|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
1-901 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1559.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 1 MSGSGANPFAQFQESFTQDGNvYKYFDLPSI-DSKYESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGWtpslkQETS- 78
Cdd:PTZ00092 8 MSSSRPNPFEKVLKTLKDGGS-YKYYSLNELhDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNW-----EENSk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 79 -DVEVSFKPARVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNK 157
Cdd:PTZ00092 82 kQIEIPFKPARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 158 ERFTFLKWGARAFDNMLIVPPGSGIVHQVNLEYLARVVFESDSsadgskILYPDSVVGTDSHTTMINGLGVLGWGVGGIE 237
Cdd:PTZ00092 162 ERFEFLKWGSKAFKNLLIVPPGSGIVHQVNLEYLARVVFNKDG------LLYPDSVVGTDSHTTMINGLGVLGWGVGGIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 238 AEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGA 317
Cdd:PTZ00092 236 AEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 318 TVGYFPIDENTLSYMRQTNRSEKKIDIIRKYLKATRQLRDYSlvdQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSM 397
Cdd:PTZ00092 316 TMGFFPIDEKTLDYLKQTGRSEEKVELIEKYLKANGLFRTYA---EQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 398 CEDFKSCLISPVGFKGFAIPPSALAASGEFQWDdGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSIL 477
Cdd:PTZ00092 393 KKDFTACLSAPVGFKGFGIPEEKHEKKVKFTYK-GKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 478 PYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHP 557
Cdd:PTZ00092 472 PYIKTSLSPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHP 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 558 NTRANYLASPLLVIAYAIAGRVDIDFEIEPLGVDSNGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQ 637
Cdd:PTZ00092 552 LTRANYLASPPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 638 TLEVSDSKLYPWSEISTYIKLPPFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPR 717
Cdd:PTZ00092 632 ELQVPKGKLYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERK 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 718 DFNSYGSRRGNDAVMARGTFANIRLVNKLASKTGPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAA 797
Cdd:PTZ00092 712 DFNTYGARRGNDEVMVRGTFANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAA 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 798 KGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVLPEGELKPGQRIQVDAD-GNVFETTL 876
Cdd:PTZ00092 792 KGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQDVTVKTDtGKTFDTIL 871
|
890 900
....*....|....*....|....*
gi 17137564 877 RFDTEVDITYYKNGGILNYMIRKML 901
Cdd:PTZ00092 872 RIDTEVEVEYFKHGGILQYVLRKLV 896
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
4-901 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1472.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 4 SGANPFaQFQESFTQDGNVYKYFDLPSIDSK----YESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGWTPSLKqetSD 79
Cdd:PRK09277 2 SSTDSF-KARKTLEVGGKSYDYYSLRALEAKglgdISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAK---PD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 80 VEVSFKPARVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNKER 159
Cdd:PRK09277 78 REIPFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 160 FTFLKWGARAFDNMLIVPPGSGIVHQVNLEYLARVVFesdSSADGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAE 239
Cdd:PRK09277 158 YQFLKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVW---TREDGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 240 AVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATV 319
Cdd:PRK09277 235 AAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 320 GYFPIDENTLSYMRQTNRSEKKIDIIRKYLKATRQLRDyslVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSMCE 399
Cdd:PRK09277 315 GFFPIDEETLDYLRLTGRDEEQVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 400 DFKSCLisPVGFKGFAIPPSALaasgefqwddGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSILPY 479
Cdd:PRK09277 392 AFAKSA--ELGVQGFGLDEAEE----------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPW 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 480 IKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHPNT 559
Cdd:PRK09277 460 VKTSLAPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 560 RANYLASPLLVIAYAIAGRVDIDFEIEPLGVDSNGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQTL 639
Cdd:PRK09277 540 KANYLASPPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAI 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 640 EVSDSKLYPWSEISTYIKLPPFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPRDF 719
Cdd:PRK09277 620 EVPEGPLYDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDF 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 720 NSYGSRRGNDAVMARGTFANIRLVNKLASKT-GPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAAK 798
Cdd:PRK09277 700 NSYGSRRGNHEVMMRGTFANIRIRNEMVPGVeGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAK 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 799 GPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVLPEgELKPGQRIQV---DADGNV--FE 873
Cdd:PRK09277 780 GTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLE-DLKPGATVTVvitRADGEVveFP 858
|
890 900
....*....|....*....|....*...
gi 17137564 874 TTLRFDTEVDITYYKNGGILNYMIRKML 901
Cdd:PRK09277 859 VLCRIDTAVEVDYYRNGGILQYVLRDLL 886
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
7-901 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 1461.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 7 NPFaQFQESFTQDGNVYKYFDLPSIDSK---YESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGWTPslkQETSDVEVS 83
Cdd:COG1048 3 DSF-KARKTLTVGGKPYTYYSLPALEEAggdISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLP---KARGDDEIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 84 FKPARVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNKERFTFL 163
Cdd:COG1048 79 FRPARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 164 KWGARAFDNMLIVPPGSGIVHQVNLEYLARVVFESDssADGSKILYPDSVVGTDSHTTMINglgvlgwgvggIEAEAVML 243
Cdd:COG1048 159 KWGQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTRE--EDGETVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 244 GQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFP 323
Cdd:COG1048 237 GQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 324 IDENTLSYMRQTNRSEKKIDIIRKYLKATRQLRDYSlvDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSMCEDFKS 403
Cdd:COG1048 317 VDEETLDYLRLTGRSEEQIELVEAYAKAQGLWRDPD--APEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 404 CLISPVGFKGFAIPPSALaasgefqwdDGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSILPYIKTS 483
Cdd:COG1048 395 ALAAPVGEELDKPVRVEV---------DGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 484 LSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHPNTRANY 563
Cdd:COG1048 466 LAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANF 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 564 LASPLLVIAYAIAGRVDIDFEIEPLGVDSNGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQTLEVSD 643
Cdd:COG1048 546 LASPPLVVAYALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPA 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 644 SKLYPWSEISTYIKLPPFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPRDFNSYG 723
Cdd:COG1048 626 GELYDWDPDSTYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYG 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 724 SRRGNDAVMARGTFANIRLVNKLASKT-GPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAAKGPFL 802
Cdd:COG1048 706 SRRGNHEVMMRGTFANIRIKNLLAPGTeGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRL 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 803 LGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVLPEGELKPGQRIQV---DADGNV--FETTLR 877
Cdd:COG1048 786 LGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAPGKTVTVtatRADGSTeeFPVLHR 865
|
890 900
....*....|....*....|....
gi 17137564 878 FDTEVDITYYKNGGILNYMIRKML 901
Cdd:COG1048 866 IDTPVEVEYYRAGGILQYVLRQLL 889
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
2-901 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1285.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 2 SGSGANPFAQFQESFTQ-DGNVY-KYFDLPSI-DSKYESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGW-TPSLKQet 77
Cdd:PLN00070 38 SMASENPFKGILTSLPKpGGGEFgKYYSLPALnDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWeNTSPKQ-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 78 sdVEVSFKPARVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNK 157
Cdd:PLN00070 116 --VEIPFKPARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 158 ERFTFLKWGARAFDNMLIVPPGSGIVHQVNLEYLARVVFESDSsadgskILYPDSVVGTDSHTTMINGLGVLGWGVGGIE 237
Cdd:PLN00070 194 ERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDG------ILYPDSVVGTDSHTTMIDGLGVAGWGVGGIE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 238 AEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGA 317
Cdd:PLN00070 268 AEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 318 TVGYFPIDENTLSYMRQTNRSEKKIDIIRKYLKATRQLRDYSLVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSM 397
Cdd:PLN00070 348 TMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEM 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 398 CEDFKSCLISPVGFKGFAIPPSALAASGEFQWDdGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSIL 477
Cdd:PLN00070 428 KADWHSCLDNKVGFKGFAVPKEAQSKVAKFSFH-GQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 478 PYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHP 557
Cdd:PLN00070 507 PWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHP 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 558 NTRANYLASPLLVIAYAIAGRVDIDFEIEPLGVDSNGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQ 637
Cdd:PLN00070 587 LTRANYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWN 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 638 TLEVSDSKLYPWSEISTYIKLPPFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPR 717
Cdd:PLN00070 667 QLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRK 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 718 DFNSYGSRRGNDAVMARGTFANIRLVNK-LASKTGPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWA 796
Cdd:PLN00070 747 DFNSYGSRRGNDEIMARGTFANIRIVNKlLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWA 826
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 797 AKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVLPE--GELKPGQRIQVDAD-GNVFE 873
Cdd:PLN00070 827 AKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSniSEIKPGQDVTVTTDnGKSFT 906
|
890 900
....*....|....*....|....*...
gi 17137564 874 TTLRFDTEVDITYYKNGGILNYMIRKML 901
Cdd:PLN00070 907 CTLRFDTEVELAYFDHGGILPYVIRNLI 934
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
14-901 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1282.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 14 ESFTQDGNVYKYFDLPSID----SKYESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGWtpsLKQETSDVEVSFKPARV 89
Cdd:PRK12881 10 KEFDVGGKTYKFYSLPALGkelgGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANW---LPERKSDDEIPFVPARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 90 ILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNKERFTFLKWGARA 169
Cdd:PRK12881 87 VMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 170 FDNMLIVPPGSGIVHQVNLEYLARVVFESDssADGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSISM 249
Cdd:PRK12881 167 FDNFRVVPPGTGIMHQVNLEYLARVVHTKE--DDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 250 LLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDENTL 329
Cdd:PRK12881 245 LIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 330 SYMRQTNRSEKKIDIIRKYLKATRQLRDyslVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSMCEDFKSCLISPV 409
Cdd:PRK12881 325 DYLRLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 410 GFKGFAIPPsalaasgefqwDDGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSILPYIKTSLSPGSG 489
Cdd:PRK12881 402 AENGFAKKA-----------QTSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 490 VVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHPNTRANYLASPLL 569
Cdd:PRK12881 471 VVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPL 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 570 VIAYAIAGRVDIDFEIEPLGVDSNGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQTLEVSDSKLYPW 649
Cdd:PRK12881 551 VVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDW 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 650 SEISTYIKLPPFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPRDFNSYGSRRGND 729
Cdd:PRK12881 631 DPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNH 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 730 AVMARGTFANIRLVNKLA-SKTGPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAV 808
Cdd:PRK12881 711 EVMMRGTFANVRIKNLMIpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAV 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 809 IAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVLPEGELKPGQRIQV---DADGNV--FETTLRFDTEVD 883
Cdd:PRK12881 791 IAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVTLvihRADGSTerVPVLCRIDTPIE 870
|
890
....*....|....*...
gi 17137564 884 ITYYKNGGILNYMIRKML 901
Cdd:PRK12881 871 VDYYKAGGILPYVLRQLL 888
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
23-901 |
0e+00 |
|
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes. [Energy metabolism, TCA cycle]
Pssm-ID: 273562 [Multi-domain] Cd Length: 876 Bit Score: 1271.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 23 YKYFDLPSI---DSKYESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGWtpsLKQETSDVEVSFKPARVILQDFTGVPA 99
Cdd:TIGR01341 3 YYYYSLKALeesGGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKW---KIGEVADTEIAFKPARVVMQDFTGVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 100 VVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNKERFTFLKWGARAFDNMLIVPPG 179
Cdd:TIGR01341 80 VVDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 180 SGIVHQVNLEYLARVVFESDSsaDGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSISMLLPEVIGYRL 259
Cdd:TIGR01341 160 TGIIHQVNLEYLATVVFKAEV--DGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 260 EGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDENTLSYMRQTNRSE 339
Cdd:TIGR01341 238 TGKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 340 KKIDIIRKYLKATRQLRDYSlvdQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSMCEDFKSCLISPVGFKGFAIPPS 419
Cdd:TIGR01341 318 DHVELVEKYARAQGLFYDDS---EEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 420 ALaasgeFQWDDGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSILPYIKTSLSPGSGVVTYYLRESG 499
Cdd:TIGR01341 395 PL-----KKKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 500 VIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHPNTRANYLASPLLVIAYAIAGRV 579
Cdd:TIGR01341 470 LLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNI 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 580 DIDFEIEPLGVDSNGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQTLEVSDSKLYPWSEISTYIKLP 659
Cdd:TIGR01341 550 DINLYTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLP 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 660 PFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPRDFNSYGSRRGNDAVMARGTFAN 739
Cdd:TIGR01341 630 PFFEEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFAN 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 740 IRLVNKLA-SKTGPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHR 818
Cdd:TIGR01341 710 IRIKNLMVkGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHR 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 819 SNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVlPEGELKPGQRIQV---DADGN--VFETTLRFDTEVDITYYKNGGIL 893
Cdd:TIGR01341 790 SNLVGMGVIPLQFPQGEDAETLGLTGDETIDID-GIKDLKPGKEVTVtftNSKGEkiTFKCVLRIDTEVELDYYKHGGIL 868
|
....*...
gi 17137564 894 NYMIRKML 901
Cdd:TIGR01341 869 QYVLRKFL 876
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
88-579 |
0e+00 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 769.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 88 RVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNKERFTFLKWGA 167
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 168 RAFDNMLIVPPGSGIVHQVNLEYLARVVFESdsSADGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSI 247
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTS--EEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 248 SMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDen 327
Cdd:cd01586 159 SMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 328 tlsymrqtnrsekkidiirkylkatrqlrdyslvdqdpqyTESVTLDLSTVVTSVSGPKRPHDRVSVssmcedfksclis 407
Cdd:cd01586 237 ----------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 408 pvgfkgfaippsalaasgefqwddgksykigHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSILPYIKTSLSPG 487
Cdd:cd01586 264 -------------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 488 SGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHPNTRANYLASP 567
Cdd:cd01586 313 SRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASP 392
|
490
....*....|..
gi 17137564 568 LLVIAYAIAGRV 579
Cdd:cd01586 393 PLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
76-577 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 622.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 76 ETSDVEVSFKPARVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSvqvdfvrsSDALTKNESLEFQR 155
Cdd:pfam00330 10 EELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 156 NKERFTFLKWGARAFdNMLIVPPGSGIVHQVNLEYLarvvfesdssadgskILYPD-SVVGTDSHTTMINglgvlgwgvg 234
Cdd:pfam00330 82 NKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG---------------LALPGmTIVGTDSHTTTHGglgalafgvg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 235 gIEAEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPE 314
Cdd:pfam00330 146 gSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 315 YGATVGYFPIDENTLSYMRQTNRSEKKidIIRKYLKATRQLRDYSlvDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSV 394
Cdd:pfam00330 226 YGATAGLFPPDETTFEYLRATGRPEAP--KGEAYDKAVAWKTLAS--DPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 395 SS-MCEDFKSCLISPVGFKGFAIppsalaasgefqWDDGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKnAVQKG 473
Cdd:pfam00330 302 SElVPDPFADAVKRKAAERALEY------------MGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKK-AVEKG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 474 LSILPYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVntieknglvccGVLSGNRNFEG 553
Cdd:pfam00330 369 LKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPGER-----------CVSSSNRNFEG 437
|
490 500
....*....|....*....|....
gi 17137564 554 RIHPNTRAnYLASPLLVIAYAIAG 577
Cdd:pfam00330 438 RQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
683-852 |
8.89e-114 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 345.03 E-value: 8.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 683 LLGDSVTTDHISPAGSIARKSPAARYLSERGLTPRDFNSYGSRRGNDAVMARGTFANIRLVNKLASKTGPSTLHVPS-GE 761
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPtGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 762 EMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLK 841
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|.
gi 17137564 842 LSGREVYNIVL 852
Cdd:cd01580 161 LTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
88-579 |
7.57e-89 |
|
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: 287.86 E-value: 7.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 88 RVILQDFTGVPAVVDFAAMRDAVrelggnpeKINPICPADLVIDHSVQvdfvrssdaltknesLEFQRNKERFTFLKWgA 167
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALG--------KVADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 168 RAFDNMLIVPPGSGIVHQVNLEYLArvvfesdssadgskiLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSI 247
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENLA---------------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 248 SMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDEN 327
Cdd:cd01351 122 WLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 328 TLSYMRQTNRSEKKidiirkylKATRQLRDYSLVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSMcedfksclis 407
Cdd:cd01351 202 TLKWLEATGRPLLK--------NLWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEV---------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 408 pvgfkgfaippsalaasgefqwddgksykiGHGSVVIAAITSCTNtSNPSVMLGAGLLAKNAVQKglsilPYIKTSLSPG 487
Cdd:cd01351 264 ------------------------------EGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGAKVA-----PGVRLIVTPG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 488 SGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLdenvvntiekNGLVCCGVLSGNRNFEGRIHPNTRANYLASP 567
Cdd:cd01351 308 SRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARL----------VADGEVGVSSGNRNFPGRLGTYERHVYLASP 377
|
490
....*....|..
gi 17137564 568 LLVIAYAIAGRV 579
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
81-901 |
2.40e-78 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 267.40 E-value: 2.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 81 EVSFKPARVILQDFTGVPAVVDFAAM-RDAVR-ELggnpekinpicpADLVIDHS-VQVDFvrssdaltkneslefqRNK 157
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgLDRVKtEL------------SVQYVDHNlLQADF----------------ENA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 158 ERFTFLKWGARAFDnmlIV--PPGSGIVHQVNLEYLARvvfesdssadgskilyP-DSVVGTDSHTT------MInglgv 228
Cdd:PRK07229 76 DDHRFLQSVAAKYG---IYfsKPGNGICHQVHLERFAF----------------PgKTLLGSDSHTPtagglgML----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 229 lgwgvgGI-----EAEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTItkhLRQLGV---VGKFVEFYGPGVAEL 300
Cdd:PRK07229 132 ------AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILEL---LRRLTVkggVGKIIEYFGPGVATL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 301 SIADRATISNMCPEYGATVGYFPIDENTLSYMRQTNRSEKKIDiirkyLKAtrqlrdyslvDQDPQYTESVTLDLSTVVT 380
Cdd:PRK07229 203 SVPERATITNMGAELGATTSIFPSDERTREFLKAQGREDDWVE-----LLA----------DPDAEYDEVIEIDLSELEP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 381 SVSGPKRPHDRVSVSSMcedfksclispvgfKGFAIppsalaasgefqwddgksykighgSVViaAITSCTNTSNPSVML 460
Cdd:PRK07229 268 LIAGPHSPDNVVPVSEV--------------AGIKV------------------------DQV--LIGSCTNSSYEDLMR 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 461 GAGLLAKNAVQKGLSILpyiktsLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSG-PLDENVVntiekngl 539
Cdd:PRK07229 308 AASILKGKKVHPKVSLV------INPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQaPATGNVS-------- 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 540 vccgVLSGNRNFEGRI-HPNTRAnYLASPLLVIAYAIAGRVDidfeiEPLGV-DSNGKEVflrdiwptrsEIQEVEHKHV 617
Cdd:PRK07229 374 ----LRTFNRNFPGRSgTKDAQV-YLASPETAAASALTGVIT-----DPRTLaLENGEYP----------KLEEPEGFAV 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 618 IPAMFQEvyskiqlGSRDWQTLEVsdsklypwsEISTYIKLPPFFEgmtrALPKLKGiekARCLLLLGDSVTTDHISPAG 697
Cdd:PRK07229 434 DDAGIIA-------PAEDGSDVEV---------VRGPNIKPLPLLE----PLPDLLE---GKVLLKVGDNITTDHIMPAG 490
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 698 siarkspaARYLSERGLTPRdfnsygsrrgndavMARGTFanIRLVNklasktgpstlhvpsgeemdifDAAERyASEGT 777
Cdd:PRK07229 491 --------AKWLPYRSNIPN--------------ISEFVF--EGVDN----------------------TFPER-AKEQG 523
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 778 PLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFL-PG-----QSADTLKLSGreVYNIv 851
Cdd:PRK07229 524 GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFAdPAdydkiEEGDVLEIED--LREF- 600
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 17137564 852 LPEGELKpgqrIQVDADGNVFETTLRFdTEVDITYYKNGGILNYmIRKML 901
Cdd:PRK07229 601 LPGGPLT----VVNVTKDEEIEVRHTL-SERQIEILLAGGALNL-IKKKL 644
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
705-834 |
8.39e-50 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 171.78 E-value: 8.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 705 AARYLSERGLTPRDFNSYGSRRGNDAVMARGTFANIRLVNKLA-SKTGPSTLHVPSGEEMDIFDAAERYASEGTPLVLVV 783
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17137564 784 GKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPG 834
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
88-579 |
5.14e-44 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 163.90 E-value: 5.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 88 RVILQDFTGVPAvvdFAAMRDAVRELGGNPEKINpicpadLVIDHSVQVDFVRSSDaltkneslefQRNKERFTFLKWGA 167
Cdd:cd01583 1 LHLVHDVTSPQA---FEGLREAGREKVWDPEKIV------AVFDHNVPTPDIKAAE----------QVKTLRKFAKEFGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 168 RAFDnmlivPPGSGIVHQVNLE-YLARvvfesdssadgskilyP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQ 245
Cdd:cd01583 62 NFFD-----VGRQGICHVILPEkGLTL----------------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 246 SISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPID 325
Cdd:cd01583 121 KLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 326 ENTLSYMRQtnrsekkidiirkylkatRQLRDYSLV--DQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSmcedfks 403
Cdd:cd01583 201 ETTFEYLKG------------------RGKAYWKELksDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSE------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 404 clISPVgfkgfaippsalaasgefqwddgksyKIGHgsVVIAaitSCTNTSNPSVMLGAGLLaknavqKGLSILPYIKTS 483
Cdd:cd01583 256 --VEGI--------------------------KIDQ--VFIG---SCTNGRLEDLRAAAEIL------KGRKVADGVRLI 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 484 LSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIG-NSGPLDEnvvntieknGLVCcgVLSGNRNFEGRIHPNTRAN 562
Cdd:cd01583 297 VVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAP---------GERC--VSTSNRNFKGRMGSPGARI 365
|
490
....*....|....*..
gi 17137564 563 YLASPLLVIAYAIAGRV 579
Cdd:cd01583 366 YLASPATAAASAITGEI 382
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-579 |
3.38e-43 |
|
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: 161.46 E-value: 3.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 90 ILQDFTGVPAVVDFAAMR-DAVR-ELggnpekinpicpADLVIDHS-VQVDFvrssdaltkneslefqRNKERFTFLKWG 166
Cdd:cd01585 4 LTQDATGTMAYLQFEAMGvDRVRtEL------------SVSYVDHNtLQTDF----------------ENADDHRFLQTV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 167 ARAFdNMLIVPPGSGIVHQVNLEYLARvvfesdssaDGSKILypdsvvGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQS 246
Cdd:cd01585 56 AARY-GIYFSRPGNGICHQVHLERFAV---------PGKTLL------GSDSHTPTAGGLGMLAIGAGGLDVALAMAGEP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 247 ISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDE 326
Cdd:cd01585 120 YYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 327 NTLSYMRQTNRSEKKIDIirkylkatrqlrdysLVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSmcedfkscli 406
Cdd:cd01585 200 RTREFLAAQGREDDWVEL---------------AADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVRE---------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 407 spvgfkgfaippsalaasgefqwddgksykIGHGSVVIAAITSCTNTSNPSVMLGAGLLaknavqKGLSILPYIKTSLSP 486
Cdd:cd01585 255 ------------------------------VAGIKVDQVAIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAP 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 487 GSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNtieknglvccgVLSGNRNFEGRIHPNTRANYLAS 566
Cdd:cd01585 299 GSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTGGVS-----------VRTFNRNFEGRSGTKDDLVYLAS 367
|
490
....*....|...
gi 17137564 567 PLLVIAYAIAGRV 579
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
88-579 |
1.98e-42 |
|
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: 160.20 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 88 RVILQDFTGVPAVvdfaamrDAVRELGG----NPEKINpicpadLVIDHSVQvdfvrssdalTKNE-SLEFQRNKERFTf 162
Cdd:COG0065 30 LHLVHDVTSPQAF-------EGLREAGGrkvwDPDRIV------AVFDHNVP----------TKDPkSAEQVKTLREFA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 163 LKWGARAFDnmlivpPGS-GIVHQVNLEY-LARvvfesdssadgskilyP-DSVVGTDSHTTM----------INGLgvl 229
Cdd:COG0065 86 KEFGITFFD------VGDpGICHVVLPEQgLVL----------------PgMTIVGGDSHTCThgafgafafgIGTT--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 230 gwgvggiEAEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATIS 309
Cdd:COG0065 141 -------DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 310 NMCPEYGATVGYFPIDENTLSYMRQtnrsekkidiirkylkatRQLRDYSLV--DQDPQYTESVTLDLSTVVTSVSGPKR 387
Cdd:COG0065 214 NMAIEAGAKAGIIAPDETTFEYLKG------------------RPFAPWRTLksDEDAVYDKEVEIDASDLEPQVAWPHS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 388 PHDRVSVSSMcedfksclispvgfKGFAIppsalaasgefqwDdgksykighgsvvIAAITSCTNtsnpsvmlgaG---- 463
Cdd:COG0065 276 PDNVVPVSEL--------------EGIKI-------------D-------------QVFIGSCTN----------Gried 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 464 LLAKNAVQKGLSILPYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIG-NSGPLDEnvvntieknGLVCc 542
Cdd:COG0065 306 LRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAP---------GERC- 375
|
490 500 510
....*....|....*....|....*....|....*...
gi 17137564 543 gVLSGNRNFEGRI-HPNTRAnYLASPLLVIAYAIAGRV 579
Cdd:COG0065 376 -ASTSNRNFEGRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
88-578 |
8.50e-41 |
|
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: 155.68 E-value: 8.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 88 RVILQDFTGVPAVVDFAAmrdavrelGGNPEkinPICPADLVIDHSVQVDFVRSSDALTKNESlefqrNKERFTFLKwGA 167
Cdd:cd01584 1 RVAMQDATAQMALLQFMS--------SGLPK---VAVPSTIHCDHLIEAQVGGEKDLKRAKDI-----NKEVYDFLA-SA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 168 RAFDNMLIVPPGSGIVHQVNLEYLArvvfesdssadgskilYPDS-VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQS 246
Cdd:cd01584 64 GAKYGIGFWKPGSGIIHQIVLENYA----------------FPGLlMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 247 ISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDE 326
Cdd:cd01584 128 WELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 327 NTLSYMRQTNRSEkkIDIIRKYLKAtrqlrDYSLVDQDPQYTESVTLDLSTVVTSVSGPKRPHdrvsvssmcedfkscli 406
Cdd:cd01584 208 RMKKYLKATGRAE--IADLADEFKD-----DLLVADEGAEYDQLIEINLSELEPHINGPFTPD----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 407 spvgfkgFAIPPSALAASGEFQ-WDDgksykighgSVVIAAITSCTNTSNPSvMLGAGLLAKNAVQKGLSilPYIKTSLS 485
Cdd:cd01584 264 -------LATPVSKFKEVAEKNgWPL---------DLRVGLIGSCTNSSYED-MGRAASIAKQALAHGLK--CKSIFTIT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 486 PGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNsgpLDENVVNTIEKNGLVCcgvlSGNRNFEGR--IHPNTRAnY 563
Cdd:cd01584 325 PGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQ---WDRKDIKKGEKNTIVT----SYNRNFTGRndANPATHA-F 396
|
490
....*....|....*
gi 17137564 564 LASPLLVIAYAIAGR 578
Cdd:cd01584 397 VASPEIVTAMAIAGT 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
89-579 |
2.68e-30 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 124.52 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 89 VILQDFTGVPAVVDFaamrdavRELGG----NPEKINpicpadLVIDHsvqvdFVRSSDAltknESLEFQRNKERFtflk 164
Cdd:PRK00402 31 VMAHDITGPLAIKEF-------EKIGGdkvfDPSKIV------IVFDH-----FVPAKDI----KSAEQQKILREF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 165 wgARA------FDNmlivppGSGIVHQVNLEY-LARvvfesdssadgskilyP-DSVVGTDSHTT--------------- 221
Cdd:PRK00402 85 --AKEqgipnfFDV------GEGICHQVLPEKgLVR----------------PgDVVVGADSHTCtygalgafatgmgst 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 222 -MinglgvlgwgvggieAEAVMLGQsISMLLPEVIGYRLEGKLGPLATSTDLVLTItkhLRQLGVVG---KFVEFYGPGV 297
Cdd:PRK00402 141 dM---------------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHI---IGDIGVDGatyKALEFTGETI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 298 AELSIADRATISNMCPEYGATVGYFPIDENTLSYMRQtnrsekkidiirkylkatRQLRDYSLV--DQDPQYTESVTLDL 375
Cdd:PRK00402 202 EALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKE------------------RAGRDYKPWksDEDAEYEEVYEIDL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 376 STVVTSVSGPKRPHDRVSVSsmcedfksclispvgfkgfaippsalaasgefqwddgksyKIGHGSVVIAAITSCTNtsn 455
Cdd:PRK00402 264 SKLEPQVAAPHLPDNVKPVS----------------------------------------EVEGTKVDQVFIGSCTN--- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 456 psvmlgaG----LLAKNAVQKGLSILPYIKTSLSPGSGVVtyYLR--ESGVIPYLEQLGFdIVGY-GCMTCIGNS-GPLD 527
Cdd:PRK00402 301 -------GrledLRIAAEILKGRKVAPGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHmGVLA 370
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 17137564 528 EnvvntieknGLVCcgVLSGNRNFEGRI-HPNTRAnYLASPLLVIAYAIAGRV 579
Cdd:PRK00402 371 P---------GEVC--LSTTNRNFKGRMgSPESEV-YLASPAVAAASAVTGKI 411
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
80-577 |
9.95e-28 |
|
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: 116.78 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 80 VEVsfKPARVILQDFTGVPAvvdFAAMRDAVRELGGNPEKINpicpadLVIDHSVQVDFVRSSDAltKNESLEFQRnker 159
Cdd:TIGR02086 22 VEV--EVDLAMTHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNVPPPTVEAAEM--QKEIREFAK---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 160 ftflKWGARAFDNmlivppGSGIVHQVNLEylarvvfesDSSADGSKIlypdsVVGTDSHTTMINGLGVLGWGVGGIE-A 238
Cdd:TIGR02086 85 ----RHGIKNFDV------GEGICHQILAE---------EGYALPGMV-----VVGGDSHTCTSGAFGAFATGMGATDmA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 239 EAVMLGQSISMLlPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGAT 318
Cdd:TIGR02086 141 IALATGKTWIKV-PETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 319 VGYFPIDENTLSYMRQTNRSEKKIdiirkylkatrqlrdySLVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSsmc 398
Cdd:TIGR02086 220 AGIIEPDEETYEYLKKRRGLEFRI----------------LVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVS--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 399 edfksclispvgfkgfaippsalaasgefqwdDGKSYKIGHgsvviAAITSCTNTSNPSVMLGAGLLaknavqKGLSILP 478
Cdd:TIGR02086 281 --------------------------------DVEGTEIDQ-----VFIGSCTNGRLEDLRIAAEIL------KGRRVHP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 479 YIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIG-NSGPLDEnvvntieknGLVCcgVLSGNRNFEGRI-H 556
Cdd:TIGR02086 318 DVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGaHMGVLGD---------GEVC--LSTTNRNFKGRMgS 386
|
490 500
....*....|....*....|.
gi 17137564 557 PNTRAnYLASPLLVIAYAIAG 577
Cdd:TIGR02086 387 PNAEI-YLASPATAAASAVEG 406
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
88-578 |
1.66e-22 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 101.91 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 88 RVILQDFTGVPAvvdFAAMRDAVRELGgNPEKinpicpADLVIDHSVQVDFVRS---SDALTKNESLEFQRNKERFtflk 164
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTVR-RPDL------TLAVVDHVVPTRPGRDrgiTDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 165 wGARAFDnmlIVPPGSGIVHQVNLEY-LARvvfesdssadgskilyPDSVVGT-DSHTTMINGLGVLGWGVGGIEAEAVM 242
Cdd:PRK12466 96 -GIRLFD---VDDPRQGIVHVVAPELgLTL----------------PGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 243 LGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYF 322
Cdd:PRK12466 156 ATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 323 PIDENTLSYMRQTNRSEKKIDIIRKyLKATRQLRDyslvDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSmcedfk 402
Cdd:PRK12466 236 APDETTFDYLRGRPRAPKGALWDAA-LAYWRTLRS----DADAVFDREVEIDAADIAPQVTWGTSPDQAVPITG------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 403 sclispvgfkgfAIPPSALAASGEFQ--WDDGKSY------------KIGHgsvviAAITSCTNtsnpsvmlgaG----L 464
Cdd:PRK12466 305 ------------RVPDPAAEADPARRaaMERALDYmgltpgtplagiPIDR-----VFIGSCTN----------GriedL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 465 LAKNAVQKGLSILPYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGnsgpLDENVVNTIEKnglvCcgV 544
Cdd:PRK12466 358 RAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA----MNDDVLAPGER----C--A 427
|
490 500 510
....*....|....*....|....*....|....
gi 17137564 545 LSGNRNFEGRIHPNTRAnYLASPLLVIAYAIAGR 578
Cdd:PRK12466 428 STTNRNFEGRQGPGART-HLMSPAMVAAAAVAGH 460
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
774-850 |
6.51e-21 |
|
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: 87.91 E-value: 6.51e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137564 774 SEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGqsADTLKLSGREVYNI 850
Cdd:cd00404 12 SPAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADP--EDYLKLHTGDELDI 86
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
684-831 |
4.20e-20 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 86.72 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 684 LGDSVTTDHISPAGsiarkspaARYLSERGLTPRdfnsygsrrgndavMARGTFANIRlvnklasktgpstlhvpsgeem 763
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLRSNIPA--------------ISEFVFHRVD---------------------- 37
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17137564 764 DIFdaAERyASEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQF 831
Cdd:cd01579 38 PTF--AER-AKAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
130-579 |
1.05e-18 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 88.83 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 130 IDHSVQVdfvRSSDALTKNESLEFQRNKERFTFLkwgarafdnmlivPPGSGIVHQVNLEylarvvfesdssadgSKILY 209
Cdd:cd01582 33 LDHDVQN---KSEKNLKKYKNIESFAKKHGIDFY-------------PAGRGIGHQIMIE---------------EGYAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 210 PDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGK 288
Cdd:cd01582 82 PGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 289 FVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDENTLsymrqtnrsekkidiirkylkatrqlrdyslvdqdpqyt 368
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHL--------------------------------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 369 esvTLDLSTVVTSVSGPkrphDRVSVSSMCEDFKSclispvgfkgfaippsalaasgefqwddgKSYKIGHgsvviAAIT 448
Cdd:cd01582 203 ---ILDLSTLSPYVSGP----NSVKVSTPLKELEA-----------------------------QNIKINK-----AYLV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 449 SCTNTSNPSVMLGAGLL-AKNAVQKGLSILPYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIG-NSGPL 526
Cdd:cd01582 242 SCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGlGQGLL 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 17137564 527 DENVVntieknglvccGVLSGNRNFEGRIHPNTRANYLASPLLVIAYAIAGRV 579
Cdd:cd01582 322 EPGEV-----------GISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
237-581 |
3.98e-16 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 82.09 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 237 EAEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTItkhLRQLGV---VGKFVEFYGPGVAELSIADRATISNMCP 313
Cdd:PRK05478 148 EVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 314 EYGATVGYFPIDENTLSYMRQTNRSEKKIDIiRKYLKATRQLRDyslvDQDPQYTESVTLDLSTV------------VTS 381
Cdd:PRK05478 225 EAGARAGLVAPDETTFEYLKGRPFAPKGEDW-DKAVAYWKTLKS----DEDAVFDKVVTLDAADIepqvtwgtnpgqVIS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 382 VSGP-------KRPHDRVSVSSMCE--DFKSclispvgfkGFAIppsalaasgefqwddgKSYKIGHgsvviAAITSCTN 452
Cdd:PRK05478 300 IDGKvpdpedfADPVKRASAERALAymGLKP---------GTPI----------------TDIKIDK-----VFIGSCTN 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 453 tsnpsvmlgaG----LLAKNAVQKGLSILPYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIG-NSGPLD 527
Cdd:PRK05478 350 ----------SriedLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLP 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 17137564 528 EnvvntieknGLVCcgVLSGNRNFEGRIHPNTRaNYLASPLLVIAYAIAGR-VDI 581
Cdd:PRK05478 420 P---------GERC--ASTSNRNFEGRQGKGGR-THLVSPAMAAAAAITGHfVDV 462
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
689-831 |
9.40e-13 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 66.72 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 689 TTDHISPAGSiarkspaarYLSERGLTPRDFNSY--GsrrgndAVMARGTFANiRLVNKLASKTGPstlhVPsgeemdif 766
Cdd:cd01578 7 TTDHISAAGP---------WLKYRGHLDNISNNLliG------AINAENGKAN-SVKNQVTGEYGP----VP-------- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137564 767 DAAERYASEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQF 831
Cdd:cd01578 59 DTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTF 123
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
780-847 |
1.65e-12 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 64.15 E-value: 1.65e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137564 780 VLVVGKDYGSGSSR---DWAAKGpflLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREV 847
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDEV 87
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
677-883 |
1.67e-12 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 67.12 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 677 KARCLLLLGDSVTTDHISPAgsiarkspaaRYLseRGLTPRDFnsygsrrgndavmARGTFANIRLVNKlasktgpstlh 756
Cdd:COG0066 7 TGRAVPLDGDNIDTDQIIPA----------RFL--KTIDREGL-------------GKHLFEDWRYDRS----------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 757 vpsgEEMDIFDAAERYAsEGTplVLVVGKDYGSGSSRD---WAAKGpflLGIKAVIAESYERIHRSNLVGMGIIPLQfLP 833
Cdd:COG0066 51 ----PDPDFVLNQPRYQ-GAD--ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17137564 834 GQSADTLklsgrevynivLPEGELKPGQRIQVD-ADGNV-FETTLRFDTEVD 883
Cdd:COG0066 120 EEAVDAL-----------FAAIEANPGDELTVDlEAGTVtNGTGETYPFEID 160
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
780-895 |
1.89e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 60.59 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 780 VLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQF--LPGQSADtlklsGREVynivlpEGEL 857
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESeeVVDALED-----GDEV------ELDL 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 17137564 858 KPGqriQVDADGNVFEttLRFDTEVDITYYKNGGILNY 895
Cdd:PRK14023 121 ETG---VLTRGGETFQ--LRPPPEFLLEALKEGSILEY 153
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
780-899 |
8.11e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 52.52 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 780 VLVVGKDYGSGSSRD---WAAKGpflLGIKAVIAESYERIHRSNLVGMGiIPLqflpgqsadtlklsgrevynIVLPE-- 854
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIG-LPV--------------------LECDEav 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17137564 855 GELKPGQRIQVDADGNVFeTTLRFDTEVDITYY--------KNGGILNYMIRK 899
Cdd:PRK00439 107 DKIEDGDEVEVDLETGVI-TNLTTGEEYKFKPIpefmleilKAGGLIEYLKKK 158
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
780-866 |
1.70e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 52.44 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 780 VLVVGKDYGSGSSRD---WAakgpfLL--GIKAVIAESYERIHRSNLVGMGIIPlqflpgqsadtlklsgrevynIVLPE 854
Cdd:PRK01641 70 ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP---------------------IVLPE 123
|
90 100
....*....|....*....|.
gi 17137564 855 GELK---------PGQRIQVD 866
Cdd:PRK01641 124 EDVDelfklveanPGAELTVD 144
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
176-388 |
2.16e-07 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 54.63 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 176 VPPGSGIVHQVNLEYLArvvfesdssADGSKILypdsvvGTDSHT------TMinglgvlgwgvggieaeAV-------- 241
Cdd:PRK11413 123 VPPHIAVIHQYMREMMA---------GGGKMIL------GSDSHTrygalgTM-----------------AVgegggelv 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 242 --MLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVV-GKFVEFYGPGVAELSIADRATISNMCPEygat 318
Cdd:PRK11413 171 kqLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE---- 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17137564 319 vgyfpidENTLSYMRQTNrsekkiDIIRKYLKATRQLRDYS-LVDQDPQYTES-VTLDLSTVVTSVSGPKRP 388
Cdd:PRK11413 247 -------TTCLSSIWQTD------EEVHNWLALHGRGQDYCeLNPQPMAYYDGcISVDLSAIKPMIALPFHP 305
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
683-830 |
5.06e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 42.92 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137564 683 LLGDSVTTDHISPAGsiarkspaarYLSERGLTPRDFNSYGSRrgndAVMARGTFANIRLVNKLASKTgpstlhvpsgee 762
Cdd:PLN00072 75 VVGDNIDTDQIIPAE----------YLTLVPSKPDEYEKLGSY----ALIGLPAFYKTRFVEPGEMKT------------ 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17137564 763 mdifdaaeRYAsegtplVLVVGKDYGSGSSRDWAakgPFLLG---IKAVIAESYERIHRSNLVGMG-IIPLQ 830
Cdd:PLN00072 129 --------KYS------IIIGGENFGCGSSREHA---PVALGaagAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| |
