|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
4-897 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1795.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 4 SLDSFNCRSTLTVNGTDYVYYSLPKAEANGLAGVSKLPYSMKVLLENLLRFEDGRSVTKEHILSVAAWLsNKGTVENEIA 83
Cdd:PRK09277 3 STDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWL-PKAKPDREIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 84 YRPARVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFL 163
Cdd:PRK09277 82 FRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 164 KWGQQAFKNFRVVPPGTGICHQVNLEYLGQTVWTKdEDGEIVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ 243
Cdd:PRK09277 162 KWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTR-EDGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 244 PVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVD 323
Cdd:PRK09277 241 PSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 324 AETVNYLTMSGREEQRIALVEAYSKAQGMWRDgDGSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAMEN 403
Cdd:PRK09277 321 EETLDYLRLTGRDEEQVALVEAYAKAQGLWRD-PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 404 DYKKPGQLENRypvEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVGEYLA 483
Cdd:PRK09277 400 GVQGFGLDEAE---EGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 484 KSGLQADLDALGFNLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVVAYALA 563
Cdd:PRK09277 477 KAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 564 GSVQKDLTSEPLGEDRDGKPVYLKDIWPSSQEIQAFIMKYVTRELYASKYADVFKGDANWQAVQVPAGQTYAWDDQSTYV 643
Cdd:PRK09277 557 GTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 644 QNPPYFVGMGKTGSGLSDIRGARVLGLFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEVMMRGT 723
Cdd:PRK09277 637 RNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGT 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 724 FANIRIRNHMLgpNGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSF 803
Cdd:PRK09277 717 FANIRIRNEMV--PGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESF 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 804 ERIHRSNLVGMGVVPFVFEDGTTWASLDLKGDETVTIEGLEgDIKPREKKIARITYADGTVRDVPLLCRIDTLDEVTYMN 883
Cdd:PRK09277 795 ERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLE-DLKPGATVTVVITRADGEVVEFPVLCRIDTAVEVDYYR 873
|
890
....*....|....
gi 1032825772 884 NGGILQTVLRDLAA 897
Cdd:PRK09277 874 NGGILQYVLRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
4-897 |
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: 1730.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 4 SLDSFNCRSTLTVNGTDYVYYSLPKAEANGlAGVSKLPYSMKVLLENLLRFEDGRSVTKEHILSVAAWLsNKGTVENEIA 83
Cdd:COG1048 1 SMDSFKARKTLTVGGKPYTYYSLPALEEAG-GDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWL-PKARGDDEIP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 84 YRPARVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFL 163
Cdd:COG1048 79 FRPARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 164 KWGQQAFKNFRVVPPGTGICHQVNLEYLGQTVWTKDEDGEIVAYPDTCVGTDSHTTMINglgvlgwgvggIEAEAAMLGQ 243
Cdd:COG1048 159 KWGQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 244 PVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVD 323
Cdd:COG1048 239 PVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 324 AETVNYLTMSGREEQRIALVEAYSKAQGMWRDGDGSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAMEN 403
Cdd:COG1048 319 EETLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 404 DYKKPGQLENRYPVEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVGEYLA 483
Cdd:COG1048 399 PVGEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 484 KSGLQADLDALGFNLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVVAYALA 563
Cdd:COG1048 479 RAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 564 GSVQKDLTSEPLGEDRDGKPVYLKDIWPSSQEIQAFIMKYVTRELYASKYADVFKGDANWQAVQVPAGQTYAWDDQSTYV 643
Cdd:COG1048 559 GTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYI 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 644 QNPPYFVGMGKTGSGLSDIRGARVLGLFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEVMMRGT 723
Cdd:COG1048 639 RRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGT 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 724 FANIRIRNHMLGpnGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSF 803
Cdd:COG1048 719 FANIRIKNLLAP--GTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESF 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 804 ERIHRSNLVGMGVVPFVFEDGTTWASLDLKGDETVTIEGLEGDIKPREKKIARITYADGTVRDVPLLCRIDTLDEVTYMN 883
Cdd:COG1048 797 ERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAPGKTVTVTATRADGSTEEFPVLHRIDTPVEVEYYR 876
|
890
....*....|....
gi 1032825772 884 NGGILQTVLRDLAA 897
Cdd:COG1048 877 AGGILQYVLRQLLA 890
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
4-897 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1458.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 4 SLDSFNCRSTLTVNGTDYVYYSLPKAEANGLAGVSKLPYSMKVLLENLLRFEDGRSVTKEHILSVAAWLSNkGTVENEIA 83
Cdd:PRK12881 2 AHNLHKTLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPE-RKSDDEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 84 YRPARVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFL 163
Cdd:PRK12881 81 FVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 164 KWGQQAFKNFRVVPPGTGICHQVNLEYLGQTVWTKDEDGEIVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ 243
Cdd:PRK12881 161 KWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 244 PVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVD 323
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 324 AETVNYLTMSGREEQRIALVEAYSKAQGMWRDgDGSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAM-- 401
Cdd:PRK12881 321 EQTLDYLRLTGRTEAQIALVEAYAKAQGLWGD-PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFsk 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 402 ---ENDYKKPGQlenrypvEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVV 478
Cdd:PRK12881 400 pvaENGFAKKAQ-------TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 479 GEYLAKSGLQADLDALGFNLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVV 558
Cdd:PRK12881 473 TEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 559 AYALAGSVQKDLTSEPLGEDRDGKPVYLKDIWPSSQEIQAFIMKYVTRELYASKYADVFKGDANWQAVQVPAGQTYAWDD 638
Cdd:PRK12881 553 AYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 639 QSTYVQNPPYFVGMGKTGSGLSDIRGARVLGLFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEV 718
Cdd:PRK12881 633 KSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEV 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 719 MMRGTFANIRIRNHMLGpnGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAV 798
Cdd:PRK12881 713 MMRGTFANVRIKNLMIP--GKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAV 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 799 IAQSFERIHRSNLVGMGVVPFVFEDGTTWASLDLKGDETVTIEGLEGDIKPREKKIARITYADGTVRDVPLLCRIDTLDE 878
Cdd:PRK12881 791 IAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVTLVIHRADGSTERVPVLCRIDTPIE 870
|
890
....*....|....*....
gi 1032825772 879 VTYMNNGGILQTVLRDLAA 897
Cdd:PRK12881 871 VDYYKAGGILPYVLRQLLA 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
21-895 |
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: 1315.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 21 YVYYSLPKAEANGlAGVSKLPYSMKVLLENLLRFEDGRSVTKEHILSVAAWLSNKgTVENEIAYRPARVLMQDFTGVPAV 100
Cdd:TIGR01341 3 YYYYSLKALEESG-GKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGE-VADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 101 VDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFLKWGQQAFKNFRVVPPGT 180
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 181 GICHQVNLEYLGQTVWTKDEDGEIVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVIGFKLTGK 260
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 261 LKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAETVNYLTMSGREEQRI 340
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 341 ALVEAYSKAQGMWRDgDGSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAMENDYKKPGQLENRYP---- 416
Cdd:TIGR01341 321 ELVEKYARAQGLFYD-DSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPlkkk 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 417 VEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVGEYLAKSGLQADLDALGF 496
Cdd:TIGR01341 400 VNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELGF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 497 NLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVVAYALAGSVQKDLTSEPLG 576
Cdd:TIGR01341 480 NLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPIG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 577 EDRDGKPVYLKDIWPSSQEIQAFIMKYVTRELYASKYADVFKGDANWQAVQVPAGQTYAWDDQSTYVQNPPYFVGMGKTG 656
Cdd:TIGR01341 560 TDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQDP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 657 SGLSDIRGARVLGLFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEVMMRGTFANIRIRNHMLgp 736
Cdd:TIGR01341 640 EEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMV-- 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 737 NGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGV 816
Cdd:TIGR01341 718 KGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGV 797
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032825772 817 VPFVFEDGTTWASLDLKGDETVTIEGLEgDIKPREKKIARITYADGTVRDVPLLCRIDTLDEVTYMNNGGILQTVLRDL 895
Cdd:TIGR01341 798 IPLQFPQGEDAETLGLTGDETIDIDGIK-DLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
9-897 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1284.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 9 NCRSTLTvNGTDYVYYSLPKAEAnglAGVSKLPYSMKVLLENLLRFEDGRSVTKEHILSVAAW--LSNKGTvenEIAYRP 86
Cdd:PTZ00092 18 KVLKTLK-DGGSYKYYSLNELHD---PRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWeeNSKKQI---EIPFKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 87 ARVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFLKWG 166
Cdd:PTZ00092 91 ARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 167 QQAFKNFRVVPPGTGICHQVNLEYLGQTVWtkDEDGeiVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVS 246
Cdd:PTZ00092 171 SKAFKNLLIVPPGSGIVHQVNLEYLARVVF--NKDG--LLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPIS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 247 MLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAET 326
Cdd:PTZ00092 247 MVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 327 VNYLTMSGREEQRIALVEAYSKAQGMWRDGDgSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAMEN--D 404
Cdd:PTZ00092 327 LDYLKQTGRSEEKVELIEKYLKANGLFRTYA-EQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSApvG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 405 YK----KPGQLENR--YPVEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVV 478
Cdd:PTZ00092 406 FKgfgiPEEKHEKKvkFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 479 GEYLAKSGLQADLDALGFNLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVV 558
Cdd:PTZ00092 486 TKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVV 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 559 AYALAGSVQKDLTSEPLGEDRDGKPVYLKDIWPSSQEIQAFIMKYVTRELYASKYADVFKGDANWQAVQVPAGQTYAWDD 638
Cdd:PTZ00092 566 AYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDE 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 639 QSTYVQNPPYFVGMGKTGSGLSDIRGARVLGLFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEV 718
Cdd:PTZ00092 646 KSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEV 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 719 MMRGTFANIRIRNHMLgpnGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAV 798
Cdd:PTZ00092 726 MVRGTFANIRLINKLC---GKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAV 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 799 IAQSFERIHRSNLVGMGVVPFVFEDGTTWASLDLKGDETVTIEGLEGDIKPREKkiARITYADGTVRDVplLCRIDTLDE 878
Cdd:PTZ00092 803 IAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQD--VTVKTDTGKTFDT--ILRIDTEVE 878
|
890
....*....|....*....
gi 1032825772 879 VTYMNNGGILQTVLRDLAA 897
Cdd:PTZ00092 879 VEYFKHGGILQYVLRKLVK 897
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
23-897 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1085.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 23 YYSLPkaeANGLAGVSKLPYSMKVLLENLLRFEDGRSVTKEHILSVAAWlSNKGTVENEIAYRPARVLMQDFTGVPAVVD 102
Cdd:PLN00070 63 YYSLP---ALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDW-ENTSPKQVEIPFKPARVLLQDFTGVPAVVD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 103 LAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFLKWGQQAFKNFRVVPPGTGI 182
Cdd:PLN00070 139 LACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 183 CHQVNLEYLGQTVWTKDEdgeiVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVIGFKLTGKLK 262
Cdd:PLN00070 219 VHQVNLEYLGRVVFNTDG----ILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 263 EGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAETVNYLTMSGREEQRIAL 342
Cdd:PLN00070 295 DGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAM 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 343 VEAYSKAQGMWRDGD--GSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAMEND-----YKKPGQLENR- 414
Cdd:PLN00070 375 IEAYLRANKMFVDYNepQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKvgfkgFAVPKEAQSKv 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 415 --YPVEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVGEYLAKSGLQADLD 492
Cdd:PLN00070 455 akFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLN 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 493 ALGFNLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVVAYALAGSVQKDLTS 572
Cdd:PLN00070 535 QQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEK 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 573 EPLGEDRDGKPVYLKDIWPSSQEIQAFIMKYVTRELYASKYADVFKGDANWQAVQVPAGQTYAWDDQSTYVQNPPYFVGM 652
Cdd:PLN00070 615 EPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNM 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 653 GKTGSGLSDIRGARVLGLFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEVMMRGTFANIRIRNH 732
Cdd:PLN00070 695 TMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNK 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 733 MLgpNGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLV 812
Cdd:PLN00070 775 LL--KGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLV 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 813 GMGVVPFVFEDGTTWASLDLKGDETVTIE--GLEGDIKPREKkiarITYADGTVRDVPLLCRIDTLDEVTYMNNGGILQT 890
Cdd:PLN00070 853 GMGIIPLCFKSGEDADTLGLTGHERYTIDlpSNISEIKPGQD----VTVTTDNGKSFTCTLRFDTEVELAYFDHGGILPY 928
|
....*..
gi 1032825772 891 VLRDLAA 897
Cdd:PLN00070 929 VIRNLIK 935
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
88-566 |
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: 737.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 88 RVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHSVIVDEFGTPTAFARNVELEYARNGERYRFLKWGQ 167
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 168 QAFKNFRVVPPGTGICHQVNLEYLGQTVWTKDEDGEIVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 247
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 248 LLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDaetv 327
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 328 nyltmsgreeqrialveayskaqgmwrdgdgsdlvfTDTLELDLGDVVPAMAGPKRPEGRIPLeniasgfasamendykk 407
Cdd:cd01586 237 ------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 408 pgqlenrypvegtdydlgHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVGEYLAKSGL 487
Cdd:cd01586 264 ------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEASGL 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032825772 488 QADLDALGFNLVGFGCTTCIGNSGPLPGPVSRTINDKGLIAAGVLSGNRNFEGRISPDVQANYLASPPLVVAYALAGSV 566
Cdd:cd01586 326 LPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
79-564 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 636.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 79 ENEIAYRPARVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKINPLVPVDLVIDHsvivdefgTPTAFARNVELEYARNGE 158
Cdd:pfam00330 13 DGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDH--------APDALDKNIEDEISRNKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 159 RYRFLKWGQQAFkNFRVVPPGTGICHQVNLEYLgqtvwtkdedgeiVAYPD-TCVGTDSHTTMINGLGVLGWGVGGIEAE 237
Cdd:pfam00330 85 QYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGGLGALAFGVGGSEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 238 AAMLGQPVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATC 317
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 318 GFFPVDAETVNYLTMSGREEQRIalVEAYSKAQGMWRDGDGSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPL-ENIASG 396
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLsELVPDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 397 FASAMENDYKKPGqleNRYPVEGTDYDLGHGDVAIAAITSCTNTSNPSVLIAAGLLArNAVAKGLKTKPWVKTSLAPGSQ 476
Cdd:pfam00330 309 FADAVKRKAAERA---LEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLK-KAVEKGLKVAPGVKASVVPGSE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 477 VVGEYLAKSGLQADLDALGFNLVGFGCTTCIGNSGPLPGpvsrtiNDkgliaAGVLSGNRNFEGRISPDVQAnYLASPPL 556
Cdd:pfam00330 385 VVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP------GE-----RCVSSSNRNFEGRQGPGGRT-HLASPAL 452
|
....*...
gi 1032825772 557 VVAYALAG 564
Cdd:pfam00330 453 VAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
670-842 |
4.33e-102 |
|
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: 314.21 E-value: 4.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 670 LFGDKITTDHISPAGSIKAASPAGSYLIGHGVGVADFNQYGTRRGNHEVMMRGTFANIRIRNHMLGpnGKEGGYTIHYPT 749
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVP--GTEGGTTHHPPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 750 KEEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWAS 829
Cdd:cd01580 79 GEVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADS 158
|
170
....*....|...
gi 1032825772 830 LDLKGDETVTIEG 842
Cdd:cd01580 159 LGLTGEETYDIIG 171
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
80-858 |
1.88e-85 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 286.66 E-value: 1.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 80 NEIAYRPARVLMQDFTGVPAVVDLAAMrdamvslgGDPEkinplVPVDLV---IDHSVIVDEFgtptafarnveleyaRN 156
Cdd:PRK07229 23 EEIAIRIDQTLTQDATGTMAYLQFEAM--------GLDR-----VKTELSvqyVDHNLLQADF---------------EN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 157 GERYRFLkwgQQAFKNFRVV--PPGTGICHQVNLE-YlgqtvwtkdedgeivAYP-DTCVGTDSHTT------MInglgv 226
Cdd:PRK07229 75 ADDHRFL---QSVAAKYGIYfsKPGNGICHQVHLErF---------------AFPgKTLLGSDSHTPtagglgML----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 227 lgwgvgGI-----EAEAAMLGQPVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLA 301
Cdd:PRK07229 132 ------AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 302 DRATIGNMGPEYGATCGFFPVDAETVNYLTMSGREEQRIALVEayskaqgmwrDgdgSDLVFTDTLELDLGDVVPAMAGP 381
Cdd:PRK07229 206 ERATITNMGAELGATTSIFPSDERTREFLKAQGREDDWVELLA----------D---PDAEYDEVIEIDLSELEPLIAGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 382 KRPEGRIPLENIAsgfasamendykkpgqlenrypveGTdydlghgDVAIAAITSCTNTSNPSVLIAAgllarnAVAKGL 461
Cdd:PRK07229 273 HSPDNVVPVSEVA------------------------GI-------KVDQVLIGSCTNSSYEDLMRAA------SILKGK 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 462 KTKPWVKTSLAPGSQVVGEYLAKSGLQADLDALGFNLVGFGCTTCIGNSG-PLPGPVS-RTIndkgliaagvlsgNRNFE 539
Cdd:PRK07229 316 KVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQaPATGNVSlRTF-------------NRNFP 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 540 GRiS--PDVQAnYLASPPLVVAYALAGsvqkDLTsEPLG-EDRDGKPVYLKDiwPssqeiqafimkyvtrELYASKYADV 616
Cdd:PRK07229 383 GR-SgtKDAQV-YLASPETAAASALTG----VIT-DPRTlALENGEYPKLEE--P---------------EGFAVDDAGI 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 617 FKGDANWQAVQVPAGQTyawddqstyVQNPPYFvgmgktgSGLSDIRGARVLGLFGDKITTDHISPAGSikaaspagsyl 696
Cdd:PRK07229 439 IAPAEDGSDVEVVRGPN---------IKPLPLL-------EPLPDLLEGKVLLKVGDNITTDHIMPAGA----------- 491
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 697 ighgvgvadfnqygtrrgnhEVMM-RGtfaNI-RIRNHMLGPngkeggytihyptkeemsiYDAA--MKYKEEGvPLVIF 772
Cdd:PRK07229 492 --------------------KWLPyRS---NIpNISEFVFEG-------------------VDNTfpERAKEQG-GGIVV 528
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 773 AGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWASLDLkgDETVTIEGLEGDIKPREK 852
Cdd:PRK07229 529 GGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEE--GDVLEIEDLREFLPGGPL 606
|
....*.
gi 1032825772 853 KIARIT 858
Cdd:PRK07229 607 TVVNVT 612
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
88-566 |
1.59e-77 |
|
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: 257.43 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 88 RVLMQDFTGVPAVVDLAAMrdamvslgGDPEKINPLVPVDLVIDHSVivdefgtptafarnvELEYARNGERYRFLKWGQ 167
Cdd:cd01351 1 RVMLQDATGPMAMKAFEIL--------AALGKVADPSQIACVHDHAV---------------QLEKPVNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 168 QAFKnFRVVPPGTGICHQVNLEYLgqtvwtkdedgeiVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 247
Cdd:cd01351 58 ALQG-IAFYRPGVGIIHQIMVENL-------------ALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 248 LLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAETV 327
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 328 NYLTMSGREEqrIALVEAYSKAQGMWRDGDGSDLVftdtLELDLGDVVPAMAGPKRPEGRIPLEniasgfasamendykk 407
Cdd:cd01351 204 KWLEATGRPL--LKNLWLAFPEELLADEGAEYDQV----IEIDLSELEPDISGPNRPDDAVSVS---------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 408 pgqlenrypvegtdyDLGHGDVAIAAITSCTNtSNPSVLIAAGllarnAVAKGLKTKPWVKTSLAPGSQVVGEYLAKSGL 487
Cdd:cd01351 262 ---------------EVEGTKIDQVLIGSCTN-NRYSDMLAAA-----KLLKGAKVAPGVRLIVTPGSRMVYATLSREGY 320
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032825772 488 QADLDALGFNLVGFGCTTCIGNSGPLPGPVsrtindkgliAAGVLSGNRNFEGRISPDVQANYLASPPLVVAYALAGSV 566
Cdd:cd01351 321 YEILVDSGARILPPGCGPCMGNGARLVADG----------EVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGKI 389
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-566 |
1.83e-52 |
|
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: 188.04 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 90 LMQDFTGVPAVVDLAAMrdamvslgGDPEkinplVPVDLV---IDHSVIVDEFgtptafarnveleyaRNGERYRFLkwg 166
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--------GVDR-----VRTELSvsyVDHNTLQTDF---------------ENADDHRFL--- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 167 QQAFKNFRVV--PPGTGICHQVNLEYLGqtvwtkdedgeivAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQP 244
Cdd:cd01585 53 QTVAARYGIYfsRPGNGICHQVHLERFA-------------VPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 245 VSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDA 324
Cdd:cd01585 120 YYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 325 ETVNYLTMSGREEQRIALVEayskaqgmwrdgdGSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIAsgfasamend 404
Cdd:cd01585 200 RTREFLAAQGREDDWVELAA-------------DADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREVA---------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 405 ykkpgqlenrypveGTDydlghgdVAIAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKPWVKTSLAPGSQVVGEYLAK 484
Cdd:cd01585 257 --------------GIK-------VDQVAIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAPGSKQVLEMLAR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 485 SGLQADLDALGFNLVGFGCTTCIG-NSGPLPGPVSrtindkgliaagVLSGNRNFEGRISPDVQANYLASPPLVVAYALA 563
Cdd:cd01585 310 NGALADLLAAGARILESACGPCIGmGQAPPTGGVS------------VRTFNRNFEGRSGTKDDLVYLASPEVAAAAALT 377
|
...
gi 1032825772 564 GSV 566
Cdd:cd01585 378 GVI 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
692-824 |
7.23e-47 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 163.31 E-value: 7.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 692 AGSYLIGHGVGVADFNQYGTRRGNHEVMMRGTFANIRIRNHMLgpNGKEGGYTIHYPTKEEMSIYDAAMKYKEEGVPLVI 771
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINF--EGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1032825772 772 FAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDG 824
Cdd:pfam00694 79 IGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
88-564 |
2.42e-44 |
|
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: 165.97 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 88 RVLMQDFTGVPAVVDLAAMRDAMVSlggDPEKInplvpVdLVIDHSVivdeFGTPTAFARNVEL--EYARngeryrflkw 165
Cdd:COG0065 30 LHLVHDVTSPQAFEGLREAGGRKVW---DPDRI-----V-AVFDHNV----PTKDPKSAEQVKTlrEFAK---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 166 gQQAFKNFRVVPPGtgICHQVNLEyLGQTVwtkdedgeivayP-DTCVGTDSHTTM----------INGLgvlgwgvggi 234
Cdd:COG0065 87 -EFGITFFDVGDPG--ICHVVLPE-QGLVL------------PgMTIVGGDSHTCThgafgafafgIGTT---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 235 EAEAAMLGQPVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYG 314
Cdd:COG0065 141 DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 315 ATCGFFPVDAETVNYLtmSGReeqrialveAYSKAQGMWRDGDGsdlVFTDTLELDLGDVVPAMAGPKRPEGRIPLENIA 394
Cdd:COG0065 221 AKAGIIAPDETTFEYL--KGR---------PFAPWRTLKSDEDA---VYDKEVEIDASDLEPQVAWPHSPDNVVPVSELE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 395 sgfasamendykkpgqlenrypvegtdydlghgDVAI--AAITSCTNtsnpSVL----IAAgllarnAVAKGLKTKPWVK 468
Cdd:COG0065 287 ---------------------------------GIKIdqVFIGSCTN----GRIedlrAAA------EILKGRKVAPGVR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 469 TSLAPGSQVVGEYLAKSGLQADLDALGFNLVGFGCTTCIGNSGplpgpvsrtindkGLIAAG---VLSGNRNFEGRI-SP 544
Cdd:COG0065 324 AIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNM-------------GVLAPGercASTSNRNFEGRMgSP 390
|
490 500
....*....|....*....|
gi 1032825772 545 DVQAnYLASPPLVVAYALAG 564
Cdd:COG0065 391 GSRT-YLASPATAAASAIAG 409
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
88-565 |
5.97e-44 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 164.54 E-value: 5.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 88 RVLMQDFTGvpavvdLAAMRDAMVSlgGDPEkinPLVPVDLVIDHsVIVDEFGTPTAFARNVELeyarNGERYRFL---- 163
Cdd:cd01584 1 RVAMQDATA------QMALLQFMSS--GLPK---VAVPSTIHCDH-LIEAQVGGEKDLKRAKDI----NKEVYDFLasag 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 164 -KWGQQAFKnfrvvpPGTGICHQVNLE-YlgqtvwtkdedgeivAYPDTC-VGTDSHTTMINGLGVLGWGVGGIEAEAAM 240
Cdd:cd01584 65 aKYGIGFWK------PGSGIIHQIVLEnY---------------AFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 241 LGQPVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFF 320
Cdd:cd01584 124 AGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 321 PVDAETVNYLTMSGREEqrIALVEAYSKAQGMWRDgdgSDLVFTDTLELDLGDVVPAMAGPKRPEGRIPLeniaSGFASA 400
Cdd:cd01584 204 PYNERMKKYLKATGRAE--IADLADEFKDDLLVAD---EGAEYDQLIEINLSELEPHINGPFTPDLATPV----SKFKEV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 401 MEndykkpgqlENRYPVegtdydlghgDVAIAAITSCTNTSNPSVLIAAGlLARNAVAKGLKTKpwVKTSLAPGSQVVGE 480
Cdd:cd01584 275 AE---------KNGWPL----------DLRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTITPGSEQIRA 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 481 YLAKSGLQADLDALGFNLVGFGCTTCIGNSgplpgpvSRTINDKGLIAAGVLSGNRNFEGRISPDVQA-NYLASPPLVVA 559
Cdd:cd01584 333 TIERDGLLQTFRDAGGIVLANACGPCIGQW-------DRKDIKKGEKNTIVTSYNRNFTGRNDANPAThAFVASPEIVTA 405
|
....*.
gi 1032825772 560 YALAGS 565
Cdd:cd01584 406 MAIAGT 411
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
88-566 |
5.90e-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: 5.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 88 RVLMQDFTGVPAVvdlAAMRDAMVSLGGDPEKINplvpvdLVIDHSVIvdefgTPTAFARNVELEYARNGERyrflkwgq 167
Cdd:cd01583 1 LHLVHDVTSPQAF---EGLREAGREKVWDPEKIV------AVFDHNVP-----TPDIKAAEQVKTLRKFAKE-------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 168 QAFKNFRVVppGTGICHQVnleyLGQTVWTKDedGEIVaypdtcVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 247
Cdd:cd01583 59 FGINFFDVG--RQGICHVI----LPEKGLTLP--GMTI------VGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 248 LLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAETV 327
Cdd:cd01583 125 RVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 328 NYLTMSGREEQRialvEAYSkaqgmwrDGDGsdlVFTDTLELDLGDVVPAMAGPKRPEGRIPLENiasgfasamendykk 407
Cdd:cd01583 205 EYLKGRGKAYWK----ELKS-------DEDA---EYDKVVEIDASELEPQVAWPHSPDNVVPVSE--------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 408 pgqlenrypVEGTDYDlghgdvaIAAITSCTNTSNPSVLIAAgllarnAVAKGLKTKPWVKTSLAPGSQVVGEYLAKSGL 487
Cdd:cd01583 256 ---------VEGIKID-------QVFIGSCTNGRLEDLRAAA------EILKGRKVADGVRLIVVPASQRVYKQAEKEGL 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032825772 488 QADLDALGFNLVGFGCTTCIGNSGPLPGPVSRtindkgliaaGVLSGNRNFEGRISPDVQANYLASPPLVVAYALAGSV 566
Cdd:cd01583 314 IEIFIEAGAEVRPPGCGACLGGHMGVLAPGER----------CVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
89-564 |
6.51e-38 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 147.25 E-value: 6.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 89 VLMQDFTGVPAVVDLAAMRDAMVSlggDPEKINplvpvdLVIDHSVivdefgtPtafARNVELEyarngERYRFL-KWG- 166
Cdd:PRK00402 31 VMAHDITGPLAIKEFEKIGGDKVF---DPSKIV------IVFDHFV-------P---AKDIKSA-----EQQKILrEFAk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 167 QQAFKNFRVVppGTGICHQVNLEYlgqtvwtkdedGEIVayP-DTCVGTDSHTT----------------Minglgvlgw 229
Cdd:PRK00402 87 EQGIPNFFDV--GEGICHQVLPEK-----------GLVR--PgDVVVGADSHTCtygalgafatgmgstdM--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 230 gvggieAEAAMLGQpVSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNM 309
Cdd:PRK00402 143 ------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 310 GPEYGATCGFFPVDAETVNYLTMSGREEQRIalveayskaqgMWRDGDGsdlVFTDTLELDLGDVVPAMAGPKRPEGRIP 389
Cdd:PRK00402 216 AIEAGAKAGIFAPDEKTLEYLKERAGRDYKP-----------WKSDEDA---EYEEVYEIDLSKLEPQVAAPHLPDNVKP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 390 LENiasgfasamendykkpgqlenrypVEGTDYDlghgdvaIAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKPWVKT 469
Cdd:PRK00402 282 VSE------------------------VEGTKVD-------QVFIGSCTNGRLEDLRIAAEIL------KGRKVAPGVRL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 470 SLAPGSQVVGEYLAKSGLQADLDALGFNLVGFGCTTCIGNSGplpgpvsrtindkGLIAAG--VLS-GNRNFEGRI-SPD 545
Cdd:PRK00402 325 IVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHM-------------GVLAPGevCLStTNRNFKGRMgSPE 391
|
490
....*....|....*....
gi 1032825772 546 VQAnYLASPPLVVAYALAG 564
Cdd:PRK00402 392 SEV-YLASPAVAAASAVTG 409
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
63-564 |
3.23e-35 |
|
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: 139.13 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 63 EHILSVAAWLSNKGtveNEIAYRPARVLM-QDFTGVPAvvdLAAMRDAMVSLGGDPEKINplvpvdLVIDHSVIVDEFGT 141
Cdd:TIGR02086 5 EKILSEKVGRPVCA---GEIVEVEVDLAMtHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNVPPPTVEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 142 ptAFARNVELEYARngeryrflkwgQQAFKNFRVvppGTGICHQVNLEylgqtvwtkdedgEIVAYP-DTCVGTDSHTTM 220
Cdd:TIGR02086 73 --AEMQKEIREFAK-----------RHGIKNFDV---GEGICHQILAE-------------EGYALPgMVVVGGDSHTCT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 221 INGLGVLGWGVGGIE-AEAAMLGQPVSMlLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMT 299
Cdd:TIGR02086 124 SGAFGAFATGMGATDmAIALATGKTWIK-VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 300 LADRATIGNMGPEYGATCGFFPVDAETVNYLTMSGREEQRIALVeayskaqgmwRDGDGsdlvFTDTLELDLGDVVPAMA 379
Cdd:TIGR02086 203 MDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRGLEFRILVP----------DPGAN----YYKEIEIDLSDLEPQVA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 380 GPKRPEGRIPLENiasgfasamendykkpgqlenrypVEGTDYDLghgdvaiAAITSCTNTSNPSVLIAAGLLarnavaK 459
Cdd:TIGR02086 269 VPHSVDNVKPVSD------------------------VEGTEIDQ-------VFIGSCTNGRLEDLRIAAEIL------K 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 460 GLKTKPWVKTSLAPGSQVVGEYLAKSGLQADLDALGFNLVGFGCTTCIG-NSGPL-PGPVSrtindkgliaagVLSGNRN 537
Cdd:TIGR02086 312 GRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGaHMGVLgDGEVC------------LSTTNRN 379
|
490 500
....*....|....*....|....*...
gi 1032825772 538 FEGRI-SPDVQAnYLASPPLVVAYALAG 564
Cdd:TIGR02086 380 FKGRMgSPNAEI-YLASPATAAASAVEG 406
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
97-566 |
3.18e-31 |
|
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: 127.18 E-value: 3.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 97 VPAVVDLAAMRD--------AMVSLGGD----PEKINplvpvdLVIDHSVivdefgtPtafARNVELEYARNgERYRFLK 164
Cdd:TIGR01343 21 IEAEIDLAMVHDitaplaikTLEEYGIDkvwnPEKIV------IVFDHQV-------P---ADTIKAAEMQK-LAREFVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 165 wgQQAFKNFRvvPPGTGICHQVNLEylgqtvwtkdedGEIVAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQP 244
Cdd:TIGR01343 84 --KQGIKYFY--DVGEGICHQVLPE------------KGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 245 VSMLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDA 324
Cdd:TIGR01343 148 TWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 325 ETVNYLTMSGREEQRIAlveayskaqgmwrDGDgSDLVFTDTLELDLGDVVPAMAGPKRPegripleniasgfasamend 404
Cdd:TIGR01343 228 KTIQYLKERRKEPFRVY-------------KSD-EDAEYAKEIEIDASQIEPVVACPHNV-------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 405 ykkpgqlENRYPVEGTDydlgHGDVAIAAITSCTNTSNPSVLIAAGLLarnavaKGLKTKPWVKTSLAPGSQVVGEYLAK 484
Cdd:TIGR01343 274 -------DNVKPVSEVE----GTEIDQVFIGSCTNGRLEDLRVAAKIL------KGRKVAPDVRLIVIPASRAVYLQALK 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 485 SGLQADLDALGFNLVGFGCTTCIG-NSGPL-PGPVSrtindkgliaagVLSGNRNFEGRI-SPDVQAnYLASPPLVVAYA 561
Cdd:TIGR01343 337 EGLIEIFVKAGAVVSTPGCGPCLGsHQGVLaPGEVC------------ISTSNRNFKGRMgHPNAEI-YLASPATAAASA 403
|
....*
gi 1032825772 562 LAGSV 566
Cdd:TIGR01343 404 VKGYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
88-564 |
9.74e-24 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 105.76 E-value: 9.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 88 RVLMQDFTGVPAVVDLAAmRDAMVSlggDPEKInpLVPVDLVIDHSVIVDEFGTPTAFARNVElEYARNGERYrflkwgq 167
Cdd:PRK12466 30 RHLLNEYTSPQAFSGLRA-RGRTVR---RPDLT--LAVVDHVVPTRPGRDRGITDPGGALQVD-YLRENCADF------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 168 qAFKNFRVVPPGTGICHQVNLEyLGqtvwtkdedgeiVAYPD-TCVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVS 246
Cdd:PRK12466 96 -GIRLFDVDDPRQGIVHVVAPE-LG------------LTLPGmVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 247 MLLPEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAET 326
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 327 VNYLtmSGREeqRIALVEAYSKAQGMWR----DGDGsdlVFTDTLELDLGDVVPAMAGPKRPE------GRIPLENIAS- 395
Cdd:PRK12466 242 FDYL--RGRP--RAPKGALWDAALAYWRtlrsDADA---VFDREVEIDAADIAPQVTWGTSPDqavpitGRVPDPAAEAd 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 396 -GFASAMEN--DYK--KPGQlenryPVEGTDYDLghgdvaiAAITSCTNtSNPSVLIAAGllarnAVAKGLKTKPWVKTS 470
Cdd:PRK12466 315 pARRAAMERalDYMglTPGT-----PLAGIPIDR-------VFIGSCTN-GRIEDLRAAA-----AVLRGRKVAPGVRAM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 471 LAPGSQVVGEYLAKSGLQADLDALGFNLVGFGCTTCIGNSGPLPGPVSRTINdkgliaagvlSGNRNFEGRISPDVQAnY 550
Cdd:PRK12466 377 VVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCAS----------TTNRNFEGRQGPGART-H 445
|
490
....*....|....
gi 1032825772 551 LASPPLVVAYALAG 564
Cdd:PRK12466 446 LMSPAMVAAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
177-566 |
7.14e-23 |
|
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: 101.54 E-value: 7.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 177 PPGTGICHQVNLEylgqtvwtkdedgEIVAYPDT-CVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLLPEVIGF 255
Cdd:cd01582 64 PAGRGIGHQIMIE-------------EGYAFPGTlAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 256 KLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAEtvnyltmsgr 335
Cdd:cd01582 131 ELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK---------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 336 eeqrialveayskaqgmwrdgdgsdlvftdTLELDLGDVVPAMAGPkrpegripleniasgfasamendykkpgqleNRY 415
Cdd:cd01582 201 ------------------------------HLILDLSTLSPYVSGP-------------------------------NSV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 416 PVEGTDYDLGHGDVAI--AAITSCTNtSNPSVLIAAGLLARNAVAKGLKTK--PWVKTSLAPGSQVVGEYLAKSGLQADL 491
Cdd:cd01582 220 KVSTPLKELEAQNIKInkAYLVSCTN-SRASDIAAAADVVKGKKEKNGKIPvaPGVEFYVAAASSEVQAAAEKNGDWQTL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032825772 492 DALGFNLVGFGCTTCIGNSGPL--PGPVsrtindkgliaaGVLSGNRNFEGRI-SPDVQAnYLASPPLVVAYALAGSV 566
Cdd:cd01582 299 LEAGATPLPAGCGPCIGLGQGLlePGEV------------GISATNRNFKGRMgSTEALA-YLASPAVVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
256-566 |
2.98e-19 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 91.72 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 256 KLTGKLKEGVTATDLVLMVVQMLRKKGVVSKFVEFFGPGLDNMTLADRATIGNMGPEYGATCGFFPVDAETVNYLtmSGR 335
Cdd:PRK05478 169 EVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYL--KGR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 336 EeqRIALVEAYSKAQGMWR----DgdgSDLVFTDTLELDLGDVVPAMAGPKRPE------GRIP-LENIASGFA-SAMEN 403
Cdd:PRK05478 247 P--FAPKGEDWDKAVAYWKtlksD---EDAVFDKVVTLDAADIEPQVTWGTNPGqvisidGKVPdPEDFADPVKrASAER 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 404 DYK----KPGQlenryPVEGTDYDlghgdvaIAAITSCTNtSNPSVLIAAGllarnAVAKGLKTKPWVKTSLAPGSQVVG 479
Cdd:PRK05478 322 ALAymglKPGT-----PITDIKID-------KVFIGSCTN-SRIEDLRAAA-----AVVKGRKVAPGVRALVVPGSGLVK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 480 EYLAKSGLQADLDALGFNLVGFGCTTCIG-NsgplpgpvsrtiNDKglIAAGVLSG---NRNFEGRispdvQAN----YL 551
Cdd:PRK05478 384 AQAEAEGLDKIFIEAGFEWREPGCSMCLAmN------------PDK--LPPGERCAstsNRNFEGR-----QGKggrtHL 444
|
330
....*....|....*
gi 1032825772 552 ASPPLVVAYALAGSV 566
Cdd:PRK05478 445 VSPAMAAAAAITGHF 459
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
672-836 |
4.36e-18 |
|
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: 80.94 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 672 GDKITTDHISPAGSikaaspagsylighgvgvadfnQYGTRRGNHEVMMRGTFanirirnHMLGPNgkeggytihYPTKe 751
Cdd:cd01579 3 GDNITTDHIMPAGA----------------------KVLPLRSNIPAISEFVF-------HRVDPT---------FAER- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 752 emsiydaamkyKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWASLD 831
Cdd:cd01579 44 -----------AKAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFE 112
|
....*
gi 1032825772 832 LkGDE 836
Cdd:cd01579 113 Q-GDQ 116
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
768-836 |
2.70e-16 |
|
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: 74.81 E-value: 2.70e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032825772 768 PLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWASLDLkGDE 836
Cdd:cd00404 16 PGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHT-GDE 83
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
674-844 |
4.72e-15 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 73.27 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 674 KITTDHISPAGsikaasPAGSYlighgvgvadfnqygtrrgnhevmmRGTFANIRiRNHMLGPNGKEGGYT---IHYPTK 750
Cdd:cd01578 5 KCTTDHISAAG------PWLKY-------------------------RGHLDNIS-NNLLIGAINAENGKAnsvKNQVTG 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 751 EEMSIYDAAMKYKEEGVPLVIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWASL 830
Cdd:cd01578 53 EYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKI 132
|
170
....*....|....
gi 1032825772 831 DlkGDETVTIEGLE 844
Cdd:cd01578 133 H--PDDKVDILGLT 144
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
770-823 |
1.17e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 58.28 E-value: 1.17e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1032825772 770 VIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFED 823
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEE 105
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
250-495 |
1.88e-08 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 58.10 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 250 PEVIGFKLTGKLKEGVTATDLVLMVVQMLRKKGVV-SKFVEFFGPGLDNMTLADRATIGNMGPEygATC--GFFPVDAET 326
Cdd:PRK11413 183 PGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQTDEEV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 327 VNYLTMSGREeqrialvEAYS--KAQGM-WRDGdgsdlvftdTLELDLGDVVPAMAGPKRPEGRIPLENIASGFASAMEN 403
Cdd:PRK11413 261 HNWLALHGRG-------QDYCelNPQPMaYYDG---------CISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILRE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032825772 404 DYKKPGQLENrypvEGTDYDL------GHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTkpwvkTSLAPGSQV 477
Cdd:PRK11413 325 VEIESERVAH----GKAKLSLldkienGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFS-----LSVYPSSQP 395
|
250
....*....|....*...
gi 1032825772 478 VGEYLAKSGLQADLDALG 495
Cdd:PRK11413 396 VFMDLAKKGVVADLMGAG 413
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
770-840 |
3.57e-08 |
|
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: 51.82 E-value: 3.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032825772 770 VIFAGVEYGNGSSR---DWAAKGtnlLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWASLDLKGDEtVTI 840
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE-VEV 89
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
770-836 |
6.51e-06 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 47.13 E-value: 6.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032825772 770 VIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVpfVFEDGTTWASLDlKGDE 836
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLP--VLECDEAVDKIE-DGDE 114
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
770-847 |
1.18e-03 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 41.77 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032825772 770 VIFAGVEYGNGSSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVVPFVFEDGTTWAslDLKGDETVTIEgLEGDI 847
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGEVYPLESEVRICE--ECKTGDVVTVE-LGNSV 206
|
|
| |
