWAAIEAPDGPLYDWDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPA 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 724 GQWLLDHGVEPHEFNTYGARRGNHEVMMRGTFANVRIENEMLDDVEGGYTIHHPTDEQTTVFEASRRYRDEGIPLVVMAG 803
Cdd:PRK12881 687 GKYLKENGVPKADFNSYGSRRGNHEVMMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAG 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 804 EEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEVFTIHGLDDGLDVMDELT 883
Cdd:PRK12881 767 EEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVT 846
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 499541635 884 VIAERADGSTVEFPVTAQVGTPAAVTYIEHGGILHYVLRRLLR 926
Cdd:PRK12881 847 LVIHRADGSTERVPVLCRIDTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
6-927 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1254.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 6 PFDAVRELDVDGTTYKMADLRALEEQglcDLDTLPVSIRILLESVLRNADGETVTAADVKNAAGWKPDVP-DAEVPFSPS 84
Cdd:PTZ00092 15 PFEKVLKTLKDGGSYKYYSLNELHDP---RLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKkQIEIPFKPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAVVDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRAIKWAQ 164
Cdd:PTZ00092 92 RVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 165 NAFENFNVVPPGTGIVHQVNLEHLGRVVHareqDGENWLLPDTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTM 244
Cdd:PTZ00092 172 KAFKNLLIVPPGSGIVHQVNLEYLARVVF----NKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 245 KLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTL 324
Cdd:PTZ00092 248 VLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 325 EYLELTGRDPDHVDLVREYLEAQGLF--GEQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQSFrgllhgefedd 402
Cdd:PTZ00092 328 DYLKQTGRSEEKVELIEKYLKANGLFrtYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDF----------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 403 lddvdEDALQRWLGEGGAADAETDggvqvepeselhpLTKRVEVDLDGETVEIGHGDVLVSAITSCTNTSNPSVMIAAGL 482
Cdd:PTZ00092 397 -----TACLSAPVGFKGFGIPEEK-------------HEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 483 LAQNAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDLWTTSV 562
Cdd:PTZ00092 459 LAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAV 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 563 LSGNRNFEARIHPKIRANYLASPPLVVAYGLAGRMDIDLEHEPLGTDDEGNPVYLADIWPDAADVQAAIHENVSPEMFEE 642
Cdd:PTZ00092 539 LSGNRNFEGRVHPLTRANYLASPPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKE 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 643 KYASVFEGDERWAALDAPTGDVYEWDEDSTYIREPPFFKDFPVEKPGVADIEDARCLLTLGDTVTTDHISPAGPFGPDLP 722
Cdd:PTZ00092 619 VYSNITQGNKQWNELQVPKGKLYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSP 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 723 AGQWLLDHGVEPHEFNTYGARRGNHEVMMRGTFANVRIENEMLDDVeGGYTIHHPTDEQTTVFEASRRYRDEGIPLVVMA 802
Cdd:PTZ00092 699 AAKYLMERGVERKDFNTYGARRGNDEVMVRGTFANIRLINKLCGKV-GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLA 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 803 GEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEVFTIHGLDDGLDVMDEL 882
Cdd:PTZ00092 778 GKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQDV 857
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 499541635 883 TViaERADGSTveFPVTAQVGTPAAVTYIEHGGILHYVLRRLLRQ 927
Cdd:PTZ00092 858 TV--KTDTGKT--FDTILRIDTEVEVEYFKHGGILQYVLRKLVKG 898
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
19-925 |
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: 1253.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 19 TYKMADLRALEEQGLcDLDTLPVSIRILLESVLRNADGETVTAADVKNAAGWK-PDVPDAEVPFSPSRVVLQDLTGVPAV 97
Cdd:TIGR01341 2 TYYYYSLKALEESGG-KISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKiGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 98 VDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRAIKWAQNAFENFNVVPPGT 177
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 178 GIVHQVNLEHLGRVVHAREQDGENWLLPDTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTMKLPEVVGVRLEGE 257
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 258 LPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTLEYLELTGRDPDHV 337
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 338 DLVREYLEAQGLFGE--QEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQSFrgllhgefeddlddvdedalqrwl 415
Cdd:TIGR01341 321 ELVEKYARAQGLFYDdsEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKF------------------------ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 416 geggAADAETDGGVQVEPESElHPLTKRVEvdldGETVEIGHGDVLVSAITSCTNTSNPSVMIAAGLLAQNAVEKGLDVP 495
Cdd:TIGR01341 377 ----SKELEKNGGDKGFTLRK-EPLKKKVN----GQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 496 PYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDLWTTSVLSGNRNFEARIHP 575
Cdd:TIGR01341 448 PYVKTSLAPGSKVVTDYLAESGLLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHP 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 576 KIRANYLASPPLVVAYGLAGRMDIDLEHEPLGTDDEGNPVYLADIWPDAADVQAAIHENVSPEMFEEKYASVFEGDERWA 655
Cdd:TIGR01341 528 LVKGNYLASPPLVVAYALAGNIDINLYTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWN 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 656 ALDAPTGDVYEWDEDSTYIREPPFFKDFPVEKPGVADIEDARCLLTLGDTVTTDHISPAGPFGPDLPAGQWLLDHGVEPH 735
Cdd:TIGR01341 608 SIKTPSGDTYSWDEKSTYIRLPPFFEEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRR 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 736 EFNTYGARRGNHEVMMRGTFANVRIENEMLDDVEGGYTIHHPTDEQTTVFEASRRYRDEGIPLVVMAGEEFGTGSSRDWA 815
Cdd:TIGR01341 688 DFNSYGSRRGNHEVMMRGTFANIRIKNLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWA 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 816 AKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEVFTIHGLDDgLDVMDELTVIAERADGSTVE 895
Cdd:TIGR01341 768 AKGTKLLGVKAVIAESFERIHRSNLVGMGVIPLQFPQGEDAETLGLTGDETIDIDGIKD-LKPGKEVTVTFTNSKGEKIT 846
|
890 900 910
....*....|....*....|....*....|
gi 499541635 896 FPVTAQVGTPAAVTYIEHGGILHYVLRRLL 925
Cdd:TIGR01341 847 FKCVLRIDTEVELDYYKHGGILQYVLRKFL 876
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
36-927 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1014.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 36 LDTLPVSIRILLESVLRNADGETVTAADVKNAAGWKPDVPD-AEVPFSPSRVVLQDLTGVPAVVDLAALRSEVDRKDRDP 114
Cdd:PLN00070 74 IDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKqVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNNLGGDP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 115 TLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRAIKWAQNAFENFNVVPPGTGIVHQVNLEHLGRVVHa 194
Cdd:PLN00070 154 NKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVF- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 195 reqDGENWLLPDTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITER 274
Cdd:PLN00070 233 ---NTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 275 LREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTLEYLELTGRDPDHVDLVREYLEAQGLF---- 350
Cdd:PLN00070 310 LRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFvdyn 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 351 -GEQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQSFRGLLHGEfeddlddvdedalqrwLGEGGAAdaetdggv 429
Cdd:PLN00070 390 ePQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNK----------------VGFKGFA-------- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 430 qVEPESElhplTKRVEVDLDGETVEIGHGDVLVSAITSCTNTSNPSVMIAAGLLAQNAVEKGLDVPPYVKTSLAPGSRVV 509
Cdd:PLN00070 446 -VPKEAQ----SKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVV 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 510 TQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDLWTTSVLSGNRNFEARIHPKIRANYLASPPLVV 589
Cdd:PLN00070 521 TKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVV 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 590 AYGLAGRMDIDLEHEPLGTDDEGNPVYLADIWPDAADVQAAIHENVSPEMFEEKYASVFEGDERWAALDAPTGDVYEWDE 669
Cdd:PLN00070 601 AYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDP 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 670 DSTYIREPPFFKDFPVEKPGVADIEDARCLLTLGDTVTTDHISPAGPFGPDLPAGQWLLDHGVEPHEFNTYGARRGNHEV 749
Cdd:PLN00070 681 KSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEI 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 750 MMRGTFANVRIENEMLDDVEGGYTIHHPTDEQTTVFEASRRYRDEGIPLVVMAGEEFGTGSSRDWAAKGTDLLGVRATIA 829
Cdd:PLN00070 761 MARGTFANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIA 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 830 ESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEVFTIHGLDD------GLDVmdelTVIAERADgstvEFPVTAQVG 903
Cdd:PLN00070 841 KSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNiseikpGQDV----TVTTDNGK----SFTCTLRFD 912
|
890 900
....*....|....*....|....
gi 499541635 904 TPAAVTYIEHGGILHYVLRRLLRQ 927
Cdd:PLN00070 913 TEVELAYFDHGGILPYVIRNLIKQ 936
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
85-597 |
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: 676.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAVVDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSVQVDYFDSEDAYEKNVELEYERNAERYRAIKWAQ 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 165 NAFENFNVVPPGTGIVHQVNLEHLGRVVHAREQDGENWLLPDTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTM 244
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 245 KLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDeqtl 324
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 325 eyleltgrdpdhvdlvreyleaqglfgeqepeyTEVVEFDLSTVEPSLAGHKRPQDRIPMgdvkqsfrgllhgefeddld 404
Cdd:cd01586 237 ---------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL-------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 405 dvdedalqrwlgeggaadaetdggvqvepeselhpltkrvevdldgetveigHGDVLVSAITSCTNTSNPSVMIAAGLLA 484
Cdd:cd01586 264 ----------------------------------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLA 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 485 QNAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPDPIEQAIDDHDLWTTSVLS 564
Cdd:cd01586 292 KKAVELGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLS 371
|
490 500 510
....*....|....*....|....*....|...
gi 499541635 565 GNRNFEARIHPKIRANYLASPPLVVAYGLAGRM 597
Cdd:cd01586 372 GNRNFEGRIHPLVRANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
76-595 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 562.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 76 DAEVPFSPSRVVLQDLTGVPAVVDLAALRSEVDRKDRDPTLVEPEIPIDLVIDHSvqvdyfdsEDAYEKNVELEYERNAE 155
Cdd:pfam00330 13 DGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISRNKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 156 RYRAIKWAQNAFeNFNVVPPGTGIVHQVNLEHLgrvvhareqdgenWLLPD-TLVGTDSHTPMiggigvvgwgvggiEAE 234
Cdd:pfam00330 85 QYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTThgglgalafgvggsEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 235 AAMLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTI 314
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 315 SMFPVDEQTLEYLELTGRDPDHVdlVREYLEAQGLFG---EQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPM-GDVKQS 390
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTlasDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLsELVPDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 391 FrgllhgefeddlddvdedalqrwlgeggaADAETDGGVQvepeselhpltKRVEVDLDGETVEIGHGDVLVSAITSCTN 470
Cdd:pfam00330 309 F-----------------------------ADAVKRKAAE-----------RALEYMGLGPGTPLSDGKVDIAFIGSCTN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 471 TSNPSVMIAAGLLAQnAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPdpieq 550
Cdd:pfam00330 349 SSIEDLRAAAGLLKK-AVEKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----- 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499541635 551 aidDHDlwtTSVLSGNRNFEARIHPKIRAnYLASPPLVVAYGLAG 595
Cdd:pfam00330 423 ---PGE---RCVSSSNRNFEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
702-871 |
2.29e-100 |
|
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: 310.36 E-value: 2.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 702 LGDTVTTDHISPAGPFGPDLPAGQWLLDHGVEPHEFNTYGARRGNHEVMMRGTFANVRIENEMLDDVEGGYTIHHPTDEQ 781
Cdd:cd01580 2 LGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 782 TTVFEASRRYRDEGIPLVVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGL 861
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLGL 161
|
170
....*....|
gi 499541635 862 DGSEVFTIHG 871
Cdd:cd01580 162 TGEETYDIIG 171
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
74-924 |
9.72e-85 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 285.50 E-value: 9.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 74 VPDAEVPFSPSRVVLQDLTGVPAVVDLAALrsEVDRKdRDPTLVEpeipidlVIDHS-VQVDYfdsedayeknveleyeR 152
Cdd:PRK07229 20 EPGEEIAIRIDQTLTQDATGTMAYLQFEAM--GLDRV-KTELSVQ-------YVDHNlLQADF----------------E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 153 NAERYRAIkwaQNAFENFNVV--PPGTGIVHQVNLEHLGRvvhareqdgenwllP-DTLVGTDSHTPMIGGIGVVGWGVG 229
Cdd:PRK07229 74 NADDHRFL---QSVAAKYGIYfsKPGNGICHQVHLERFAF--------------PgKTLLGSDSHTPTAGGLGMLAIGAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 230 GIEAEAAMLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPE 309
Cdd:PRK07229 137 GLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 310 QGSTISMFPVDEQTLEYLELTGRDPDHVDLVreyleaqglfGEQEPEYTEVVEFDLSTVEPSLAGHKRPqDRipmgdvkq 389
Cdd:PRK07229 217 LGATTSIFPSDERTREFLKAQGREDDWVELL----------ADPDAEYDEVIEIDLSELEPLIAGPHSP-DN-------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 390 sfrgllhgefeddlddvdedalqrwlgeggaadaetdggvqVEPESELhpltKRVEVDldgetveighgdvlVSAITSCT 469
Cdd:PRK07229 278 -----------------------------------------VVPVSEV----AGIKVD--------------QVLIGSCT 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 470 NTSNPSVMIAAGLLaqnaveKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGplpDPIE 549
Cdd:PRK07229 299 NSSYEDLMRAASIL------KGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APAT 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 550 QAIddhdlwttSVLSGNRNFEARIHPKIRANYLASPPLVVAYGLAGRMDidleheplgtddegNPVYLADIWPDAADVQA 629
Cdd:PRK07229 370 GNV--------SLRTFNRNFPGRSGTKDAQVYLASPETAAASALTGVIT--------------DPRTLALENGEYPKLEE 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 630 AIHENVSPEMFEEkyasvfegderwaalDAPTGDVYEwdedstyIREPPFFKDFPVEKPgVADIEDARCLLTLGDTVTTD 709
Cdd:PRK07229 428 PEGFAVDDAGIIA---------------PAEDGSDVE-------VVRGPNIKPLPLLEP-LPDLLEGKVLLKVGDNITTD 484
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 710 HISPAGPfgpdlpagQWLldhgvephefntygarrgnhevMMRGtfaNV-RIENEMLddveggytihHPTDEqttvfEAS 788
Cdd:PRK07229 485 HIMPAGA--------KWL----------------------PYRS---NIpNISEFVF----------EGVDN-----TFP 516
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 789 RRYRDEGIPLVVmAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDgsEVFT 868
Cdd:PRK07229 517 ERAKEQGGGIVV-GGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEG--DVLE 593
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 499541635 869 IHGLDDGLDvMDELTVIAERADgstVEFPVTAQVgTPAAVTYIEHGGILHYVLRRL 924
Cdd:PRK07229 594 IEDLREFLP-GGPLTVVNVTKD---EEIEVRHTL-SERQIEILLAGGALNLIKKKL 644
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-595 |
4.23e-78 |
|
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: 259.35 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAVVDLAALRseVDRKDRDPTlvepeiPIDLVIDHSVQvdyfdsedayeknveLEYERNAERYRAIKWAQ 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILA--ALGKVADPS------QIACVHDHAVQ---------------LEKPVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 165 NAFEnFNVVPPGTGIVHQVNLEHLGrvvhareqdgenwLLPDTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTM 244
Cdd:cd01351 58 ALQG-IAFYRPGVGIIHQIMVENLA-------------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 245 KLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTL 324
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 325 EYLELTGR--DPDHVDLVREYLEAQGlfgeqEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQsfrgllhgefedd 402
Cdd:cd01351 204 KWLEATGRplLKNLWLAFPEELLADE-----GAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 403 lddvdedalqrwlgeggaadaetdggvqvepeselhpltkrvevdldgetveighGDVLVSAITSCTNtSNPSVMIAAGL 482
Cdd:cd01351 266 -------------------------------------------------------TKIDQVLIGSCTN-NRYSDMLAAAK 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 483 LAqnaveKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPdpieqaiddhDLWTTSV 562
Cdd:cd01351 290 LL-----KGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLV----------ADGEVGV 354
|
490 500 510
....*....|....*....|....*....|...
gi 499541635 563 LSGNRNFEARIHPKIRANYLASPPLVVAYGLAG 595
Cdd:cd01351 355 SSGNRNFPGRLGTYERHVYLASPELAAATAIAG 387
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
87-595 |
2.29e-53 |
|
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: 190.74 E-value: 2.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 87 VLQDLTGVPAVVDLAALrsEVDRkdrdptlVEPEIPIDLVIDHSVQVDYfdsedayeknveleyeRNAERYRAIkwaQNA 166
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--GVDR-------VRTELSVSYVDHNTLQTDF----------------ENADDHRFL---QTV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 167 FENFNVV--PPGTGIVHQVNLEHLGRvvhareqdgenwllP-DTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVT 243
Cdd:cd01585 56 AARYGIYfsRPGNGICHQVHLERFAV--------------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 244 MKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQT 323
Cdd:cd01585 122 IPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 324 LEYLELTGRDPDHVDLVreyleaqglfGEQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVkqsfrgllhgefeddl 403
Cdd:cd01585 202 REFLAAQGREDDWVELA----------ADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREV---------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 404 ddvdedalqrwlgeggaadaetdGGVQVepeselhpltkrvevdldgETVEIGhgdvlvsaitSCTNTSNPSVMIAAGLL 483
Cdd:cd01585 256 -----------------------AGIKV-------------------DQVAIG----------SCTNSSYEDLMTVAAIL 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 484 aqnaveKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAG-PLPDPIeqaiddhdlwttSV 562
Cdd:cd01585 284 ------KGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQaPPTGGV------------SV 345
|
490 500 510
....*....|....*....|....*....|...
gi 499541635 563 LSGNRNFEARIHPKIRANYLASPPLVVAYGLAG 595
Cdd:cd01585 346 RTFNRNFEGRSGTKDDLVYLASPEVAAAAALTG 378
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
85-596 |
4.66e-46 |
|
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: 170.06 E-value: 4.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAVvdlAALRSEVDRKDRDPTLvepeipIDLVIDHSVQVDyfdSEDAYEKNVELEyeRNAERYRAikwaq 164
Cdd:cd01583 1 LHLVHDVTSPQAF---EGLREAGREKVWDPEK------IVAVFDHNVPTP---DIKAAEQVKTLR--KFAKEFGI----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 165 nafENFNVVppGTGIVHQVNLEhlgrvvhareqdgENWLLP-DTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVT 243
Cdd:cd01583 62 ---NFFDVG--RQGICHVILPE-------------KGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLW 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 244 MKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQT 323
Cdd:cd01583 124 FRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 324 LEYLEltgrdpdhvdlVREYLEAQGLFGEQEPEYTEVVEFDLSTVEPSLA-GHkRPQDRIPMGdvkqsfrgllhgefedd 402
Cdd:cd01583 204 FEYLK-----------GRGKAYWKELKSDEDAEYDKVVEIDASELEPQVAwPH-SPDNVVPVS----------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 403 lddvdedalqrwlgeggaadaetdggvQVEPeselhpltkrVEVDldgeTVEIGhgdvlvsaitSCTNTSNPSVMIAAGL 482
Cdd:cd01583 255 ---------------------------EVEG----------IKID----QVFIG----------SCTNGRLEDLRAAAEI 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 483 LaqnaveKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIG-NAGPLPDpieqaiDDHDLWTTs 561
Cdd:cd01583 284 L------KGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAP------GERCVSTS- 350
|
490 500 510
....*....|....*....|....*....|....*.
gi 499541635 562 vlsgNRNFEARI-HPKIRaNYLASPPLVVAYGLAGR 596
Cdd:cd01583 351 ----NRNFKGRMgSPGAR-IYLASPATAAASAITGE 381
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-597 |
4.25e-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: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAVVDLAAlrsevdrkdrdPTLVEPEIPIDLVIDHSVQvdyfdSEDAYEKNVELEYERNAERYRAIKWAQ 164
Cdd:cd01584 1 RVAMQDATAQMALLQFMS-----------SGLPKVAVPSTIHCDHLIE-----AQVGGEKDLKRAKDINKEVYDFLASAG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 165 NAFeNFNVVPPGTGIVHQVNLEhlgrvvhareqdgeNWLLPDTL-VGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVT 243
Cdd:cd01584 65 AKY-GIGFWKPGSGIIHQIVLE--------------NYAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 244 MKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQT 323
Cdd:cd01584 130 LKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 324 LEYLELTGRDpDHVDLVREYlEAQGLFGEQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGDVKQsfrgllhgefeddl 403
Cdd:cd01584 210 KKYLKATGRA-EIADLADEF-KDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKE-------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 404 ddvdedalqrwlgeggaadaetdggvqvEPESELHPLtkrvevdldgetveighgDVLVSAITSCTNTSNPSvMIAAGLL 483
Cdd:cd01584 274 ----------------------------VAEKNGWPL------------------DLRVGLIGSCTNSSYED-MGRAASI 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 484 AQNAVEKGLDvpPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAgplpdpieqaiDDHDL----WT 559
Cdd:cd01584 307 AKQALAHGLK--CKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQW-----------DRKDIkkgeKN 373
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499541635 560 TSVLSGNRNFEAR--IHPKIRAnYLASPPLVVAYGLAGRM 597
Cdd:cd01584 374 TIVTSYNRNFTGRndANPATHA-FVASPEIVTAMAIAGTL 412
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
731-853 |
9.35e-44 |
|
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: 154.83 E-value: 9.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 731 GVEPHEFNTYGARRGNHEVMMRGTFANVRIENEMLDDVEGGYTIHHPTDEQTTVFEASRRYRDEGIPLVVMAGEEFGTGS 810
Cdd:pfam00694 9 GKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIGGKNFGCGS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 499541635 811 SRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDG 853
Cdd:pfam00694 89 SREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
85-596 |
7.04e-40 |
|
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: 152.88 E-value: 7.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAVvdlAALRSEVDRKDRDPTLvepeipIDLVIDHSVqvdyfdsedaYEKNveleyERNAERYRAIKwaQ 164
Cdd:COG0065 30 LHLVHDVTSPQAF---EGLREAGGRKVWDPDR------IVAVFDHNV----------PTKD-----PKSAEQVKTLR--E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 165 NAFEnFNVV--PPGT-GIVHQVNLEHlGRVvhareqdgenwlLP-DTLVGTDSHTPMiggigvvgwgvggiEAEAAMLGQ 240
Cdd:COG0065 84 FAKE-FGITffDVGDpGICHVVLPEQ-GLV------------LPgMTIVGGDSHTCThgafgafafgigttDVAHVLATG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 241 PVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVD 320
Cdd:COG0065 150 TLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 321 EQTLEYLEltgrdpdhvdlVREYLEAQGLFGEQEPEYTEVVEFDLSTVEPSLA-GHkRPQDRIPMGDVKQsfrgllhgef 399
Cdd:COG0065 230 ETTFEYLK-----------GRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAwPH-SPDNVVPVSELEG---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 400 eddlddvdedalqrwlgeggaadaetdggvqvepeselhpltkrVEVDldgeTVEIGhgdvlvsaitSCTNTsnpsvMI- 478
Cdd:COG0065 288 --------------------------------------------IKID----QVFIG----------SCTNG-----RIe 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 479 ----AAGLLaqnaveKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIG-NAGPLPDPiEQAId 553
Cdd:COG0065 305 dlraAAEIL------KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAPG-ERCA- 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 499541635 554 dhdlwTTSvlsgNRNFEARI-HPKIRAnYLASPPLVVAYGLAGR 596
Cdd:COG0065 377 -----STS----NRNFEGRMgSPGSRT-YLASPATAAASAIAGR 410
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
48-596 |
4.91e-33 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 132.99 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 48 ESVLRNADGETVTAADVKNAagwKPDVpdaevpfspsrVVLQDLTGVPAVvdlAALRSEVDRKDRDPTlvepeiPIDLVI 127
Cdd:PRK00402 7 EKILARHSGRDVSPGDIVEA---KVDL-----------VMAHDITGPLAI---KEFEKIGGDKVFDPS------KIVIVF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 128 DHSVQvdyfdsedayEKNVELeyernAERYRAI-KWAQN-AFENFNVVppGTGIVHQVNLEHlGRVvhareqdgenwlLP 205
Cdd:PRK00402 64 DHFVP----------AKDIKS-----AEQQKILrEFAKEqGIPNFFDV--GEGICHQVLPEK-GLV------------RP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 206 -DTLVGTDSHTP----------------MiggigvvgwgvggieAEAAMLGQpVTMKLPEVVGVRLEGELPEGATATDLV 268
Cdd:PRK00402 114 gDVVVGADSHTCtygalgafatgmgstdM---------------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 269 LHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTLEYL-ELTGRDPDHVdlvreyleaq 347
Cdd:PRK00402 178 LHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLkERAGRDYKPW---------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 348 glFGEQEPEYTEVVEFDLSTVEPSLA-GHKrPQdripmgdvkqsfrgllhgefeddlddvdedalqrwlgeggaadaetd 426
Cdd:PRK00402 248 --KSDEDAEYEEVYEIDLSKLEPQVAaPHL-PD----------------------------------------------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 427 ggvQVEPESELhpltKRVEVDLdgetVEIGhgdvlvsaitSCTNTSNPSVMIAAGLLaqnaveKGLDVPPYVKTSLAPGS 506
Cdd:PRK00402 278 ---NVKPVSEV----EGTKVDQ----VFIG----------SCTNGRLEDLRIAAEIL------KGRKVAPGVRLIVIPAS 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 507 RVVTQYLEESGLLPYLEELGyAVVGY-GCTTCIG-NAGPLPDPiEQAIddhdlwTTSvlsgNRNFEARI-HP--KIranY 581
Cdd:PRK00402 331 QKIYLQALKEGLIEIFVDAG-AVVSTpTCGPCLGgHMGVLAPG-EVCL------STT----NRNFKGRMgSPesEV---Y 395
|
570
....*....|....*
gi 499541635 582 LASPPLVVAYGLAGR 596
Cdd:PRK00402 396 LASPAVAAASAVTGK 410
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
123-597 |
4.82e-26 |
|
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: 111.77 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 123 IDLVIDHSVQVDYFDSEDAYEKnveleyernaeryrAIKWAQN-AFENFNvvPPGTGIVHQVNLEhlgrvvhareqdgEN 201
Cdd:TIGR01343 56 IVIVFDHQVPADTIKAAEMQKL--------------AREFVKKqGIKYFY--DVGEGICHQVLPE-------------KG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 202 WLLP-DTLVGTDSHTPMIGGIGVVGWGVGGIEAEAAMLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGV 280
Cdd:TIGR01343 107 LVKPgDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 281 VDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPVDEQTLEYLELTGRDPdhvdlVREYLeaqglfGEQEPEYTEV 360
Cdd:TIGR01343 187 TYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP-----FRVYK------SDEDAEYAKE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 361 VEFDLSTVEPSLAGHKRPQDripmgdvkqsfrgllhgefeddlddvdedalqrwlgeggaadaetdggvqVEPESELhpl 440
Cdd:TIGR01343 256 IEIDASQIEPVVACPHNVDN--------------------------------------------------VKPVSEV--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 441 tKRVEVDldgeTVEIGhgdvlvsaitSCTNTSNPSVMIAAGLLaqnaveKGLDVPPYVKTSLAPGSR-VVTQYLEEsGLL 519
Cdd:TIGR01343 283 -EGTEID----QVFIG----------SCTNGRLEDLRVAAKIL------KGRKVAPDVRLIVIPASRaVYLQALKE-GLI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 520 PYLEELGyAVVGY-GCTTCIGNAGPLPDPIEQAIddhdlwTTSvlsgNRNFEARI-HPKIRAnYLASPPLVVAYGLAGRM 597
Cdd:TIGR01343 341 EIFVKAG-AVVSTpGCGPCLGSHQGVLAPGEVCI------STS----NRNFKGRMgHPNAEI-YLASPATAAASAVKGYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
85-596 |
9.50e-26 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 111.92 E-value: 9.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 85 RVVLQDLTGVPAvvdLAALRsEVDRKDRDPTLVEpeipidLVIDHSV-----------------QVDYFDsedayeknve 147
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLR-ARGRTVRRPDLTL------AVVDHVVptrpgrdrgitdpggalQVDYLR---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 148 leyeRNAERYraikwaqnAFENFNVVPPGTGIVHQVNLEHlgrvvhareqdgeNWLLPD-TLVGTDSHTPMIGGIGVVGW 226
Cdd:PRK12466 90 ----ENCADF--------GIRLFDVDDPRQGIVHVVAPEL-------------GLTLPGmVIVCGDSHTTTYGALGALAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 227 GVGGIEAEAAMLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANM 306
Cdd:PRK12466 145 GIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 307 APEQGSTISMFPVDEQTLEYLELTGRDPDHVDLVREYLEAQGLFGEQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPMGD 386
Cdd:PRK12466 225 AVEAGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 387 VKQSFRGllhgefedDLDDVDEDALQRWLGEGGaadaetdggvqvepeseLHPLTKRVEVDLDGetVEIGhgdvlvsait 466
Cdd:PRK12466 305 RVPDPAA--------EADPARRAAMERALDYMG-----------------LTPGTPLAGIPIDR--VFIG---------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 467 SCTNTSNPSVMIAAgllaqnAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIGNAGPLPD 546
Cdd:PRK12466 348 SCTNGRIEDLRAAA------AVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLA 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499541635 547 PIEQAIDdhdlwTTsvlsgNRNFEARIHPKIRAnYLASPPLVVAYGLAGR 596
Cdd:PRK12466 422 PGERCAS-----TT-----NRNFEGRQGPGART-HLMSPAMVAAAAVAGH 460
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
797-871 |
4.05e-18 |
|
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: 79.82 E-value: 4.05e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499541635 797 PLVVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDswESLGLDGSEVFTIHG 871
Cdd:cd00404 16 PGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE--DYLKLHTGDELDIYP 88
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
141-597 |
1.87e-17 |
|
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: 85.36 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 141 AYEKNVELEYERNAERYRAIkwaqnafENF------NVVPPGTGIVHQVNLEhlgrvvhareqdgENWLLPDTL-VGTDS 213
Cdd:cd01582 32 TLDHDVQNKSEKNLKKYKNI-------ESFakkhgiDFYPAGRGIGHQIMIE-------------EGYAFPGTLaVASDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 214 HTPMIGGIGVVGWGVGGIEAEAAMLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVE 293
Cdd:cd01582 92 HSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 294 NLTVPDRATIANMAPEQGSTISMFPVDeqtleyleltgrdpdhvdlvreyleAQGLFgeqepeytevveFDLSTVEPSLA 373
Cdd:cd01582 172 SLSVDTRLTIANMTTEWGALSGLFPTD-------------------------AKHLI------------LDLSTLSPYVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 374 GhkrpqdripmgdvkqsfrgllhgefeddlddvdedalqrwlgeggaadaetdggvqvepeselhPLTKRVEVDLDgetv 453
Cdd:cd01582 215 G----------------------------------------------------------------PNSVKVSTPLK---- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 454 EIGHGDVLVSA--ITSCTNTSNPSVMIAAGLLAQNAVEKGLD-VPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVV 530
Cdd:cd01582 227 ELEAQNIKINKayLVSCTNSRASDIAAAADVVKGKKEKNGKIpVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPL 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499541635 531 GYGCTTCIGNAGPLPDPIEQAIDdhdlwttsvlSGNRNFEARIHPKIRANYLASPPLVVAYGLAGRM 597
Cdd:cd01582 307 PAGCGPCIGLGQGLLEPGEVGIS----------ATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
240-596 |
2.30e-17 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 85.94 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 240 QPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVVDRFVEFFGPGVENLTVPDRATIANMAPEQGSTISMFPV 319
Cdd:PRK05478 156 QTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 320 DEQTLEYLEltGRD----PDHVDLVREYLEAqgLFGEQEPEYTEVVEFDLSTVEPSLAGHKRPQDRIPmgdVKQSFRgll 395
Cdd:PRK05478 236 DETTFEYLK--GRPfapkGEDWDKAVAYWKT--LKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVIS---IDGKVP--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 396 hgefeddlddvdedalqrwlgeggAADAETDGGVQVEPES-----ELHPLTKRVEVDLDgeTVEIGhgdvlvsaitSCTN 470
Cdd:PRK05478 306 ------------------------DPEDFADPVKRASAERalaymGLKPGTPITDIKID--KVFIG----------SCTN 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 471 TSNPSVMIAAgllaqnAVEKGLDVPPYVKTSLAPGSRVVTQYLEESGLLPYLEELGYAVVGYGCTTCIG-NagplPDPIE 549
Cdd:PRK05478 350 SRIEDLRAAA------AVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmN----PDKLP 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499541635 550 QaiDDHdlwttSVLSGNRNFEARIHPKIRAnYLASPPLVVAYGLAGR 596
Cdd:PRK05478 420 P--GER-----CASTSNRNFEGRQGKGGRT-HLVSPAMAAAAAITGH 458
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
707-874 |
7.90e-17 |
|
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: 78.28 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 707 TTDHISPAGPfgpdlpagqWLLDHGvepHEFNTygarrGNHevMMRGTfanVRIENEMLDDVEGGYtihhpTDEQTTVFE 786
Cdd:cd01578 7 TTDHISAAGP---------WLKYRG---HLDNI-----SNN--LLIGA---INAENGKANSVKNQV-----TGEYGPVPD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 787 ASRRYRDEGIPLVVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESlgLDGSEV 866
Cdd:cd01578 60 TARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDK--IHPDDK 137
|
....*...
gi 499541635 867 FTIHGLDD 874
Cdd:cd01578 138 VDILGLTD 145
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
702-857 |
1.47e-15 |
|
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: 73.63 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 702 LGDTVTTDHISPAG----PFGPDLPAGQWLLDHGVEPhefntygarrgnhevmmrgTFAnvrienemlddveggytihhp 777
Cdd:cd01579 2 VGDNITTDHIMPAGakvlPLRSNIPAISEFVFHRVDP-------------------TFA--------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 778 tdeqttvfeasRRYRDEGiPLVVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWE 857
Cdd:cd01579 42 -----------ERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYD 109
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
799-866 |
4.39e-13 |
|
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: 65.69 E-value: 4.39e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499541635 799 VVMAGEEFGTGSSR---DWAAKGtdlLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDSWESLGLDGSEV 866
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDEV 87
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
237-373 |
1.50e-11 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 68.50 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 237 MLGQPVTMKLPEVVGVRLEGELPEGATATDLVLHITERLREVGVV-DRFVEFFGPGVENLTVPDRATIANMAPEQGSTIS 315
Cdd:PRK11413 173 LLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSS 252
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499541635 316 MFPVDEQTLEYLELTGRDPDHVDLvreyleaqglfgeqEPE----YTEVVEFDLSTVEPSLA 373
Cdd:PRK11413 253 IWQTDEEVHNWLALHGRGQDYCEL--------------NPQpmayYDGCISVDLSAIKPMIA 300
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
790-898 |
6.33e-09 |
|
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: 56.72 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 790 RYRDEGIpLVvmAGEEFGTGSSRD---WAAKGtdlLGVRATIAESYERIYRDNLVGMGVLPLQFDDGDS---WESLGLDG 863
Cdd:COG0066 61 RYQGADI-LV--AGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVdalFAAIEANP 134
|
90 100 110
....*....|....*....|....*....|....*
gi 499541635 864 SEVFTIhglddglDVmDELTVIAerADGSTVEFPV 898
Cdd:COG0066 135 GDELTV-------DL-EAGTVTN--GTGETYPFEI 159
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
799-866 |
1.28e-08 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 55.19 E-value: 1.28e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499541635 799 VVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMGVLPlqFDDGDSWESLGlDGSEV 866
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALE-DGDEV 116
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
799-924 |
6.22e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 52.91 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 799 VVMAGEEFGTGSSRD---WAAKGTdllGVRATIAESYERIYRDNLVGMGVLPLQFDDgdsweslgldgsevfTIHGLDDG 875
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKAA---GVSAVIAKSFARIFYRNAINIGLPVLECDE---------------AVDKIEDG 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499541635 876 ldvmDELTVIAE------RADGSTVEF-PVtaqvgTPAAVTYIEHGGILHYVLRRL 924
Cdd:PRK00439 113 ----DEVEVDLEtgvitnLTTGEEYKFkPI-----PEFMLEILKAGGLIEYLKKKG 159
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
799-849 |
6.15e-06 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 48.70 E-value: 6.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499541635 799 VVMAGEEFGTGSSRDWAAKGTDLLGVRATIAESYERIYRDNLVGMG-VLPLQ 849
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
790-847 |
5.74e-05 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 45.12 E-value: 5.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499541635 790 RYRDEGIpLVvmAGEEFGTGSSRD---WAakgtdLL--GVRATIAESYERIYRDNLVGMGVLP 847
Cdd:PRK01641 64 RYQGASI-LL--AGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
175-387 |
1.91e-04 |
|
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: 44.80 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 175 PGTGIVHQVnlehLGRVvhareqdgenwLLPDTL-VGTDSHTPMIGGIGVVGWGVGGieAEAAMLGQpVTMKLPEVVGVR 253
Cdd:cd01581 91 PGDGVIHSW----LNRM-----------LLPDTVgTGGDSHTRFPIGISFPAGSGLV--AFAAATGV-MPLDMPESVLVR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 254 LEGELPEGATATDLV-----LHITERLREVGVVDRFVEFFG-----PGVENLTVPDRATIANMAPEQGSTISMFPVDEQT 323
Cdd:cd01581 153 FKGKMQPGITLRDLVnaipyYAIQQGLLTVEKKGKKNVFNGrileiEGLPDLKVEQAFELTDASAERSAAACTVRLDKEP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499541635 324 L-EYLELTGR-----------DPDHVDLVREYLEAQ-----GLFGEQEPEYTEVVEFDLSTV-EPSLAGHKRPQDRIPMG 385
Cdd:cd01581 233 ViEYLESNVVlmkimiangydDARTLLRRIIAMEEWlanppLLEPDADAEYAAVIEIDLDDIkEPILACPNDPDDVKLLS 312
|
..
gi 499541635 386 DV 387
Cdd:cd01581 313 EV 314
|
|
| |
