|
Name |
Accession |
Description |
Interval |
E-value |
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
1-864 |
0e+00 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 1905.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 1 MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAVAKGEAKSPL 80
Cdd:COG1049 1 MLEAYRKHVAERAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEATSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 81 LTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRP 160
Cdd:COG1049 81 ISPEKAVELLGTMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKAGNAYAKQVLQSWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 161 ALAEKLTVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGiepdqpgvvgPIKQIEALQQKGFPLAYVGDVV 240
Cdd:COG1049 161 ELPEKITVTVFKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG----------PLKTIAELKAKGHPVAYVGDVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 241 GTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNhE 320
Cdd:COG1049 231 GTGSSRKSATNSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVIDIYPYEGKITK-E 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 321 TGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRP 400
Cdd:COG1049 310 NGEVISTFELKPDTLLDEVRAGGRIPLIIGRGLTDKAREALGLPPSDVFRRPEAPADSGKGYTLAQKMVGKACGVEGVRP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 401 GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIH 480
Cdd:COG1049 390 GTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 481 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQ 560
Cdd:COG1049 470 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 561 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRT 640
Cdd:COG1049 550 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDART 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 641 LERRIQGMEKWLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAA 720
Cdd:COG1049 630 LERRIAAMEEWLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCMTNIGHFRAA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 721 GKLLDAhKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG 800
Cdd:COG1049 710 GKLLEG-KGNLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKG 788
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829376 801 ANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFNQLSQYTEKADGVIFQTA 864
Cdd:COG1049 789 ANVYLGSAELAAVCALLGRLPTVEEYMEYVKKIDPMADDIYRYLNFDQIEEYQEKADVVIPVIA 852
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
1-846 |
0e+00 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 1801.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 1 MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAVAKGEAKSPL 80
Cdd:PRK09238 1 MLEAYRKHVAERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 81 LTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRP 160
Cdd:PRK09238 81 ISPEKAVELLGTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAGNAYAKEVLESWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 161 ALAEKLTVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGiepdqpgvvgPIKQIEALQQKGFPLAYVGDVV 240
Cdd:PRK09238 161 ELPEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG----------PIKQIEELKKKGHPVAYVGDVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 241 GTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNhE 320
Cdd:PRK09238 231 GTGSSRKSATNSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSGALPIELDVSKLNMGDVIDIYPYKGKIRN-E 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 321 TGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRP 400
Cdd:PRK09238 310 TGEVIATFKLKTDVLLDEVRAGGRIPLIIGRGLTTKAREALGLPPSDVFRKPKQPADSGKGFTLAQKMVGRACGVPGVRP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 401 GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIH 480
Cdd:PRK09238 390 GTYCEPKMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 481 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQ 560
Cdd:PRK09238 470 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 561 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRT 640
Cdd:PRK09238 550 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDART 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 641 LERRIQGMEKWLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAA 720
Cdd:PRK09238 630 LERRIAAMEEWLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNIGHFRAA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 721 GKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG 800
Cdd:PRK09238 710 GKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKG 789
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 15829376 801 ANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNF 846
Cdd:PRK09238 790 ANVYLGSAELAAVCALLGRIPTVEEYQEYVAEIDATADDIYRYLNF 835
|
|
| acnB |
TIGR00117 |
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This ... |
1-854 |
0e+00 |
|
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This model describes aconitase 2, AcnB, which has weak similarity to aconitase 1. It is found almost exclusively in the Proteobacteria. [Energy metabolism, TCA cycle]
Pssm-ID: 129223 [Multi-domain] Cd Length: 844 Bit Score: 1616.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 1 MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAVAKGEAKSPL 80
Cdd:TIGR00117 1 MLEEYRKHVAERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKCPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 81 LTPEKAIELLGTMQGGYNIHPLIDALD--DAKLAPIAAKALSHTLLMFDNFYDVEEKAKAgNEYAKQVMQSWADAEWFLN 158
Cdd:TIGR00117 81 ISPEKAIELLGTMQGGYNVHPLIDALDsqDANIAPIAAKALSHTLLVFDNFYDVEEKSKT-NEYAKQVMQSWADAEWFLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 159 RPALAEKLTVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGIEPdqpgvvgpikQIEALQQKGFPLAYVGD 238
Cdd:TIGR00117 160 KPALAEKITVTVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREGIEP----------QIEALKQKGFPVAYVGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 239 VVGTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRN 318
Cdd:TIGR00117 230 VVGTGSSRKSATNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDSGALPIEVDVSNLNMGDVIDIYPYKGEITN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 319 HEtGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGI 398
Cdd:TIGR00117 310 HE-GELLATFELKPETLLDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQPKAPAESDKGFTLAQKMVGRACGVKGI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 399 RPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGV 478
Cdd:TIGR00117 389 RPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 479 IHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAI 558
Cdd:TIGR00117 469 IHSWLNRMLLPDTVGTGGDSHTRFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAI 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 559 KQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDR 638
Cdd:TIGR00117 549 KQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDR 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 639 RTLERRIQGMEKWLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFR 718
Cdd:TIGR00117 629 RTLERRIQGMEKWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSCMTNIGHFR 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 719 AAGKLLDAHkGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLG 798
Cdd:TIGR00117 709 AAGKILDAA-GQLPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVADGATVFSTSTRNFPNRMG 787
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829376 799 TGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVD-TYRYLNFNQLSQYTE 854
Cdd:TIGR00117 788 TGANVYLGSAELAAVCALLGKIPTPEEYQTYVSEKDKTAVDkTYRYLNFNQLSNFTE 844
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
2-859 |
0e+00 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 1564.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 2 LEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAVAKGEAKSPLL 81
Cdd:PLN00094 71 LAEYEAHVAERAQEGIAPKPLDAKQVSELIAQLEAPKSEDADRLVDLLVNRVPPGVDEAAYVKASWLAAVAKGETRSPLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 82 TPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRPA 161
Cdd:PLN00094 151 SRARAVEILGTMQGGYNISPLVDALDDDELGRIAADQLSHTLLVFDAFHDVQAKAKKGNAYATQVMESWADAEWFTKKPP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 162 LAEKLTVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGIEpdqpgvvGPIKQIEALQQKGFPLAYVGDVVG 241
Cdd:PLN00094 231 VPEKITVTVFKVTGETNTDDLSPAQDAWSRPDIPLHALAMLKNPREGIQ-------GPIAQIEELKKKGHPLAYVGDVVG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 242 TGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHET 321
Cdd:PLN00094 304 TGSSRKSATNSVLWFMGDDIPNVPNKRTGGVCIGGKIAPIFFNTMEDSGALPIEMDVKNLNMGDVIDIYPYEGVVKRHGT 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 322 GELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGV-KGIRP 400
Cdd:PLN00094 384 DEVITTFSLKTPVLLDEVRAGGRIPLIIGRGLTSKAREALGLDASDVFRMPSVPESKPKGFTLAQKMVGKACGVdEGILP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 401 GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIH 480
Cdd:PLN00094 464 GTYCEPRMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVVTHHTLPDFIRNRGGVSLRPGDGVIH 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 481 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQ 560
Cdd:PLN00094 544 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIPYTAIQD 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 561 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRT 640
Cdd:PLN00094 624 GLLTVEKKGKKNVFSGRILEIEGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIEYLNSNVVMLKWMIAEGYGDRRT 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 641 LERRIQGMEKWLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAA 720
Cdd:PLN00094 704 LERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIKEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCMTNIGHFRAA 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 721 GKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG 800
Cdd:PLN00094 784 GKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARVAEKSTVVSTSTRNFPNRLGKG 863
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829376 801 ANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFNQLSQYTEKADGV 859
Cdd:PLN00094 864 ANVYLASAELAAVAAILGRLPTVEEYLSYMEKLDATASDTYRYLNFDELPEYVESAEKV 922
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
384-820 |
0e+00 |
|
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: 827.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 384 LAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDF 463
Cdd:cd01581 1 LAQKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTLPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 464 IMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPG 543
Cdd:cd01581 81 ISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 544 ITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSN 623
Cdd:cd01581 161 ITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYLESN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 624 IVLLKWMIAEGYGDRRTLERRIQGMEKWLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKID 703
Cdd:cd01581 241 VVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGKKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 704 EVFIGSCMTNIGHFRAAGKLLDAhKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGA 783
Cdd:cd01581 321 EVFIGSCMTNIGHFRAAAKILRG-KEFKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVADGA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 15829376 784 TVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKL 820
Cdd:cd01581 400 TVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| Aconitase_2_N |
pfam06434 |
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several ... |
168-382 |
2.36e-141 |
|
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several bacterial Aconitate hydratase 2 proteins and is found in conjunction with pfam00330.
Pssm-ID: 461912 [Multi-domain] Cd Length: 204 Bit Score: 416.61 E-value: 2.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 168 VTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGiepdqpgvvgPIKQIEALQQKGFPLAYVGDVVGTGSSRK 247
Cdd:pfam06434 1 VTVFKVEGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG----------PLKTIAELKKKGHPLAYVGDVVGTGSSRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 248 SATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNhETGELLAT 327
Cdd:pfam06434 71 SATNSVLWHIGEDIPYVPNKRTGGVVIGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVITIYPYEGKITN-ENGEVIST 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829376 328 FELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGF 382
Cdd:pfam06434 150 FSLKPNTLLDEVRAGGRIPLIIGRGLTDKAREALGLEPSDVFTRPKQPADSGKGY 204
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
410-820 |
6.79e-134 |
|
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: 404.96 E-value: 6.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 410 SVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYP--KPVDVNTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRML 487
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGKVADPSQIACVHDHAVQleKPVNNEGHKFLSFFAALQGIAFYRPGVGIIHQIMVENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 488 -LPDTVGTGGDSHTRF---PIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQGll 563
Cdd:cd01351 81 aLPGDLLVGSDSHTTSyggLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 564 tvekkgkkniFSGRILEIEGLP--DLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWmiaegygdrrtl 641
Cdd:cd01351 159 ----------VLNRIVEFYGEGvsSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKN------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 642 erriqgmeKWLANPELLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNI-GHFRAA 720
Cdd:cd01351 217 --------LWLAFPEELLADEGAEYDQVIEIDLSEL-EPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRySDMLAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 721 GKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQAR-VADGATVVSTSTRNFPNRLGT 799
Cdd:cd01351 288 AKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARlVADGEVGVSSGNRNFPGRLGT 367
|
410 420
....*....|....*....|..
gi 15829376 800 G-ANVFLASAELAAVAALIGKL 820
Cdd:cd01351 368 YeRHVYLASPELAAATAIAGKI 389
|
|
| Aconitase_B_N |
pfam11791 |
Aconitate B N-terminal domain; This family represents the N-terminal domain of Aconitase B. |
5-156 |
6.33e-104 |
|
Aconitate B N-terminal domain; This family represents the N-terminal domain of Aconitase B.
Pssm-ID: 463349 [Multi-domain] Cd Length: 151 Bit Score: 317.47 E-value: 6.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 5 YRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAVAKGEAKSPLLTPE 84
Cdd:pfam11791 1 YRKHVAERAALGIPPLPLDAEQTAELIELLKNPPAGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAIAKGEASSPLISPE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829376 85 KAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAgNEYAKQVMQSWADAEWF 156
Cdd:pfam11791 81 EAVELLGTMLGGYNVAPLIDLLDDAELAAEAAEALKKTLLVYDAFHDVAELAKA-NAYAKEVLESWANAEWF 151
|
|
| AcnB_Swivel |
cd01576 |
Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of ... |
171-311 |
1.85e-77 |
|
Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of the TCA cycle. It catalyses the formation of cis-aconitate from citrate. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The domain structure of Aconitase B is different from other Aconitases in that he swivel domain that is found at N-terminus of B family is normally found at C-terminus for other Aconitases. In most members of the family, there is also a HEAT domain before domain 4, which is believed to play a role in protein-protein interaction.
Pssm-ID: 238808 [Multi-domain] Cd Length: 131 Bit Score: 247.00 E-value: 1.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 171 FKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGIEPDqpgvvgpikqIEALQQKGFPLAYVGDVVGTGSSRKSAT 250
Cdd:cd01576 1 FKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNKREGEIVA----------IAQLKPKGHPVAYVGDVVGTGSSRKSAT 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829376 251 NSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYP 311
Cdd:cd01576 71 NSVLWHTGKDIPFVPNKRAGGVVLGGKIAPIFFNTAEDSGALPIQLDVSVLDMGDILNIDG 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
475-800 |
2.72e-42 |
|
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: 158.89 E-value: 2.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 475 GDGVIHSWLNRM--LLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGIT 545
Cdd:cd01583 68 RQGICHVILPEKglTLPGMTIVGGDSHTcthgafgAFATGI----GTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 546 LRDLVhaipLYAIkqGLLTVEKKGKKNI-FSGrileiEGLPDLKVEQAFELTDASAERSA-AGctiklnkepiieylnsn 623
Cdd:cd01583 144 AKDVI----LYII--GKIGVDGATYKAMeFAG-----EAIESLSMEERMTLCNMAIEAGAkAG----------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 624 ivllkwMIAEgygDRRTLERrIQGMEKwlANPELLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARPLSAVQGEKID 703
Cdd:cd01583 196 ------IVAP---DETTFEY-LKGRGK--AYWKELKSDEDAEYDKVVEIDASEL-EPQVAWPHSPDNVVPVSEVEGIKID 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 704 EVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVA 780
Cdd:cd01583 263 QVFIGSC-TNgrLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLA 341
|
330 340
....*....|....*....|
gi 15829376 781 DGATVVSTSTRNFPNRLGTG 800
Cdd:cd01583 342 PGERCVSTSNRNFKGRMGSP 361
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
383-798 |
8.26e-40 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273960 Cd Length: 413 Bit Score: 152.61 E-value: 8.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 383 SLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVNTHHTLP 461
Cdd:TIGR02086 2 TLAEKILSEKVG-RPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARvWDPEKIVIAFDHNVPPPTVEAAEMQKEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 462 DFIMNRGGVSLRPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESV 532
Cdd:TIGR02086 81 EFAKRHGIKNFDVGEGICHQILaeEGYALPGMVVVGGDSHTctsgafgAFATGM----GATDMAIALATGKTWIKVPETI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 533 LVRFKGKMQPGITLRDLVhaiplyaikqglLTVEKKGKKNIFSGRILEIEGLP--DLKVEQAFELTDASAERSAAGCTIK 610
Cdd:TIGR02086 157 RVVVEGKPEEGVTAKDVA------------LHIVGELGADGATYMAIEFFGLPieNMDMDGRLTLCNMAVEMGAKAGIIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 611 LNKEPIiEYLNSnivllkwmiaegygdRRTLERRIqgmekwlanpelLEADADAEYAAVIDIDLADIkEPILCAPNDPDD 690
Cdd:TIGR02086 225 PDEETY-EYLKK---------------RRGLEFRI------------LVPDPGANYYKEIEIDLSDL-EPQVAVPHSVDN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 691 ARPLSAVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPG 768
Cdd:TIGR02086 276 VKPVSDVEGTEIDQVFIGSC-TNgrLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPG 354
|
410 420 430
....*....|....*....|....*....|.
gi 15829376 769 CSLCMGNQARV-ADGATVVSTSTRNFPNRLG 798
Cdd:TIGR02086 355 CGPCLGAHMGVlGDGEVCLSTTNRNFKGRMG 385
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
381-804 |
1.66e-38 |
|
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: 148.64 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 381 GFSLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVNTHHT 459
Cdd:COG0065 2 GMTLAEKILARHAG-REVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKvWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 460 LPDFI---------MNRGGVS---------LRPGDGVIhswlnrmllpdtvgtGGDSHT-------RFPIGIsfpaGSGL 514
Cdd:COG0065 81 LREFAkefgitffdVGDPGIChvvlpeqglVLPGMTIV---------------GGDSHTcthgafgAFAFGI----GTTD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 515 VAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIplyaIkqGLLTVEkkGkkniFSGRILEI--EGLPDLKVEQA 592
Cdd:COG0065 142 VAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAI----I--GKIGAD--G----ATGKAIEFagEAIRALSMEER 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 593 FELTDASAERSA-AGctiklnkepIIEYlnsnivllkwmiaegygDRRTLErriqgmekWL-----ANPELLEADADAEY 666
Cdd:COG0065 210 MTLCNMAIEAGAkAG---------IIAP-----------------DETTFE--------YLkgrpfAPWRTLKSDEDAVY 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 667 AAVIDIDLADIkEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMD 744
Cdd:COG0065 256 DKEVEIDASDL-EPQVAWPHSPDNVVPVSELEGIKIDQVFIGSC-TNgrIEDLRAAAEILKGRKVAPGVRAIVVPGSQEV 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829376 745 AAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVADGATVVSTSTRNFPNRLG-TGANVF 804
Cdd:COG0065 334 YRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAPGERCASTSNRNFEGRMGsPGSRTY 395
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
383-798 |
3.07e-38 |
|
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: 147.98 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 383 SLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVNTHHTLP 461
Cdd:TIGR01343 1 TIAEKILSKKSG-KEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKvWNPEKIVIVFDHQVPADTIKAAEMQKLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 462 DFIMNRGGVSL-RPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPES 531
Cdd:TIGR01343 80 EFVKKQGIKYFyDVGEGICHQVLpeKGLVKPGDLVVGADSHTctygafgAFATGM----GSTDMAYAIATGKTWFKVPET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 532 VLVRFKGKMQPGITLRDLVhaipLYAIKQglltVEKKGKknifSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTI 609
Cdd:TIGR01343 156 IRVNITGKLNPGVTAKDVI----LEVIGE----IGVDGA----TYMAMEFGGetVKNMDMEGRLTLANMAIEAGGKTGII 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 610 KLNkEPIIEYLNSnivllkwmiaegYGDRRtlERRIQGMEKwlANPElleadadaeyaAVIDIDLADIkEPILCAPNDPD 689
Cdd:TIGR01343 224 EPD-EKTIQYLKE------------RRKEP--FRVYKSDED--AEYA-----------KEIEIDASQI-EPVVACPHNVD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 690 DARPLSAVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIP 767
Cdd:TIGR01343 275 NVKPVSEVEGTEIDQVFIGSC-TNgrLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTP 353
|
410 420 430
....*....|....*....|....*....|..
gi 15829376 768 GCSLCMG-NQARVADGATVVSTSTRNFPNRLG 798
Cdd:TIGR01343 354 GCGPCLGsHQGVLAPGEVCISTSNRNFKGRMG 385
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
381-798 |
3.06e-37 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 144.93 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 381 GFSLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLaclG----FSADLVMQSFCHtaAYPKPvDVNT 456
Cdd:PRK00402 2 GMTLAEKILARHSG-RDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKI---GgdkvFDPSKIVIVFDH--FVPAK-DIKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 457 H------------HTLPDFIMNRGGVS---------LRPGDGVIhswlnrmllpdtvgtGGDSHT-------RFPIGIsf 508
Cdd:PRK00402 75 AeqqkilrefakeQGIPNFFDVGEGIChqvlpekglVRPGDVVV---------------GADSHTctygalgAFATGM-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 509 paGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVhaipLYAIkqGLLTVEkkGkkniFSGRILEI--EGLPD 586
Cdd:PRK00402 138 --GSTDMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVI----LHII--GDIGVD--G----ATYKALEFtgETIEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 587 LKVEQAFELTDASAERSA-AGctiklnkepIIEYlnsnivllkwmiaegygDRRTLE----RRIQGMEKWLANPEllead 661
Cdd:PRK00402 204 LSMDERMTLANMAIEAGAkAG---------IFAP-----------------DEKTLEylkeRAGRDYKPWKSDED----- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 662 adAEYAAVIDIDLADIkEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAP 739
Cdd:PRK00402 253 --AEYEEVYEIDLSKL-EPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSC-TNgrLEDLRIAAEILKGRKVAPGVRLIVIP 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 740 PTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVADGATVVSTSTRNFPNRLG 798
Cdd:PRK00402 329 ASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGgHMGVLAPGEVCLSTTNRNFKGRMG 388
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
411-804 |
1.54e-30 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 126.00 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 411 VGSQDTTGPMTrdeLKDLACLG---FSADLVMQSFCHTAaypkPVDVNTHHTLPDFI------MNRG------------- 468
Cdd:pfam00330 23 VLMHDVTSPQA---FVDLRAAGravRRPGGTPATIDHLV----PTDLVIDHAPDALDkniedeISRNkeqydflewnakk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 469 -GVSL-RPGDGVIHSWL--NRMLLPDTVGTGGDSHTR---------FPIGisfpaGSGLVAfAAATGVMPLDMPESVLVR 535
Cdd:pfam00330 96 fGIRFvPPGQGIVHQVGleYGLALPGMTIVGTDSHTTthgglgalaFGVG-----GSEAEH-VLATQPLEMKKPKVVGVK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 536 FKGKMQPGITLRDLVHAIplyaikQGLLTveKKGkkniFSGRILEI--EGLPDLKVEQAFELTDASAErsaAGCTIKlnk 613
Cdd:pfam00330 170 LTGKLPPGVTAKDVILAI------IGKLG--VKG----GTGKVVEFfgPGVRSLSMEGRATICNMAIE---YGATAG--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 614 epIIEYLNsniVLLKWMIAEGygdrRTLERRIqgmEKWLANPELLEADADAEYA--AVIDIDLADIkEPILCAPNDPDDA 691
Cdd:pfam00330 232 --LFPPDE---TTFEYLRATG----RPEAPKG---EAYDKAVAWKTLASDPGAEydKVVEIDLSTI-EPMVTGPTRPQDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 692 RPLSA-----------------------------VQGEKIDEVFIGSCmTN--IGHFRAAGKLLD--AHKGQLP---TRL 735
Cdd:pfam00330 299 VPLSElvpdpfadavkrkaaeraleymglgpgtpLSDGKVDIAFIGSC-TNssIEDLRAAAGLLKkaVEKGLKVapgVKA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829376 736 WVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTGANVF 804
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPGERCVSSSNRNFEGRQGPGGRTH 446
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
413-799 |
3.59e-27 |
|
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: 114.47 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 413 SQDTTGPMtrdelkdlACLGFSA--------DLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIHS-WL 483
Cdd:cd01585 5 TQDATGTM--------AYLQFEAmgvdrvrtELSVSYVDHNTLQTDFENADDHRFLQTVAARYGIYFSRPGNGICHQvHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 484 NRMLLPDTVGTGGDSHTRFPIGISFPA--GSGL-VAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLV-HAIPLYAIK 559
Cdd:cd01585 77 ERFAVPGKTLLGSDSHTPTAGGLGMLAigAGGLdVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIlELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 560 QGLltvekkgkknifsGRILEI--EGLPDLKVEQAFELTDASAErsaAGCTIKLnkepiieyLNSNIVLLKWMIAEGYGD 637
Cdd:cd01585 157 GGV-------------GKIFEYtgPGVATLSVPERATITNMGAE---LGATTSI--------FPSDERTREFLAAQGRED 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 638 rrtlerriqgmeKWLAnpelLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCmTNIGH- 716
Cdd:cd01585 213 ------------DWVE----LAADADAEYDEEIEIDLSEL-EPLIARPHSPDNVVPVREVAGIKVDQVAIGSC-TNSSYe 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 717 -FRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVADGATVvSTSTRNFP 794
Cdd:cd01585 275 dLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGmGQAPPTGGVSV-RTFNRNFE 353
|
....*
gi 15829376 795 NRLGT 799
Cdd:cd01585 354 GRSGT 358
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
414-804 |
3.20e-21 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 99.07 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 414 QDTTGPMtrdelkdlACLGFSA--------DLvmqsfchTAAYpkpVDVNTHHTLP------DFIM---NRGGVSL-RPG 475
Cdd:PRK07229 35 QDATGTM--------AYLQFEAmgldrvktEL-------SVQY---VDHNLLQADFenaddhRFLQsvaAKYGIYFsKPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 476 DGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL-----------VAFAAATGVMPLDMPESVLVRFKGKMQPG 543
Cdd:PRK07229 97 NGICHQvHLERFAFPGKTLLGSDSHT--------PTAGGLgmlaigaggldVALAMAGGPYYLKMPKVVGVKLTGKLPPW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 544 ITLRDLVhaipLYAIkqGLLTVekKGKKnifsGRILEI--EGLPDLKVeqafeltdasAERSaagcTIklnkepiieyln 621
Cdd:PRK07229 169 VSAKDVI----LELL--RRLTV--KGGV----GKIIEYfgPGVATLSV----------PERA----TI------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 622 SNivllkwMIAE--------GYgDRRTLE-RRIQGMEK----WLANPElleadadAEYAAVIDIDLADIkEPILCAPNDP 688
Cdd:PRK07229 211 TN------MGAElgattsifPS-DERTREfLKAQGREDdwveLLADPD-------AEYDEVIEIDLSEL-EPLIAGPHSP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 689 DDARPLSAVQGEKIDEVFIGSCmTNIGH--FRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEI 766
Cdd:PRK07229 276 DNVVPVSEVAGIKVDQVLIGSC-TNSSYedLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILE 354
|
410 420 430
....*....|....*....|....*....|....*....
gi 15829376 767 PGCSLCMGNQARVADGATVVSTSTRNFPNRLGT-GANVF 804
Cdd:PRK07229 355 NACGPCIGMGQAPATGNVSLRTFNRNFPGRSGTkDAQVY 393
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
172-311 |
1.21e-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: 81.36 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 172 KVTGETNTDDLSPAPdawsrpdiplhalamlknaregiepdqpgvvgpikqiealqqkgfPLAYVGD-VVGTGSSRKSAT 250
Cdd:cd00404 1 KVAGNITTDHISPAG---------------------------------------------PGVVIGDeNYGTGSSREHAA 35
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829376 251 NSVLWFMGDdiphvpnkrgggLCLGGKIAPIFFNTMEDAGALPIEVDVSN----LNMGDVIDVYP 311
Cdd:cd00404 36 LELRLLGGR------------AVIAKSFARIFFRNLVDQGLLPLEFADPEdylkLHTGDELDIYP 88
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
486-801 |
7.30e-16 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 81.10 E-value: 7.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 486 MLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAI----- 553
Cdd:PRK12466 119 LTLPGMVIVCGDSHTttygalgALAFGI----GTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALiarig 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 554 ----PLYAIKqglltvekkgkkniFSGrileiEGLPDLKVEQAFELTDASAERSAAGCTIKLNkEPIIEYLnsnivllkw 629
Cdd:PRK12466 195 adgaTGYAIE--------------FAG-----EAIRALSMEGRMTLCNMAVEAGARGGLIAPD-ETTFDYL--------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 630 miaegygdrRTLERRIQG--MEKWLANPELLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARPLSA----------- 696
Cdd:PRK12466 246 ---------RGRPRAPKGalWDAALAYWRTLRSDADAVFDREVEIDAADI-APQVTWGTSPDQAVPITGrvpdpaaeadp 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 697 --------------------VQGEKIDEVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYY 754
Cdd:PRK12466 316 arraameraldymgltpgtpLAGIPIDRVFIGSC-TNgrIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLA 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15829376 755 SVFGKSGARIEIPGCSLCMG-NQARVADGATVVSTSTRNFPNRLGTGA 801
Cdd:PRK12466 395 RIFIAAGFEWREPGCSMCLAmNDDVLAPGERCASTTNRNFEGRQGPGA 442
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
701-801 |
5.99e-13 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 72.07 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 701 KIDEVFIGSCmTN--IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQA 777
Cdd:PRK05478 338 KIDKVFIGSC-TNsrIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPD 416
|
90 100
....*....|....*....|....
gi 15829376 778 RVADGATVVSTSTRNFPNRLGTGA 801
Cdd:PRK05478 417 KLPPGERCASTSNRNFEGRQGKGG 440
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
473-796 |
1.29e-07 |
|
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: 54.75 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 473 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGKM 540
Cdd:cd01584 73 KPGSGIIHQIvLENYAFPGLLMIGTDSHT--------PNAGGLggiaigVGGADAVDVMAgipweLKCPKVIGVKLTGKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 541 QPGITLRDLVHAIplyaikQGLLTVeKKGkknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKLNkEPIIE 618
Cdd:cd01584 145 SGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYfgPGVDSLSCTGMGTICNMGAEIGATTSVFPYN-ERMKK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 619 YLNsnivllkwmiAEGYGDRRTLERRIQgmekwlanPELLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARPLSAVQ 698
Cdd:cd01584 212 YLK----------ATGRAEIADLADEFK--------DDLLVADEGAEYDQLIEINLSEL-EPHINGPFTPDLATPVSKFK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 699 GE--------KIDEVFIGSCmTN-----IGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIE 765
Cdd:cd01584 273 EVaekngwplDLRVGLIGSC-TNssyedMGRAASIAKQALAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVL 351
|
330 340 350
....*....|....*....|....*....|....*
gi 15829376 766 IPGCSLCMGNQARV----ADGATVVSTSTRNFPNR 796
Cdd:cd01584 352 ANACGPCIGQWDRKdikkGEKNTIVTSYNRNFTGR 386
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
474-589 |
5.23e-05 |
|
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: 46.53 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 474 PGDGVIHS----WLNR-----------MLLPDTVgTGGDSHTRFPIGISFpAGSGlVAFAAATGVM---PLDM--PESVL 533
Cdd:cd01586 91 PGTGIIHQvnleYLARvvftseedgdgVAYPDSV-VGTDSHTTMINGLGV-LGWG-VGGIEAEAVMlgqPISMllPEVVG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829376 534 VRFKGKMQPGITLRDLVhaiplyaikqglLTVEKKGKKNIFSGRILEI--EGLPDLKV 589
Cdd:cd01586 168 VKLTGKLRPGVTATDLV------------LTVTQMLRKVGVVGKFVEFfgPGVAKLSV 213
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
489-553 |
9.64e-04 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 43.00 E-value: 9.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829376 489 PDT-VGTggDSHTRFPIGISFPA---GsGLVAFAAATGvMPLDM--PESVLVRFKGKMQPGITLRDLVHAI 553
Cdd:PRK12881 205 PDTlVGT--DSHTTMINGIGVLGwgvG-GIEAEAVMLG-QPVYMliPDVVGVELTGKLREGVTATDLVLTV 271
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
474-553 |
1.29e-03 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 42.42 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 474 PGDGVIHS----------WLNR----MLLPDT-VGTggDSHTRFPIGISFPA---GsGLVAFAAATGvMPLDM--PESVL 533
Cdd:PRK09277 176 PGTGICHQvnleylapvvWTREdgelVAYPDTlVGT--DSHTTMINGLGVLGwgvG-GIEAEAAMLG-QPSSMliPEVVG 251
|
90 100
....*....|....*....|
gi 15829376 534 VRFKGKMQPGITLRDLVHAI 553
Cdd:PRK09277 252 VKLTGKLPEGVTATDLVLTV 271
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
474-604 |
2.06e-03 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 41.71 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 474 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAG---SGLVAFAAATGvMPLDM--PESVLVRFK 537
Cdd:PLN00070 214 PGSGIVHQvnleYLGRvvfntdgILYPDSV-VGTDSHTTMIDGLGV-AGwgvGGIEAEAAMLG-QPMSMvlPGVVGFKLS 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829376 538 GKMQPGITLRDLVhaiplyaikqglLTVEKKGKKNIFSGRILEI--EGLPDLKVEQAFELTDASAERSA 604
Cdd:PLN00070 291 GKLRDGVTATDLV------------LTVTQMLRKHGVVGKFVEFygEGMSELSLADRATIANMSPEYGA 347
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
469-698 |
3.41e-03 |
|
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: 41.24 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 469 GVSLRPGDGVihswlnRMLLPDT-VGTggDSHTrfP---------IGIsfpaGsGLVAFAAATGvMPLDM--PESVLVRF 536
Cdd:COG1048 189 VVWTREEDGE------TVAYPDTlVGT--DSHT--TminglgvlgWGV----G-GIEAEAAMLG-QPVSMliPEVVGVKL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 537 KGKMQPGITLRDLVhaiplyaikqglLTV-EKKGKKNIfSGRILEI--EGLPDLKVeqafeltdasAERSaagcTIklnk 613
Cdd:COG1048 253 TGKLPEGVTATDLV------------LTVtEMLRKKGV-VGKFVEFfgPGLASLSL----------ADRA----TI---- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 614 epiieylnSNivllkwMIAEgYG--------DRRTLE------R------------RIQGMekWlANPElleaDADAEYA 667
Cdd:COG1048 302 --------AN------MAPE-YGatcgffpvDEETLDylrltgRseeqielveayaKAQGL--W-RDPD----APEPYYS 359
|
250 260 270
....*....|....*....|....*....|.
gi 15829376 668 AVIDIDLADIkEPILCAPNDPDDARPLSAVQ 698
Cdd:COG1048 360 DVLELDLSTV-EPSLAGPKRPQDRIPLSDLK 389
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
474-550 |
3.57e-03 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 41.15 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829376 474 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAGSGlVAFAAATGVM---PLDM--PESVLVRFK 537
Cdd:PTZ00092 182 PGSGIVHQvnleYLARvvfnkdgLLYPDSV-VGTDSHTTMINGLGV-LGWG-VGGIEAEAVMlgqPISMvlPEVVGFKLT 258
|
90
....*....|...
gi 15829376 538 GKMQPGITLRDLV 550
Cdd:PTZ00092 259 GKLSEHVTATDLV 271
|
|
| |
