|
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: 1901.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 1 MLEEYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPL 80
Cdd:COG1049 1 MLEAYRKHVAERAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEATSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 81 VSPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLSRP 160
Cdd:COG1049 81 ISPEKAVELLGTMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKAGNAYAKQVLQSWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 161 PLAEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGiepdqpgvvgPIKQIEALQKKGYPLAYVGDVV 240
Cdd:COG1049 161 ELPEKITVTVFKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG----------PLKTIAELKAKGHPVAYVGDVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 241 GTGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNhE 320
Cdd:COG1049 231 GTGSSRKSATNSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVIDIYPYEGKITK-E 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 321 TDELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGFSLAQKMVGRACGVKGIRP 400
Cdd:COG1049 310 NGEVISTFELKPDTLLDEVRAGGRIPLIIGRGLTDKAREALGLPPSDVFRRPEAPADSGKGYTLAQKMVGKACGVEGVRP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 401 GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGVIH 480
Cdd:COG1049 390 GTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 481 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQ 560
Cdd:COG1049 470 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 561 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWMIAEGYGDRRT 640
Cdd:COG1049 550 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDART 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 641 LERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFRAA 720
Cdd:COG1049 630 LERRIAAMEEWLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCMTNIGHFRAA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 721 GKLLDNhKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG 800
Cdd:COG1049 710 GKLLEG-KGNLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKG 788
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2769776238 801 ANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFDQLSQYTEKADGVIFQTA 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: 1800.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 1 MLEEYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPL 80
Cdd:PRK09238 1 MLEAYRKHVAERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 81 VSPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLSRP 160
Cdd:PRK09238 81 ISPEKAVELLGTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAGNAYAKEVLESWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 161 PLAEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGiepdqpgvvgPIKQIEALQKKGYPLAYVGDVV 240
Cdd:PRK09238 161 ELPEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG----------PIKQIEELKKKGHPVAYVGDVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 241 GTGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNhE 320
Cdd:PRK09238 231 GTGSSRKSATNSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSGALPIELDVSKLNMGDVIDIYPYKGKIRN-E 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 321 TDELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGFSLAQKMVGRACGVKGIRP 400
Cdd:PRK09238 310 TGEVIATFKLKTDVLLDEVRAGGRIPLIIGRGLTTKAREALGLPPSDVFRKPKQPADSGKGFTLAQKMVGRACGVPGVRP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 401 GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGVIH 480
Cdd:PRK09238 390 GTYCEPKMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 481 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQ 560
Cdd:PRK09238 470 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 561 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWMIAEGYGDRRT 640
Cdd:PRK09238 550 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDART 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 641 LERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFRAA 720
Cdd:PRK09238 630 LERRIAAMEEWLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNIGHFRAA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 721 GKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG 800
Cdd:PRK09238 710 GKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKG 789
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 2769776238 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: 1584.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 1 MLEEYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPL 80
Cdd:TIGR00117 1 MLEEYRKHVAERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKCPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 81 VSPEKAIELLGTMQGGYNIHPLIDALD--DAKLAPIAAKALSHTLLMFDNFYDVEEKAKAgNEYAKQVMQSWADAEWFLS 158
Cdd:TIGR00117 81 ISPEKAIELLGTMQGGYNVHPLIDALDsqDANIAPIAAKALSHTLLVFDNFYDVEEKSKT-NEYAKQVMQSWADAEWFLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 159 RPPLAEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGIEPdqpgvvgpikQIEALQKKGYPLAYVGD 238
Cdd:TIGR00117 160 KPALAEKITVTVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREGIEP----------QIEALKQKGFPVAYVGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 239 VVGTGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRN 318
Cdd:TIGR00117 230 VVGTGSSRKSATNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDSGALPIEVDVSNLNMGDVIDIYPYKGEITN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 319 HEtDELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGFSLAQKMVGRACGVKGI 398
Cdd:TIGR00117 310 HE-GELLATFELKPETLLDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQPKAPAESDKGFTLAQKMVGRACGVKGI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 399 RPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGV 478
Cdd:TIGR00117 389 RPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 479 IHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAI 558
Cdd:TIGR00117 469 IHSWLNRMLLPDTVGTGGDSHTRFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAI 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 559 KQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWMIAEGYGDR 638
Cdd:TIGR00117 549 KQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDR 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 639 RTLERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFR 718
Cdd:TIGR00117 629 RTLERRIQGMEKWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSCMTNIGHFR 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 719 AAGKLLDNHkGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLG 798
Cdd:TIGR00117 709 AAGKILDAA-GQLPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVADGATVFSTSTRNFPNRMG 787
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 2769776238 799 TGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVD-TYRYLNFDQLSQYTE 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: 1574.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 2 LEEYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPLV 81
Cdd:PLN00094 71 LAEYEAHVAERAQEGIAPKPLDAKQVSELIAQLEAPKSEDADRLVDLLVNRVPPGVDEAAYVKASWLAAVAKGETRSPLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 82 SPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLSRPP 161
Cdd:PLN00094 151 SRARAVEILGTMQGGYNISPLVDALDDDELGRIAADQLSHTLLVFDAFHDVQAKAKKGNAYATQVMESWADAEWFTKKPP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 162 LAEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGIEpdqpgvvGPIKQIEALQKKGYPLAYVGDVVG 241
Cdd:PLN00094 231 VPEKITVTVFKVTGETNTDDLSPAQDAWSRPDIPLHALAMLKNPREGIQ-------GPIAQIEELKKKGHPLAYVGDVVG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 242 TGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHET 321
Cdd:PLN00094 304 TGSSRKSATNSVLWFMGDDIPNVPNKRTGGVCIGGKIAPIFFNTMEDSGALPIEMDVKNLNMGDVIDIYPYEGVVKRHGT 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 322 DELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGFSLAQKMVGRACGV-KGIRP 400
Cdd:PLN00094 384 DEVITTFSLKTPVLLDEVRAGGRIPLIIGRGLTSKAREALGLDASDVFRMPSVPESKPKGFTLAQKMVGKACGVdEGILP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 401 GAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGVIH 480
Cdd:PLN00094 464 GTYCEPRMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVVTHHTLPDFIRNRGGVSLRPGDGVIH 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 481 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQ 560
Cdd:PLN00094 544 SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIPYTAIQD 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 561 GLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWMIAEGYGDRRT 640
Cdd:PLN00094 624 GLLTVEKKGKKNVFSGRILEIEGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIEYLNSNVVMLKWMIAEGYGDRRT 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 641 LERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFRAA 720
Cdd:PLN00094 704 LERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIKEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCMTNIGHFRAA 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 721 GKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTG 800
Cdd:PLN00094 784 GKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARVAEKSTVVSTSTRNFPNRLGKG 863
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 2769776238 801 ANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFDQLSQYTEKADGV 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: 824.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 384 LAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDF 463
Cdd:cd01581 1 LAQKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTLPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 464 IMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPG 543
Cdd:cd01581 81 ISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 544 ITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSN 623
Cdd:cd01581 161 ITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYLESN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 624 IVLLKWMIAEGYGDRRTLERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKID 703
Cdd:cd01581 241 VVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGKKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 704 EVFIGSCMTNIGHFRAAGKLLDNhKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGA 783
Cdd:cd01581 321 EVFIGSCMTNIGHFRAAAKILRG-KEFKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVADGA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 2769776238 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 |
2.63e-139 |
|
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: 411.60 E-value: 2.63e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 168 VTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGiepdqpgvvgPIKQIEALQKKGYPLAYVGDVVGTGSSRK 247
Cdd:pfam06434 1 VTVFKVEGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG----------PLKTIAELKKKGHPLAYVGDVVGTGSSRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 248 SATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNhETDELLAT 327
Cdd:pfam06434 71 SATNSVLWHIGEDIPYVPNKRTGGVVIGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVITIYPYEGKITN-ENGEVIST 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2769776238 328 FELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGF 382
Cdd:pfam06434 150 FSLKPNTLLDEVRAGGRIPLIIGRGLTDKAREALGLEPSDVFTRPKQPADSGKGY 204
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
410-820 |
1.38e-130 |
|
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: 396.48 E-value: 1.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 410 SVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYP--KPVDVTTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRML 487
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGKVADPSQIACVHDHAVQleKPVNNEGHKFLSFFAALQGIAFYRPGVGIIHQIMVENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 488 -LPDTVGTGGDSHTRF---PIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQGll 563
Cdd:cd01351 81 aLPGDLLVGSDSHTTSyggLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 564 tvekkgkkniFSGRILEIEGLP--DLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWmiaegygdrrtl 641
Cdd:cd01351 159 ----------VLNRIVEFYGEGvsSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKN------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 642 erriqgmeKWLADPQLLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNI-GHFRAA 720
Cdd:cd01351 217 --------LWLAFPEELLADEGAEYDQVIEIDLSEL-EPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRySDMLAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 721 GKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQAR-VADGATVVSTSTRNFPNRLGT 799
Cdd:cd01351 288 AKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARlVADGEVGVSSGNRNFPGRLGT 367
|
410 420
....*....|....*....|..
gi 2769776238 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 |
3.77e-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: 318.24 E-value: 3.77e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 5 YRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPLVSPE 84
Cdd:pfam11791 1 YRKHVAERAALGIPPLPLDAEQTAELIELLKNPPAGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAIAKGEASSPLISPE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769776238 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 |
4.23e-76 |
|
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: 243.54 E-value: 4.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 171 FKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGIEPDqpgvvgpikqIEALQKKGYPLAYVGDVVGTGSSRKSAT 250
Cdd:cd01576 1 FKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNKREGEIVA----------IAQLKPKGHPVAYVGDVVGTGSSRKSAT 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769776238 251 NSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYP 311
Cdd:cd01576 71 NSVLWHTGKDIPFVPNKRAGGVVLGGKIAPIFFNTAEDSGALPIQLDVSVLDMGDILNIDG 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
475-800 |
4.97e-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: 158.12 E-value: 4.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 475 GDGVIHSWLNRM--LLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGIT 545
Cdd:cd01583 68 RQGICHVILPEKglTLPGMTIVGGDSHTcthgafgAFATGI----GTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 546 LRDLVhaipLYAIkqGLLTVEKKGKKNI-FSGrileiEGLPDLKVEQAFELTDASAERSA-AGctiklnkepiveyltsn 623
Cdd:cd01583 144 AKDVI----LYII--GKIGVDGATYKAMeFAG-----EAIESLSMEERMTLCNMAIEAGAkAG----------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 624 ivllkwMIAEgygDRRTLERrIQGMEKwlADPQLLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARLLSDVQGEKID 703
Cdd:cd01583 196 ------IVAP---DETTFEY-LKGRGK--AYWKELKSDEDAEYDKVVEIDASEL-EPQVAWPHSPDNVVPVSEVEGIKID 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 704 EVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVA 780
Cdd:cd01583 263 QVFIGSC-TNgrLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLA 341
|
330 340
....*....|....*....|
gi 2769776238 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 |
5.61e-39 |
|
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: 149.91 E-value: 5.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 383 SLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVTTHHTLP 461
Cdd:TIGR02086 2 TLAEKILSEKVG-RPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARvWDPEKIVIAFDHNVPPPTVEAAEMQKEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 462 DFIMNRGGVSLRPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESV 532
Cdd:TIGR02086 81 EFAKRHGIKNFDVGEGICHQILaeEGYALPGMVVVGGDSHTctsgafgAFATGM----GATDMAIALATGKTWIKVPETI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 533 LVRFKGKMQPGITLRDLVhaiplyaikqglLTVEKKGKKNIFSGRILEIEGLP--DLKVEQAFELTDASAERSAAGCTIK 610
Cdd:TIGR02086 157 RVVVEGKPEEGVTAKDVA------------LHIVGELGADGATYMAIEFFGLPieNMDMDGRLTLCNMAVEMGAKAGIIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 611 LNKEPiVEYLTSnivllkwmiaegygdRRTLERRIqgmekWLADPQlleadadAEYAAVIDIDLADIkEPILCAPNDPDD 690
Cdd:TIGR02086 225 PDEET-YEYLKK---------------RRGLEFRI-----LVPDPG-------ANYYKEIEIDLSDL-EPQVAVPHSVDN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 691 ARLLSDVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPG 768
Cdd:TIGR02086 276 VKPVSDVEGTEIDQVFIGSC-TNgrLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPG 354
|
410 420 430
....*....|....*....|....*....|.
gi 2769776238 769 CSLCMGNQARV-ADGATVVSTSTRNFPNRLG 798
Cdd:TIGR02086 355 CGPCLGAHMGVlGDGEVCLSTTNRNFKGRMG 385
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
381-804 |
2.36e-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: 148.25 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 381 GFSLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVTTHHT 459
Cdd:COG0065 2 GMTLAEKILARHAG-REVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKvWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 460 LPDFI---------MNRGGVS---------LRPGDGVIhswlnrmllpdtvgtGGDSHT-------RFPIGIsfpaGSGL 514
Cdd:COG0065 81 LREFAkefgitffdVGDPGIChvvlpeqglVLPGMTIV---------------GGDSHTcthgafgAFAFGI----GTTD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 515 VAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIplyaIkqGLLTVEkkGkkniFSGRILEI--EGLPDLKVEQA 592
Cdd:COG0065 142 VAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAI----I--GKIGAD--G----ATGKAIEFagEAIRALSMEER 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 593 FELTDASAERSA-AGctiklnkepiveyltsnivllkwMIAEgygDRRTLE----RRIQGMEKWLADPQlleadadAEYA 667
Cdd:COG0065 210 MTLCNMAIEAGAkAG-----------------------IIAP---DETTFEylkgRPFAPWRTLKSDED-------AVYD 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 668 AVIDIDLADIkEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDA 745
Cdd:COG0065 257 KEVEIDASDL-EPQVAWPHSPDNVVPVSELEGIKIDQVFIGSC-TNgrIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVY 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769776238 746 AQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVADGATVVSTSTRNFPNRLG-TGANVF 804
Cdd:COG0065 335 RQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAPGERCASTSNRNFEGRMGsPGSRTY 395
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
383-798 |
1.97e-37 |
|
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: 145.67 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 383 SLAQKMVGRACGvKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAyPKPVDVTTHHTLP 461
Cdd:TIGR01343 1 TIAEKILSKKSG-KEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKvWNPEKIVIVFDHQVP-ADTIKAAEMQKLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 462 DFIMNRGGVSL--RPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPE 530
Cdd:TIGR01343 79 REFVKKQGIKYfyDVGEGICHQVLpeKGLVKPGDLVVGADSHTctygafgAFATGM----GSTDMAYAIATGKTWFKVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 531 SVLVRFKGKMQPGITLRDLVhaipLYAIKQglltVEKKGKknifSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCT 608
Cdd:TIGR01343 155 TIRVNITGKLNPGVTAKDVI----LEVIGE----IGVDGA----TYMAMEFGGetVKNMDMEGRLTLANMAIEAGGKTGI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 609 IKLNkEPIVEYLTsnivllkwmiaegygdrrtlERRIQGMEKWLADPQlleadadAEYAAVIDIDLADIkEPILCAPNDP 688
Cdd:TIGR01343 223 IEPD-EKTIQYLK--------------------ERRKEPFRVYKSDED-------AEYAKEIEIDASQI-EPVVACPHNV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 689 DDARLLSDVQGEKIDEVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEI 766
Cdd:TIGR01343 274 DNVKPVSEVEGTEIDQVFIGSC-TNgrLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVST 352
|
410 420 430
....*....|....*....|....*....|...
gi 2769776238 767 PGCSLCMG-NQARVADGATVVSTSTRNFPNRLG 798
Cdd:TIGR01343 353 PGCGPCLGsHQGVLAPGEVCISTSNRNFKGRMG 385
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
475-798 |
2.12e-37 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 145.70 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 475 GDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGIT 545
Cdd:PRK00402 97 GEGICHQVLpeKGLVRPGDVVVGADSHTctygalgAFATGM----GSTDMAAAMATGKTWFKVPETIKVVLEGKLPPGVT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 546 LRDLVhaipLYAIkqGLLTVEkkGkkniFSGRILEI--EGLPDLKVEQAFELTDASAERSA-AGctiklnkepIVEYlts 622
Cdd:PRK00402 173 AKDVI----LHII--GDIGVD--G----ATYKALEFtgETIEALSMDERMTLANMAIEAGAkAG---------IFAP--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 623 nivllkwmiaegygDRRTLE----RRIQGMEKWLADPqlleadaDAEYAAVIDIDLADIkEPILCAPNDPDDARLLSDVQ 698
Cdd:PRK00402 229 --------------DEKTLEylkeRAGRDYKPWKSDE-------DAEYEEVYEIDLSKL-EPQVAAPHLPDNVKPVSEVE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 699 GEKIDEVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-N 775
Cdd:PRK00402 287 GTKVDQVFIGSC-TNgrLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGgH 365
|
330 340
....*....|....*....|...
gi 2769776238 776 QARVADGATVVSTSTRNFPNRLG 798
Cdd:PRK00402 366 MGVLAPGEVCLSTTNRNFKGRMG 388
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
411-804 |
3.59e-30 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 124.84 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 411 VGSQDTTGPMTrdeLKDLACLG---FSADLVMQSFCHTAaypkPVDVTTHHTLPDFI------MNRG------------- 468
Cdd:pfam00330 23 VLMHDVTSPQA---FVDLRAAGravRRPGGTPATIDHLV----PTDLVIDHAPDALDkniedeISRNkeqydflewnakk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 469 -GVSL-RPGDGVIHSWL--NRMLLPDTVGTGGDSHTR---------FPIGisfpaGSGLVAfAAATGVMPLDMPESVLVR 535
Cdd:pfam00330 96 fGIRFvPPGQGIVHQVGleYGLALPGMTIVGTDSHTTthgglgalaFGVG-----GSEAEH-VLATQPLEMKKPKVVGVK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 536 FKGKMQPGITLRDLVHAIplyaikQGLLTveKKGkkniFSGRILEI--EGLPDLKVEQAFELTDASAErsaAGCTiklnk 613
Cdd:pfam00330 170 LTGKLPPGVTAKDVILAI------IGKLG--VKG----GTGKVVEFfgPGVRSLSMEGRATICNMAIE---YGAT----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 614 epiveylTSNI----VLLKWMIAEGYGDRRTLER--RIQGMEKWLADPqlleadaDAEYAAVIDIDLADIkEPILCAPND 687
Cdd:pfam00330 230 -------AGLFppdeTTFEYLRATGRPEAPKGEAydKAVAWKTLASDP-------GAEYDKVVEIDLSTI-EPMVTGPTR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 688 PDDARLLSD-----------------------------VQGEKIDEVFIGSCmTN--IGHFRAAGKLLDN--HKGQLP-- 732
Cdd:pfam00330 295 PQDAVPLSElvpdpfadavkrkaaeraleymglgpgtpLSDGKVDIAFIGSC-TNssIEDLRAAAGLLKKavEKGLKVap 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2769776238 733 -TRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTGANVF 804
Cdd:pfam00330 374 gVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPGERCVSSSNRNFEGRQGPGGRTH 446
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
413-799 |
3.49e-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: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 413 SQDTTGPMtrdelkdlACLGFSA--------DLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGVIHS-WL 483
Cdd:cd01585 5 TQDATGTM--------AYLQFEAmgvdrvrtELSVSYVDHNTLQTDFENADDHRFLQTVAARYGIYFSRPGNGICHQvHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 484 NRMLLPDTVGTGGDSHTRFPIGISFPA--GSGL-VAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLV-HAIPLYAIK 559
Cdd:cd01585 77 ERFAVPGKTLLGSDSHTPTAGGLGMLAigAGGLdVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIlELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 560 QGLltvekkgkknifsGRILEI--EGLPDLKVEQAFELTDASAERSAagctiklnkepiveylTSNIVLlkwmiaegyGD 637
Cdd:cd01585 157 GGV-------------GKIFEYtgPGVATLSVPERATITNMGAELGA----------------TTSIFP---------SD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 638 RRTLE-RRIQGMEkwlADPQLLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCmTNIGH 716
Cdd:cd01585 199 ERTREfLAAQGRE---DDWVELAADADAEYDEEIEIDLSEL-EPLIARPHSPDNVVPVREVAGIKVDQVAIGSC-TNSSY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 717 --FRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQARVADGATVvSTSTRNF 793
Cdd:cd01585 274 edLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGmGQAPPTGGVSV-RTFNRNF 352
|
....*.
gi 2769776238 794 PNRLGT 799
Cdd:cd01585 353 EGRSGT 358
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
473-804 |
4.00e-20 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 95.60 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 473 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL-----------VAFAAATGVMPLDMPESVLVRFKGKM 540
Cdd:PRK07229 94 KPGNGICHQvHLERFAFPGKTLLGSDSHT--------PTAGGLgmlaigaggldVALAMAGGPYYLKMPKVVGVKLTGKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 541 QPGITLRDLVhaipLYAIkqGLLTVekKGKKnifsGRILEI--EGLPDLKVEQAFELTDASAERSAAgCTIklnkepive 618
Cdd:PRK07229 166 PPWVSAKDVI----LELL--RRLTV--KGGV----GKIIEYfgPGVATLSVPERATITNMGAELGAT-TSI--------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 619 yLTSNIVLLKWMIAEGygdrrtlerRIQGMEKWLADPqlleadaDAEYAAVIDIDLADIkEPILCAPNDPDDARLLSDVQ 698
Cdd:PRK07229 224 -FPSDERTREFLKAQG---------REDDWVELLADP-------DAEYDEVIEIDLSEL-EPLIAGPHSPDNVVPVSEVA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 699 GEKIDEVFIGSCmTNIGH--FRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQ 776
Cdd:PRK07229 286 GIKVDQVLIGSC-TNSSYedLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMG 364
|
330 340
....*....|....*....|....*....
gi 2769776238 777 ARVADGATVVSTSTRNFPNRLGT-GANVF 804
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRSGTkDAQVY 393
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
172-311 |
7.71e-19 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 81.75 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 172 KVTGETNTDDLSPAPdawsrpdiplhaqamlknaregiepdqpgvvgpikqiealqkkgyPLAYVGD-VVGTGSSRKSAT 250
Cdd:cd00404 1 KVAGNITTDHISPAG---------------------------------------------PGVVIGDeNYGTGSSREHAA 35
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2769776238 251 NSVLWFMGDdipnvpnkrgggLCLGGKIAPIFFNTMEDAGALPIEVDVSN----LNMGDVIDVYP 311
Cdd:cd00404 36 LELRLLGGR------------AVIAKSFARIFFRNLVDQGLLPLEFADPEdylkLHTGDELDIYP 88
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
486-801 |
4.70e-15 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 78.79 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 486 MLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAI----- 553
Cdd:PRK12466 119 LTLPGMVIVCGDSHTttygalgALAFGI----GTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALiarig 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 554 ----PLYAIKqglltvekkgkkniFSGrileiEGLPDLKVEQAFELTDASAERSAAGCTIKLNkEPIVEYLtsnivllkw 629
Cdd:PRK12466 195 adgaTGYAIE--------------FAG-----EAIRALSMEGRMTLCNMAVEAGARGGLIAPD-ETTFDYL--------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 630 miaegygdrRTLERRIQG--MEKWLADPQLLEADADAEYAAVIDIDLADIkEPILCAPNDPDDA----------RLLSD- 696
Cdd:PRK12466 246 ---------RGRPRAPKGalWDAALAYWRTLRSDADAVFDREVEIDAADI-APQVTWGTSPDQAvpitgrvpdpAAEADp 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 697 --------------------VQGEKIDEVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYY 754
Cdd:PRK12466 316 arraameraldymgltpgtpLAGIPIDRVFIGSC-TNgrIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLA 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2769776238 755 SVFGKSGARIEIPGCSLCMG-NQARVADGATVVSTSTRNFPNRLGTGA 801
Cdd:PRK12466 395 RIFIAAGFEWREPGCSMCLAmNDDVLAPGERCASTTNRNFEGRQGPGA 442
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
701-801 |
2.94e-13 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 72.85 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 701 KIDEVFIGSCmTN--IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMG-NQA 777
Cdd:PRK05478 338 KIDKVFIGSC-TNsrIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPD 416
|
90 100
....*....|....*....|....
gi 2769776238 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 |
5.15e-06 |
|
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: 49.75 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 473 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGKM 540
Cdd:cd01584 73 KPGSGIIHQIvLENYAFPGLLMIGTDSHT--------PNAGGLggiaigVGGADAVDVMAgipweLKCPKVIGVKLTGKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 541 QPGITLRDLVHAIplyaikQGLLTVeKKGkknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKLNkEPIVE 618
Cdd:cd01584 145 SGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYfgPGVDSLSCTGMGTICNMGAEIGATTSVFPYN-ERMKK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 619 YLTsnivllkwmiAEGYGDRRTLERRIQgmekwladPQLLEADADAEYAAVIDIDLADIkEPILCAPNDPDDARLLSDVQ 698
Cdd:cd01584 212 YLK----------ATGRAEIADLADEFK--------DDLLVADEGAEYDQLIEINLSEL-EPHINGPFTPDLATPVSKFK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 699 GE--------KIDEVFIGSCmTN-----IGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIE 765
Cdd:cd01584 273 EVaekngwplDLRVGLIGSC-TNssyedMGRAASIAKQALAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVL 351
|
330 340 350
....*....|....*....|....*....|....*
gi 2769776238 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 |
5.28e-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: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 474 PGDGVIHS----WLNR-----------MLLPDTVgTGGDSHTRFPIGISFpAGSGlVAFAAATGVM---PLDM--PESVL 533
Cdd:cd01586 91 PGTGIIHQvnleYLARvvftseedgdgVAYPDSV-VGTDSHTTMINGLGV-LGWG-VGGIEAEAVMlgqPISMllPEVVG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2769776238 534 VRFKGKMQPGITLRDLVhaiplyaikqglLTVEKKGKKNIFSGRILEI--EGLPDLKV 589
Cdd:cd01586 168 VKLTGKLRPGVTATDLV------------LTVTQMLRKVGVVGKFVEFfgPGVAKLSV 213
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
489-553 |
9.73e-04 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 43.00 E-value: 9.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769776238 489 PDT-VGTggDSHTRFPIGISFPA---GsGLVAFAAATGvMPLDM--PESVLVRFKGKMQPGITLRDLVHAI 553
Cdd:PRK12881 205 PDTlVGT--DSHTTMINGIGVLGwgvG-GIEAEAVMLG-QPVYMliPDVVGVELTGKLREGVTATDLVLTV 271
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
474-553 |
1.31e-03 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 42.42 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 474 PGDGVIHS----------WLNR----MLLPDT-VGTggDSHTRFPIGISFPA---GsGLVAFAAATGvMPLDM--PESVL 533
Cdd:PRK09277 176 PGTGICHQvnleylapvvWTREdgelVAYPDTlVGT--DSHTTMINGLGVLGwgvG-GIEAEAAMLG-QPSSMliPEVVG 251
|
90 100
....*....|....*....|
gi 2769776238 534 VRFKGKMQPGITLRDLVHAI 553
Cdd:PRK09277 252 VKLTGKLPEGVTATDLVLTV 271
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
474-604 |
2.10e-03 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 41.71 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 474 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAG---SGLVAFAAATGvMPLDM--PESVLVRFK 537
Cdd:PLN00070 214 PGSGIVHQvnleYLGRvvfntdgILYPDSV-VGTDSHTTMIDGLGV-AGwgvGGIEAEAAMLG-QPMSMvlPGVVGFKLS 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2769776238 538 GKMQPGITLRDLVhaiplyaikqglLTVEKKGKKNIFSGRILEI--EGLPDLKVEQAFELTDASAERSA 604
Cdd:PLN00070 291 GKLRDGVTATDLV------------LTVTQMLRKHGVVGKFVEFygEGMSELSLADRATIANMSPEYGA 347
|
|
| 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 2769776238 474 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAGSGlVAFAAATGVM---PLDM--PESVLVRFK 537
Cdd:PTZ00092 182 PGSGIVHQvnleYLARvvfnkdgLLYPDSV-VGTDSHTTMINGLGV-LGWG-VGGIEAEAVMlgqPISMvlPEVVGFKLT 258
|
90
....*....|...
gi 2769776238 538 GKMQPGITLRDLV 550
Cdd:PTZ00092 259 GKLSEHVTATDLV 271
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
469-698 |
6.96e-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: 40.09 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 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 2769776238 537 KGKMQPGITLRDLVhaiplyaikqglLTV-EKKGKKNIfSGRILEI--EGLPDLKVeqafeltdasAERSaagcTIklnk 613
Cdd:COG1048 253 TGKLPEGVTATDLV------------LTVtEMLRKKGV-VGKFVEFfgPGLASLSL----------ADRA----TI---- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769776238 614 epiveyltSNivllkwMIAEgYG--------DRRTLE------R------------RIQGMekWlADPQlleaDADAEYA 667
Cdd:COG1048 302 --------AN------MAPE-YGatcgffpvDEETLDylrltgRseeqielveayaKAQGL--W-RDPD----APEPYYS 359
|
250 260 270
....*....|....*....|....*....|.
gi 2769776238 668 AVIDIDLADIkEPILCAPNDPDDARLLSDVQ 698
Cdd:COG1048 360 DVLELDLSTV-EPSLAGPKRPQDRIPLSDLK 389
|
|
| |
