|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-913 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1759.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 1 MPSVNSLNTLKTLQVGDKTYHYFSLPDA-AKSLGELDKLPMSLKVLLENLLRWEDEKTVTGADLKALAAWLKERRSDREI 79
Cdd:PRK09277 1 MSSTDSFKARKTLEVGGKSYDYYSLRALeAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 80 QYRPARVLMQDFTGVPAVVDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAF 159
Cdd:PRK09277 81 PFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 160 LRWGQSAFDNFSVVPPGTGICHQVNLEYLGRTVWTKdEDGRTYAFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
Cdd:PRK09277 161 LKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTR-EDGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 240 QPVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPV 319
Cdd:PRK09277 240 QPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 320 DEVTLEYLRLSGRPSDTVKLVEAYSKAQGLWRLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVAQAFSDFIDL 399
Cdd:PRK09277 320 DEETLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 400 QFKPTSKEEgrleseggggvavgnadlageasyEHEGQSHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKGLK 479
Cdd:PRK09277 400 GVQGFGLDE------------------------AEEGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 480 RKPWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEGRV 559
Cdd:PRK09277 456 VKPWVKTSLAPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRI 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 560 HPLVKTNWLASPPLVVAYALAGTVRTDLSREPLGEDPHGKPVYLRDIWPSSQEIADAVNQ-VNTSMFHKEYAEVFAGDEQ 638
Cdd:PRK09277 536 HPLVKANYLASPPLVVAYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKaVKPEMFRKEYADVFEGDER 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 639 WQAIEVPQAATYVWQDDSTYIQHPPFFDDIDGPPPVVKDVAGARVLALLGDSVTTDHISPAGNIKADSPAGQYLRDKGVE 718
Cdd:PRK09277 616 WNAIEVPEGPLYDWDPDSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVE 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 719 PKDFNSYGSRRGNHEVMMRGTFANIRIRNEMLGGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRD 798
Cdd:PRK09277 696 PKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRD 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 799 WAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDILGLSgvELTPRMNLTLVITREDGS 878
Cdd:PRK09277 776 WAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLE--DLKPGATVTVVITRADGE 853
|
890 900 910
....*....|....*....|....*....|....*
gi 1086084978 879 REKIEVLCRIDTLNEVEYFKSGGILHYVLRQLIAS 913
Cdd:PRK09277 854 VVEFPVLCRIDTAVEVDYYRNGGILQYVLRDLLAS 888
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-913 |
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: 1729.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 3 SVNSLNTLKTLQVGDKTYHYFSLPDAAKSLGELDKLPMSLKVLLENLLRWEDEKTVTGADLKALAAWLKERRSDREIQYR 82
Cdd:COG1048 1 SMDSFKARKTLTVGGKPYTYYSLPALEEAGGDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 83 PARVLMQDFTGVPAVVDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAFLRW 162
Cdd:COG1048 81 PARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 163 GQSAFDNFSVVPPGTGICHQVNLEYLGRTVWTKDEDGRTYAFPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPV 242
Cdd:COG1048 161 GQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 243 SMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEV 322
Cdd:COG1048 241 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 323 TLEYLRLSGRPSDTVKLVEAYSKAQGLWRLPGQ-EPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVAQAFSDFIDLQF 401
Cdd:COG1048 321 TLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDApEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 402 KPtskeegrleseggggvavgnaDLAGEASYEHEGQSHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKGLKRK 481
Cdd:COG1048 401 GE---------------------ELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 482 PWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEGRVHP 561
Cdd:COG1048 460 PWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 562 LVKTNWLASPPLVVAYALAGTVRTDLSREPLGEDPHGKPVYLRDIWPSSQEIADAVNQ-VNTSMFHKEYAEVFAGDEQWQ 640
Cdd:COG1048 540 DVKANFLASPPLVVAYALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKaVTPEMFRARYADVFDGDERWQ 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 641 AIEVPQAATYVWQDDSTYIQHPPFFDDIDGPPPVVKDVAGARVLALLGDSVTTDHISPAGNIKADSPAGQYLRDKGVEPK 720
Cdd:COG1048 620 ALEVPAGELYDWDPDSTYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPK 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 721 DFNSYGSRRGNHEVMMRGTFANIRIRNEMLGGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRDWA 800
Cdd:COG1048 700 DFNSYGSRRGNHEVMMRGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWA 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 801 AKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDILGLSGvELTPRMNLTLVITREDGSRE 880
Cdd:COG1048 780 AKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDE-GLAPGKTVTVTATRADGSTE 858
|
890 900 910
....*....|....*....|....*....|...
gi 1086084978 881 KIEVLCRIDTLNEVEYFKSGGILHYVLRQLIAS 913
Cdd:COG1048 859 EFPVLHRIDTPVEVEYYRAGGILQYVLRQLLAA 891
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
2-912 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1656.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 2 PSVNSLNTLKTLQVGDKTYHYFSLPDAAKSLGE-LDKLPMSLKVLLENLLRWEDEKTVTGADLKALAAWLKERRSDREIQ 80
Cdd:PRK12881 1 MAHNLHKTLKEFDVGGKTYKFYSLPALGKELGGdLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 81 YRPARVLMQDFTGVPAVVDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAFL 160
Cdd:PRK12881 81 FVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 161 RWGQSAFDNFSVVPPGTGICHQVNLEYLGRTVWTKDEDGRTYAFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ 240
Cdd:PRK12881 161 KWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 241 PVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVD 320
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 321 EVTLEYLRLSGRPSDTVKLVEAYSKAQGLWRLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVAQAFSDFIDlq 400
Cdd:PRK12881 321 EQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFS-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 401 fkptskeegrleseggggvavgnaDLAGEASYEHEGQ---SHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKG 477
Cdd:PRK12881 399 ------------------------KPVAENGFAKKAQtsnGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 478 LKRKPWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEG 557
Cdd:PRK12881 455 LTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 558 RVHPLVKTNWLASPPLVVAYALAGTVRTDLSREPLGEDPHGKPVYLRDIWPSSQEIADAV-NQVNTSMFHKEYAEVFAGD 636
Cdd:PRK12881 535 RIHPNIKANFLASPPLVVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVaFAVDPEDFRKNYAEVFKGS 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 637 EQWQAIEVPQAATYVWQDDSTYIQHPPFFDDIDGPPPVVKDVAGARVLALLGDSVTTDHISPAGNIKADSPAGQYLRDKG 716
Cdd:PRK12881 615 ELWAAIEAPDGPLYDWDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENG 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 717 VEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMLGGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIAGQEYGTGSS 796
Cdd:PRK12881 695 VPKADFNSYGSRRGNHEVMMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSS 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 797 RDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDILGLSGvELTPRMNLTLVITRED 876
Cdd:PRK12881 775 RDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPG-EIKPRQDVTLVIHRAD 853
|
890 900 910
....*....|....*....|....*....|....*.
gi 1086084978 877 GSREKIEVLCRIDTLNEVEYFKSGGILHYVLRQLIA 912
Cdd:PRK12881 854 GSTERVPVLCRIDTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
18-911 |
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: 1375.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 18 KTYHYFSLPDAAKSLGELDKLPMSLKVLLENLLRWEDEKTVTGADLKALAAWLKERRSDREIQYRPARVLMQDFTGVPAV 97
Cdd:TIGR01341 1 KTYYYYSLKALEESGGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 98 VDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAFLRWGQSAFDNFSVVPPGT 177
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 178 GICHQVNLEYLGRTVWTKDEDGRTYAFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGFKLTGK 257
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 258 LKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTLEYLRLSGRPSDTV 337
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 338 KLVEAYSKAQGLWRLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVAQAFSDFIDlqfKPTSKEEGRLESEGGg 417
Cdd:TIGR01341 321 ELVEKYARAQGLFYDDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELE---KNGGDKGFTLRKEPL- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 418 gvavgnadlageaSYEHEGQSHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKGLKRKPWVKSSLAPGSKVVTD 497
Cdd:TIGR01341 397 -------------KKKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 498 YYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEGRVHPLVKTNWLASPPLVVAY 577
Cdd:TIGR01341 464 YLAESGLLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAY 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 578 ALAGTVRTDLSREPLGEDPHGKPVYLRDIWPSSQEIADAVNQ-VNTSMFHKEYAEVFAGDEQWQAIEVPQAATYVWQDDS 656
Cdd:TIGR01341 544 ALAGNIDINLYTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMaVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKS 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 657 TYIQHPPFFDDIDGPPPVVKDVAGARVLALLGDSVTTDHISPAGNIKADSPAGQYLRDKGVEPKDFNSYGSRRGNHEVMM 736
Cdd:TIGR01341 624 TYIRLPPFFEEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMM 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 737 RGTFANIRIRNEMLGGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAES 816
Cdd:TIGR01341 704 RGTFANIRIKNLMVKGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAES 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 817 FERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDILGLSgvELTPRMNLTLVITREDGSREKIEVLCRIDTLNEVEY 896
Cdd:TIGR01341 784 FERIHRSNLVGMGVIPLQFPQGEDAETLGLTGDETIDIDGIK--DLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDY 861
|
890
....*....|....*
gi 1086084978 897 FKSGGILHYVLRQLI 911
Cdd:TIGR01341 862 YKHGGILQYVLRKFL 876
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
10-913 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1318.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 10 LKTLQVGdKTYHYFSLPDAAKSlgELDKLPMSLKVLLENLLRWEDEKTVTGADLKALAAWLKERRSDREIQYRPARVLMQ 89
Cdd:PTZ00092 20 LKTLKDG-GSYKYYSLNELHDP--RLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPARVLLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 90 DFTGVPAVVDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAFLRWGQSAFDN 169
Cdd:PTZ00092 97 DFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSKAFKN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 170 FSVVPPGTGICHQVNLEYLGRTVWtkDEDGRTYafPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEV 249
Cdd:PTZ00092 177 LLIVPPGSGIVHQVNLEYLARVVF--NKDGLLY--PDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 250 IGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTLEYLRL 329
Cdd:PTZ00092 253 VGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 330 SGRPSDTVKLVEAYSKAQGLWRLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVAQafsDFIDLQFKPTSKEEG 409
Cdd:PTZ00092 333 TGRSEEKVELIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKK---DFTACLSAPVGFKGF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 410 RLESEggggvavgnaDLAGEASYEHEGQSHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKGLKRKPWVKSSLA 489
Cdd:PTZ00092 410 GIPEE----------KHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 490 PGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEGRVHPLVKTNWLA 569
Cdd:PTZ00092 480 PGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 570 SPPLVVAYALAGTVRTDLSREPLGEDPHGKPVYLRDIWPSSQEIADAVNQ-VNTSMFHKEYAEVFAGDEQWQAIEVPQAA 648
Cdd:PTZ00092 560 SPPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKyVKPEMFKEVYSNITQGNKQWNELQVPKGK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 649 TYVWQDDSTYIQHPPFFDDIDGPPPVVKDVAGARVLALLGDSVTTDHISPAGNIKADSPAGQYLRDKGVEPKDFNSYGSR 728
Cdd:PTZ00092 640 LYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGAR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 729 RGNHEVMMRGTFANIRIRNEMLgGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRDWAAKGTNLLG 808
Cdd:PTZ00092 720 RGNDEVMVRGTFANIRLINKLC-GKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQG 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 809 VKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDILGLSGvELTPrmNLTLVITREDGSreKIEVLCRI 888
Cdd:PTZ00092 799 VKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSG-ELKP--GQDVTVKTDTGK--TFDTILRI 873
|
890 900
....*....|....*....|....*
gi 1086084978 889 DTLNEVEYFKSGGILHYVLRQLIAS 913
Cdd:PTZ00092 874 DTEVEVEYFKHGGILQYVLRKLVKG 898
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
22-913 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1115.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 22 YFSLPdaAKSLGELDKLPMSLKVLLENLLRWEDEKTVTGADLKALAAWLKERRSDREIQYRPARVLMQDFTGVPAVVDLA 101
Cdd:PLN00070 63 YYSLP--ALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKPARVLLQDFTGVPAVVDLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 102 AMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAFLRWGQSAFDNFSVVPPGTGICH 181
Cdd:PLN00070 141 CMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 182 QVNLEYLGRTVWTKDedgrTYAFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGFKLTGKLKEG 261
Cdd:PLN00070 221 QVNLEYLGRVVFNTD----GILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 262 ITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTLEYLRLSGRPSDTVKLVE 341
Cdd:PLN00070 297 VTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 342 AYSKAQGL---WRLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVAQAFSDFID--LQFK--PTSKEEgrlese 414
Cdd:PLN00070 377 AYLRANKMfvdYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDnkVGFKgfAVPKEA------ 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 415 ggggvavgnADLAGEASYEheGQSHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKGLKRKPWVKSSLAPGSKV 494
Cdd:PLN00070 451 ---------QSKVAKFSFH--GQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGV 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 495 VTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEGRVHPLVKTNWLASPPLV 574
Cdd:PLN00070 520 VTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLV 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 575 VAYALAGTVRTDLSREPLGEDPHGKPVYLRDIWPSSQEIADAV-NQVNTSMFHKEYAEVFAGDEQWQAIEVPQAATYVWQ 653
Cdd:PLN00070 600 VAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVqSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWD 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 654 DDSTYIQHPPFFDDIDGPPPVVKDVAGARVLALLGDSVTTDHISPAGNIKADSPAGQYLRDKGVEPKDFNSYGSRRGNHE 733
Cdd:PLN00070 680 PKSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDE 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 734 VMMRGTFANIRIRNEMLGGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVI 813
Cdd:PLN00070 760 IMARGTFANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVI 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 814 AESFERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDILGLSGV-ELTPRMNLTlVITreDGSREKIEVLcRIDTLN 892
Cdd:PLN00070 840 AKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNIsEIKPGQDVT-VTT--DNGKSFTCTL-RFDTEV 915
|
890 900
....*....|....*....|.
gi 1086084978 893 EVEYFKSGGILHYVLRQLIAS 913
Cdd:PLN00070 916 ELAYFDHGGILPYVIRNLIKQ 936
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
85-583 |
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: 722.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 85 RVLMQDFTGVPAVVDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSVMVDKFASSSAFEQNVDIEMQRNGERYAFLRWGQ 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 165 SAFDNFSVVPPGTGICHQVNLEYLGRTVWTKDEDGRTYAFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 245 LIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDevtl 324
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 325 eylrlsgrpsdtvklveayskaqglwrlpgqepvfTDSLALDMGSVEASLAGPKRPQDRVALpsvaqafsdfidlqfkpt 404
Cdd:cd01586 237 -----------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL------------------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 405 skeegrleseggggvavgnadlageasyehegqshplkHGAVVIAAITSCTNTSNPSVMMAAGLVAKKAVEKGLKRKPWV 484
Cdd:cd01586 264 --------------------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 485 KSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAADLTVASVLSGNRNFEGRVHPLVK 564
Cdd:cd01586 306 KTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVR 385
|
490
....*....|....*....
gi 1086084978 565 TNWLASPPLVVAYALAGTV 583
Cdd:cd01586 386 ANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
73-581 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 629.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 73 RRSDREIQYRPARVLMQDFTGVPAVVDLAAMRAAMAKAGGDPQRINPLSPVDLVIDHSvmvdkfasSSAFEQNVDIEMQR 152
Cdd:pfam00330 10 EELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 153 NGERYAFLRWGQSAFdNFSVVPPGTGICHQVNLEYLgrtvwtkdedgrtYAFPD-TLVGTDSHTTMINglgvlgwgvggI 231
Cdd:pfam00330 82 NKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGglgalafgvggS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 232 EAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYG 311
Cdd:pfam00330 148 EAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 312 ATCGFFPVDEVTLEYLRLSGRPSdtVKLVEAYSKAQGLWRLPGQE-PVFTDSLALDMGSVEASLAGPKRPQDRVALpsva 390
Cdd:pfam00330 228 ATAGLFPPDETTFEYLRATGRPE--APKGEAYDKAVAWKTLASDPgAEYDKVVEIDLSTIEPMVTGPTRPQDAVPL---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 391 qafSDFIDLQFKPTSKEEGRLESeggggvavgnadlageASYEHEGQSHPLKHGAVVIAAITSCTNTSNPSVMMAAGLVa 470
Cdd:pfam00330 302 ---SELVPDPFADAVKRKAAERA----------------LEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 471 KKAVEKGLKRKPWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPiekaiqaadltVASVLS 550
Cdd:pfam00330 362 KKAVEKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPG-----------ERCVSS 430
|
490 500 510
....*....|....*....|....*....|.
gi 1086084978 551 GNRNFEGRVHPLVKTnWLASPPLVVAYALAG 581
Cdd:pfam00330 431 SNRNFEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
686-856 |
8.02e-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: 345.42 E-value: 8.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 686 LLGDSVTTDHISPAGNIKADSPAGQYLRDKGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMLGGEEGGNTYYIPTME 765
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 766 KMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLN 845
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|.
gi 1086084978 846 LKGTESIDILG 856
Cdd:cd01580 161 LTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-583 |
1.51e-80 |
|
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: 265.90 E-value: 1.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 85 RVLMQDFTGVPAVVDLAAmraamakaGGDPQRINPLSPVDLVIDHSVMVDKfasssafeqnvdiemQRNGERYAFLRWGq 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEI--------LAALGKVADPSQIACVHDHAVQLEK---------------PVNNEGHKFLSFF- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 165 SAFDNFSVVPPGTGICHQVNLEYLGRtvwtkdedgrtyaFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSM 244
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENLAL-------------PGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 245 LIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTL 324
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 325 EYLRLSGRPsDTVKLVEAYSKAQglwrLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRVALPSVaqafsdfidlqfkpt 404
Cdd:cd01351 204 KWLEATGRP-LLKNLWLAFPEEL----LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEV--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 405 skeegrleseggggvavgnadlageasyehegqshplKHGAVVIAAITSCTNtSNPSVMMAAGLVAKKAvekglKRKPWV 484
Cdd:cd01351 264 -------------------------------------EGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGV 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 485 KSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKaiqaadltvaSVLSGNRNFEGRVHPLVK 564
Cdd:cd01351 301 RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEV----------GVSSGNRNFPGRLGTYER 370
|
490
....*....|....*....
gi 1086084978 565 TNWLASPPLVVAYALAGTV 583
Cdd:cd01351 371 HVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
78-910 |
1.91e-80 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 273.56 E-value: 1.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 78 EIQYRPARVLMQDFTGVPAVVDLAAMraamakagGDPQRINPLSpvdlV--IDHsvmvdkfasssafeqNVDIEMQRNGE 155
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAM--------GLDRVKTELS----VqyVDH---------------NLLQADFENAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 156 RYAFLrwgQSAFDNFSVV--PPGTGICHQVNLEylgrtvwtkdedgrTYAFP-DTLVGTDSHTT------MInglgvlgw 226
Cdd:PRK07229 77 DHRFL---QSVAAKYGIYfsKPGNGICHQVHLE--------------RFAFPgKTLLGSDSHTPtagglgML-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 227 gvgGI-----EAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRA 301
Cdd:PRK07229 132 ---AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 302 TIANMAPEYGATCGFFPVDEVTLEYLRLSGRPSDTVKLveayskaqglwrLPGQEPVFTDSLALDMGSVEASLAGPKRPq 381
Cdd:PRK07229 209 TITNMGAELGATTSIFPSDERTREFLKAQGREDDWVEL------------LADPDAEYDEVIEIDLSELEPLIAGPHSP- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 382 DRVAlpsvaqafsdfidlqfkPTSkeegrleseggggvavgnaDLAGEasyehegqshplkhgAVVIAAITSCTNTSNPS 461
Cdd:PRK07229 276 DNVV-----------------PVS-------------------EVAGI---------------KVDQVLIGSCTNSSYED 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 462 VMMAAGLVakkaveKGLKRKPWVKSSLAPGSKVVtdYYKAA--GLTKYLDELGFALVGYGCTTCIGNSGplpEPIEKAIq 539
Cdd:PRK07229 305 LMRAASIL------KGKKVHPKVSLVINPGSRQV--LEMLArdGALADLIAAGARILENACGPCIGMGQ---APATGNV- 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 540 aadltvaSVLSGNRNFEGR-------VhplvktnWLASPPLVVAYALAGTV---RTDlsreplgEDPHGKPVYLRDiwPS 609
Cdd:PRK07229 373 -------SLRTFNRNFPGRsgtkdaqV-------YLASPETAAASALTGVItdpRTL-------ALENGEYPKLEE--PE 429
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 610 SQEiadavnqVNTSMFhkeyaevFAGDEQWQAIEVPQAATyvwqddstyIQHPPFFDdidgPPPvvkDVAGARVLALLGD 689
Cdd:PRK07229 430 GFA-------VDDAGI-------IAPAEDGSDVEVVRGPN---------IKPLPLLE----PLP---DLLEGKVLLKVGD 479
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 690 SVTTDHISPAGNikadspagQYLRdkgvepkdfnsygsrrgnhevmMRGtfaNI-RIRNEMLGGEEggNTYYiptmekmp 768
Cdd:PRK07229 480 NITTDHIMPAGA--------KWLP----------------------YRS---NIpNISEFVFEGVD--NTFP-------- 516
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 769 iydaaMRYQASGtPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQF-------KLDQNr 841
Cdd:PRK07229 517 -----ERAKEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFadpadydKIEEG- 589
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1086084978 842 kslnlkgtESIDILGLSgvELTPRMNLTLVITREDgsrEKIEVlcrIDTLNE--VEYFKSGGILHYVLRQL 910
Cdd:PRK07229 590 --------DVLEIEDLR--EFLPGGPLTVVNVTKD---EEIEV---RHTLSErqIEILLAGGALNLIKKKL 644
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
708-836 |
1.80e-55 |
|
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: 187.57 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 708 AGQYLRDKGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMLGGEEGGNTYYIPTMEKMPIYDAAMRYQASGTPLVVIA 787
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1086084978 788 GQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFK 836
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFP 129
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
152-583 |
1.61e-45 |
|
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: 168.40 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 152 RNGERYAFLrwgQSAFDNFSVV--PPGTGICHQVNLEYLGRTvwtkdedGRTyafpdtLVGTDSHTTMINGLGVLGWGVG 229
Cdd:cd01585 44 ENADDHRFL---QTVAARYGIYfsRPGNGICHQVHLERFAVP-------GKT------LLGSDSHTPTAGGLGMLAIGAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 230 GIEAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPE 309
Cdd:cd01585 108 GLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 310 YGATCGFFPVDEVTLEYLRLSGRPSDTVKLveayskaqglwrLPGQEPVFTDSLALDMGSVEASLAGPKRPqDRVAlpsv 389
Cdd:cd01585 188 LGATTSIFPSDERTREFLAAQGREDDWVEL------------AADADAEYDEEIEIDLSELEPLIARPHSP-DNVV---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 390 aqafsdfidlqfkpTSKEEGRLEseggggvavgnadlageasyehegqshplkhgaVVIAAITSCTNTSNPSVMMAAGLV 469
Cdd:cd01585 251 --------------PVREVAGIK---------------------------------VDQVAIGSCTNSSYEDLMTVAAIL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 470 AKKAVEkglkrkPWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSgplpepiekaiQAADLTVASVL 549
Cdd:cd01585 284 KGRRVH------PHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMG-----------QAPPTGGVSVR 346
|
410 420 430
....*....|....*....|....*....|....
gi 1086084978 550 SGNRNFEGRVHPLVKTNWLASPPLVVAYALAGTV 583
Cdd:cd01585 347 TFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
113-583 |
9.44e-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: 157.35 E-value: 9.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 113 DPQRINplspvdLVIDHSVmvdkfasssaFEQNVDIEMQRNGERYAFLRWGQSAFDnfsvvPPGTGICHQVNLEyLGRTV 192
Cdd:cd01583 26 DPEKIV------AVFDHNV----------PTPDIKAAEQVKTLRKFAKEFGINFFD-----VGRQGICHVILPE-KGLTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 193 wtkdedgrtyafP-DTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTV 271
Cdd:cd01583 84 ------------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 272 TQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTLEYLRlsGRPSDTVKLVEAYSKAqglwr 351
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLK--GRGKAYWKELKSDEDA----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 352 lpgqepVFTDSLALDMGSVEaslagpkrpqdrvalPSVAqafsdfidlqfKPTSKEEGRLESEGGggvavgnadlageas 431
Cdd:cd01583 225 ------EYDKVVEIDASELE---------------PQVA-----------WPHSPDNVVPVSEVE--------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 432 yehegqshPLKHGAVVIAaitSCTNTSNPSVMMAAGLVakkaveKGLKRKPWVKSSLAPGSKVVtdyYKAA---GLTKYL 508
Cdd:cd01583 258 --------GIKIDQVFIG---SCTNGRLEDLRAAAEIL------KGRKVADGVRLIVVPASQRV---YKQAekeGLIEIF 317
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1086084978 509 DELGFALVGYGCTTCIG-NSGPLPEpiekaiqaaDLTVASvlSGNRNFEGRV-HPLVKTnWLASPPLVVAYALAGTV 583
Cdd:cd01583 318 IEAGAEVRPPGCGACLGgHMGVLAP---------GERCVS--TSNRNFKGRMgSPGARI-YLASPATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
85-586 |
2.75e-41 |
|
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: 157.11 E-value: 2.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 85 RVLMQDFTGVPAVVDLAAMraamakaGG----DPQRInplspVdLVIDHSVmvdkFASSSAFEQNVDIeMQRNGERY--A 158
Cdd:COG0065 30 LHLVHDVTSPQAFEGLREA-------GGrkvwDPDRI-----V-AVFDHNV----PTKDPKSAEQVKT-LREFAKEFgiT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 159 FLRWGQSafdnfsvvppgtGICHQVNLEyLGrtvwtkdedgrtYAFP-DTLVGTDSHTTM----------INGLgvlgwg 227
Cdd:COG0065 92 FFDVGDP------------GICHVVLPE-QG------------LVLPgMTIVGGDSHTCThgafgafafgIGTT------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 228 vggiEAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMA 307
Cdd:COG0065 141 ----DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 308 PEYGATCGFFPVDEVTLEYLRlsGRPSDTVKLVEAYSKAqglwrlpgqepVFTDSLALDMGSVEaslagpkrPQdrVALP 387
Cdd:COG0065 217 IEAGAKAGIIAPDETTFEYLK--GRPFAPWRTLKSDEDA-----------VYDKEVEIDASDLE--------PQ--VAWP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 388 -SVAQAfsdfidlqfKPTSKEEGRleseggggvavgnadlageasyehegqshplkhgAVVIAAITSCTNtsnpsvmmaa 466
Cdd:COG0065 274 hSPDNV---------VPVSELEGI----------------------------------KIDQVFIGSCTN---------- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 467 G----LVAKKAVEKGLKRKPWVKSSLAPGSKVVtdyYKAA---GLTKYLDELGFALVGYGCTTCIG-NSGPLpepiekai 538
Cdd:COG0065 301 GriedLRAAAEILKGRKVAPGVRAIVVPGSQEV---YRQAeaeGLDEIFIEAGAEWREPGCGMCLGmNMGVL-------- 369
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1086084978 539 qAADLTVASvlSGNRNFEGRV-HPLVKTnWLASPPLVVAYALAGTVrTD 586
Cdd:COG0065 370 -APGERCAS--TSNRNFEGRMgSPGSRT-YLASPATAAASAIAGRI-TD 413
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-582 |
1.04e-37 |
|
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: 146.43 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 85 RVLMQDFTGVPAVVDLAAMraamakagGDPQrinPLSPVDLVIDHSVMVDKFAsssafEQNVDIEMQRNGERYAFLrwgQ 164
Cdd:cd01584 1 RVAMQDATAQMALLQFMSS--------GLPK---VAVPSTIHCDHLIEAQVGG-----EKDLKRAKDINKEVYDFL---A 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 165 SAFDNFSV--VPPGTGICHQVNLEylgrtvwtkdedgrTYAFPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQP 241
Cdd:cd01584 62 SAGAKYGIgfWKPGSGIIHQIVLE--------------NYAFPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 242 VSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDE 321
Cdd:cd01584 128 WELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 322 VTLEYLRLSGRpSDTVKLVEAYsKAQGLWRLPGQEpvFTDSLALDMGSVEASLAGPkrpqdrvALPSVAQAFSDfidlqF 401
Cdd:cd01584 208 RMKKYLKATGR-AEIADLADEF-KDDLLVADEGAE--YDQLIEINLSELEPHINGP-------FTPDLATPVSK-----F 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 402 KPTSKEEGrleseggggvavgnadlageasyehegqsHPLKhgaVVIAAITSCTNTSNPSVMMAAGlVAKKAVEKGLKRK 481
Cdd:cd01584 272 KEVAEKNG-----------------------------WPLD---LRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLKCK 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 482 pwVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIG--NSGPLPEPIEKAIqaadltvasVLSGNRNFEGRV 559
Cdd:cd01584 319 --SIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRN 387
|
490 500
....*....|....*....|....
gi 1086084978 560 HPLVKT-NWLASPPLVVAYALAGT 582
Cdd:cd01584 388 DANPAThAFVASPEIVTAMAIAGT 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
86-581 |
1.38e-31 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 128.37 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 86 VLMQDFTGVPAVVDLAAMRAAMAKaggDPQRINplspvdLVIDHSVMVDKFASSsafeqnvdiEMQRngeryaFLR-WGQ 164
Cdd:PRK00402 31 VMAHDITGPLAIKEFEKIGGDKVF---DPSKIV------IVFDHFVPAKDIKSA---------EQQK------ILReFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 165 S-AFDNFSVVppGTGICHQVNLEylgrtvwtkdedgRTYAFP-DTLVGTDSHTT----------------Minglgvlgw 226
Cdd:PRK00402 87 EqGIPNFFDV--GEGICHQVLPE-------------KGLVRPgDVVVGADSHTCtygalgafatgmgstdM--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 227 gvggieAEAAMLGQpVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANM 306
Cdd:PRK00402 143 ------AAAMATGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 307 APEYGATCGFFPVDEVTLEYLRlsGRPSDTVKLVEAYSKAqglwrlpgqepVFTDSLALDMGSVEaslagpkrPQdrVAL 386
Cdd:PRK00402 216 AIEAGAKAGIFAPDEKTLEYLK--ERAGRDYKPWKSDEDA-----------EYEEVYEIDLSKLE--------PQ--VAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 387 P-SVAQAfsdfidlqfKPTSKEEGRleseggggvavgnadlageasyehegqshplkhgAVVIAAITSCTNTSNPSVMMA 465
Cdd:PRK00402 273 PhLPDNV---------KPVSEVEGT----------------------------------KVDQVFIGSCTNGRLEDLRIA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 466 AglvakkAVEKGLKRKPWVKSSLAPGSKVVtdyYKAA---GLTKYLDELGfALVGY-GCTTCIGNSGplpepiekAIQAA 541
Cdd:PRK00402 310 A------EILKGRKVAPGVRLIVIPASQKI---YLQAlkeGLIEIFVDAG-AVVSTpTCGPCLGGHM--------GVLAP 371
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1086084978 542 DLTVASvlSGNRNFEGRV-HPLVKTnWLASPPLVVAYALAG 581
Cdd:PRK00402 372 GEVCLS--TTNRNFKGRMgSPESEV-YLASPAVAAASAVTG 409
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
113-581 |
2.57e-25 |
|
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: 109.85 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 113 DPQRINplspvdLVIDHSVMVDKFASSsafeqnvdiEMQRNGERYAfLRWGQSAFDNfsvvppGTGICHQVNLEylgrtv 192
Cdd:TIGR02086 53 DPEKIV------IAFDHNVPPPTVEAA---------EMQKEIREFA-KRHGIKNFDV------GEGICHQILAE------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 193 wtkdedgRTYAFP-DTLVGTDSHTTMINGLGVLGWGVGGIE-AEAAMLGQPVSMlIPEVIGFKLTGKLKEGITATDLVLT 270
Cdd:TIGR02086 105 -------EGYALPgMVVVGGDSHTCTSGAFGAFATGMGATDmAIALATGKTWIK-VPETIRVVVEGKPEEGVTAKDVALH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 271 VTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTLEYLRLSGRPSDTVKlveayskaqglw 350
Cdd:TIGR02086 177 IVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRGLEFRIL------------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 351 rLPGQEPVFTDSLALDMGSVEASLAGPKRPQDRValpSVAQAFSDFIDLQFkptskeegrleseggggvavgnadlagea 430
Cdd:TIGR02086 245 -VPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVK---PVSDVEGTEIDQVF----------------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 431 syehegqshplkhgavviaaITSCTNTSNPSVMMAAglvakkAVEKGLKRKPWVKSSLAPGSKVVtdYYKA--AGLTKYL 508
Cdd:TIGR02086 292 --------------------IGSCTNGRLEDLRIAA------EILKGRRVHPDVRLIVIPASRKV--YLRAleEGIILTL 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1086084978 509 DELGFALVGYGCTTCIGnsgplpepIEKAIQAADLTVASvlSGNRNFEGRV-HPLVKTnWLASPPLVVAYALAG 581
Cdd:TIGR02086 344 VRAGAMICPPGCGPCLG--------AHMGVLGDGEVCLS--TTNRNFKGRMgSPNAEI-YLASPATAAASAVEG 406
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
113-583 |
2.00e-24 |
|
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: 107.15 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 113 DPQRINplspvdLVIDHSVMVDKFASSsafeqnvdiEMQRNGERYAflrwGQSAFDNFSvvPPGTGICHQVNLEylgrtv 192
Cdd:TIGR01343 52 NPEKIV------IVFDHQVPADTIKAA---------EMQKLAREFV----KKQGIKYFY--DVGEGICHQVLPE------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 193 wtkdedgRTYAFP-DTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTV 271
Cdd:TIGR01343 105 -------KGLVKPgDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVTAKDVILEV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 272 TQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEVTLEYLR-LSGRPSDTVKLVEayskaqglw 350
Cdd:TIGR01343 178 IGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKeRRKEPFRVYKSDE--------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 351 rlpgqEPVFTDSLALDMGSVEASLAGPKRPqDRValpsvaqafsdfidlqfKPTSKEEGRleseggggvavgnadlagea 430
Cdd:TIGR01343 249 -----DAEYAKEIEIDASQIEPVVACPHNV-DNV-----------------KPVSEVEGT-------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 431 syehegqshPLKHgavviAAITSCTNTSNPSVMMAAglvakkAVEKGLKRKPWVKSSLAPGSKVVtdYYKAA--GLTKYL 508
Cdd:TIGR01343 286 ---------EIDQ-----VFIGSCTNGRLEDLRVAA------KILKGRKVAPDVRLIVIPASRAV--YLQALkeGLIEIF 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1086084978 509 DELGfALVGY-GCTTCIGNSGPLPEPIEKAIQaadltvasvlSGNRNFEGRVHPLVKTNWLASPPLVVAYALAGTV 583
Cdd:TIGR01343 344 VKAG-AVVSTpGCGPCLGSHQGVLAPGEVCIS----------TSNRNFKGRMGHPNAEIYLASPATAAASAVKGYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
232-590 |
5.74e-23 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 103.45 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 232 EAEAAMLGQPVSMLIPEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYG 311
Cdd:PRK12466 150 EVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 312 ATCGFFPVDEVTLEYLRlsGRPSDTVklVEAYSKAQGLWR-LPGQE-PVFTDSLALDMGSVEASLAGPKRPQDRVALPSV 389
Cdd:PRK12466 230 ARGGLIAPDETTFDYLR--GRPRAPK--GALWDAALAYWRtLRSDAdAVFDREVEIDAADIAPQVTWGTSPDQAVPITGR 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 390 ---AQAFSDFIDLQfkptskeegrleseggggvavgnadlAGEASYE----HEGQshPLKHGAVVIAAITSCTNTSNPSV 462
Cdd:PRK12466 306 vpdPAAEADPARRA--------------------------AMERALDymglTPGT--PLAGIPIDRVFIGSCTNGRIEDL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 463 MMAAglvakkAVEKGLKRKPWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKaiqaad 542
Cdd:PRK12466 358 RAAA------AVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGER------ 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1086084978 543 ltVASvlSGNRNFEGRVHPLVKTNwLASPPLVVAYALAGT---VRTDLSRE 590
Cdd:PRK12466 426 --CAS--TTNRNFEGRQGPGARTH-LMSPAMVAAAAVAGHitdVRSLLQAG 471
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
174-583 |
2.40e-22 |
|
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: 100.00 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 174 PPGTGICHQVNLEylgrtvwtkdedgRTYAFPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGF 252
Cdd:cd01582 64 PAGRGIGHQIMIE-------------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 253 KLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDevtleylrlsgr 332
Cdd:cd01582 131 ELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD------------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 333 psdtvklveayskaqglwrlpgqepvfTDSLALDMGSVEASLAGPKrpqdrvalpSVAQAfsdfidlqfkpTSKEEgrLE 412
Cdd:cd01582 199 ---------------------------AKHLILDLSTLSPYVSGPN---------SVKVS-----------TPLKE--LE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 413 SEggggvavgnaDLAGEASYehegqshplkhgavviaaITSCTNTSNPSVMMAAGLV-AKKAVEKGLKRKPWVKSSLAPG 491
Cdd:cd01582 230 AQ----------NIKINKAY------------------LVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 492 SKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIGNSGPLPEPIEKAIQAAdltvasvlsgNRNFEGRVHPLVKTNWLASP 571
Cdd:cd01582 282 SSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISAT----------NRNFKGRMGSTEALAYLASP 351
|
410
....*....|..
gi 1086084978 572 PLVVAYALAGTV 583
Cdd:cd01582 352 AVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
780-846 |
4.97e-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: 88.29 E-value: 4.97e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1086084978 780 GTPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLNL 846
Cdd:cd00404 14 AGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHT 80
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
243-583 |
6.98e-20 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 93.65 E-value: 6.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 243 SMLIpevigfKLTGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGDGLADLPLADRATIANMAPEYGATCGFFPVDEV 322
Cdd:PRK05478 165 TMKI------EVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDET 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 323 TLEYLRlsGRPSdtVKLVEAYSKAQGLWR-LPGQE-PVFTDSLALD---------------MG-SVEASLAGPKRPQDRV 384
Cdd:PRK05478 239 TFEYLK--GRPF--APKGEDWDKAVAYWKtLKSDEdAVFDKVVTLDaadiepqvtwgtnpgQViSIDGKVPDPEDFADPV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 385 ALPSVAQAFsDFIDLQfkptskeegrleseggggvavgnadlAGEasyehegqshPLKHGAVVIAAITSCTNTSNPSVMM 464
Cdd:PRK05478 315 KRASAERAL-AYMGLK--------------------------PGT----------PITDIKIDKVFIGSCTNSRIEDLRA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 465 AAGLVakkaveKGLKRKPWVKSSLAPGSKVVTDYYKAAGLTKYLDELGFALVGYGCTTCIG-NSGPLPePIEKAiqaadl 543
Cdd:PRK05478 358 AAAVV------KGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLP-PGERC------ 424
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1086084978 544 tvASvlSGNRNFEGRVHPLVKTNwLASPPLVVAYALAGTV 583
Cdd:PRK05478 425 --AS--TSNRNFEGRQGKGGRTH-LVSPAMAAAAAITGHF 459
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
687-836 |
1.70e-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: 82.10 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 687 LGDSVTTDHISPAGnikadspaGQYLrdkgvepkdfnsygSRRGNHEVMMRGTFANIRirnemlggeeggntyyiPTMek 766
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVL--------------PLRSNIPAISEFVFHRVD-----------------PTF-- 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 767 mpiydaAMRYQASGtPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFK 836
Cdd:cd01579 41 ------AERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFA 103
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
692-864 |
1.86e-17 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 80.21 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 692 TTDHISPAGnikadsPAGQYlrdkgvepkdfnsygsrrgnhevmmRGTFANIRirNEMLGGE---EGGNTYYIP---TME 765
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIS--NNLLIGAinaENGKANSVKnqvTGE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 766 KMPIYDAAMRYQASGTPLVVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQF--KLDQNRks 843
Cdd:cd01578 54 YGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFadPADYDK-- 131
|
170 180
....*....|....*....|.
gi 1086084978 844 lnLKGTESIDILGLSgvELTP 864
Cdd:cd01578 132 --IHPDDKVDILGLT--DFAP 148
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
784-833 |
1.61e-11 |
|
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: 61.07 E-value: 1.61e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1086084978 784 VVIAGQEYGTGSSR---DWAAKGtnlLGVKAVIAESFERIHRSNLVGMGVLPL 833
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
681-834 |
1.42e-10 |
|
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: 61.34 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 681 ARVLALLGDSVTTDHISPAgnikadspagQYLrdKGVEPKDFnsygsrrGNHevmmrgTFANIRirnemlggeeggntYY 760
Cdd:COG0066 8 GRAVPLDGDNIDTDQIIPA----------RFL--KTIDREGL-------GKH------LFEDWR--------------YD 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1086084978 761 IPTMEKMPIYDAAMRyQASgtplVVIAGQEYGTGSSRD---WAAKGtnlLGVKAVIAESFERIHRSNLVGMGVLPLQ 834
Cdd:COG0066 49 RSPDPDFVLNQPRYQ-GAD----ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
784-834 |
2.69e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 57.12 E-value: 2.69e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1086084978 784 VVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQ 834
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFE 102
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
784-877 |
5.34e-08 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 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: 273961 [Multi-domain] Cd Length: 154 Bit Score: 53.19 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 784 VVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKL----DQNRKSLNLKgTESIDILGLSG 859
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIEAKTegikDGDEVTVDLE-TGEIRVNGNEE 128
|
90
....*....|....*...
gi 1086084978 860 VELTPRMNLTLVITREDG 877
Cdd:TIGR02087 129 YKGEPLPDFLLEILREGG 146
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
784-833 |
1.12e-07 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 52.14 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1086084978 784 VVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGvLPL 833
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
775-878 |
6.84e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 50.90 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 775 RYQ-ASgtplVVIAGQEYGTGSSRD---WAakgtnLL--GVKAVIAESFERIHRSNLVGMGVLPLQfkLDQnrkslnlkg 848
Cdd:PRK01641 64 RYQgAS----ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIV--LPE--------- 123
|
90 100 110
....*....|....*....|....*....|....*
gi 1086084978 849 tESIDILgLSGVELTPRMNLT-----LVITREDGS 878
Cdd:PRK01641 124 -EDVDEL-FKLVEANPGAELTvdleaQTVTAPDKT 156
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
784-834 |
1.46e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 47.55 E-value: 1.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1086084978 784 VVIAGQEYGTGSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMG-VLPLQ 834
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
247-380 |
1.87e-05 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 48.47 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086084978 247 PEVIGFKLTGKLKEGITATDLVLTVTQMLRKKGVV-GKFVEFYGDGLADLPLADRATIANMAPEygATC--GFFPVDEVT 323
Cdd:PRK11413 183 PGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQTDEEV 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1086084978 324 LEYLRLSGRPsdtvklvEAYSKaqglwrLPGQEPVFTDSL-ALDMGSVEASLAGPKRP 380
Cdd:PRK11413 261 HNWLALHGRG-------QDYCE------LNPQPMAYYDGCiSVDLSAIKPMIALPFHP 305
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
794-854 |
2.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 38.93 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1086084978 794 GSSRDWAAKGTNLLGVKAVIAESFERIHRSNLVGMGVLPLQFKLDQNRKSLNLKGTESIDI 854
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPTDQVTV 63
|
|
| |
