|
Name |
Accession |
Description |
Interval |
E-value |
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-904 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1679.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 1 MAHNLHKTLKEFDSGSGKGKFYSLPQLGKELKTKIERLPVSIRIVLESVLRNYDGKKITEEHIEQLANWQPTAKRVDEIP 80
Cdd:PRK12881 1 MAHNLHKTLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 81 FVVSRVVLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFM 160
Cdd:PRK12881 81 FVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 161 KWGMQAFDTFKVVPPGVGIVHQVNLEYLARGVHKKADGGDTVYYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQ 240
Cdd:PRK12881 161 KWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 241 PVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVD 320
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 321 EKTIEYFEGTGRTKAEIAAFENYFKAQKLFGIPKAgDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIGNVKSTFTELFSK 400
Cdd:PRK12881 321 EQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKA-EPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 401 PVAENGFAKKAEdlnaqytTSNGVDVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIKTSLAPGSRIV 480
Cdd:PRK12881 400 PVAENGFAKKAQ-------TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 481 TEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRANFLASPPLVV 560
Cdd:PRK12881 473 TEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 561 AYAIAGNITRDLMTEPVGKGKDGYDIYLGDIWPTSDEIHALLKFALDPKKFEDNYSKLTKKGDLWSKIEGETGQVYDW-P 639
Cdd:PRK12881 553 AYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWdP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 640 KSTYIAEPPFFghDFSMEPAASIPTVQGARALGIFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADFNSYGSRRGNH 719
Cdd:PRK12881 633 KSTYIRRPPFF--DFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNH 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 720 DVMMRGTFANVRIKNLMIPAKadgtrvEGGLTIHQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQL 799
Cdd:PRK12881 711 EVMMRGTFANVRIKNLMIPGK------EGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRL 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 800 LGVKAVIARSFERIHRSNLVGMGVLPLQFKGADSVQSLGITGEETYDIEGLGDDFKPQQDVTLVIHRKNGETTRVPVLLR 879
Cdd:PRK12881 785 LGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVTLVIHRADGSTERVPVLCR 864
|
890 900
....*....|....*....|....*
gi 500211529 880 IDTPIEVDYYKHGGILPFVLRSLLA 904
Cdd:PRK12881 865 IDTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-905 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1637.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 1 MAHNLHKTLKEFDSGSGKGKFYSLPQLGKELKTKIERLPVSIRIVLESVLRNYDGKKITEEHIEQLANWQPTAKRVDEIP 80
Cdd:PRK09277 2 SSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 81 FVVSRVVLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFM 160
Cdd:PRK09277 82 FRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 161 KWGMQAFDTFKVVPPGVGIVHQVNLEYLARGVHKKADGgDTVYYPDTLVGTDSHTTMINgigvvgwgvggiEAEAGMLGQ 240
Cdd:PRK09277 162 KWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTREDG-ELVAYPDTLVGTDSHTTMINglgvlgwgvggiEAEAAMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 241 PVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVD 320
Cdd:PRK09277 241 PSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 321 EKTIEYFEGTGRTKAEIAAFENYFKAQKLFGIPKAgDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIGNVKSTFTElfSK 400
Cdd:PRK09277 321 EETLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLE-EPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK--SA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 401 PVAENGFAKKAEDLNAQYttsngvDVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIKTSLAPGSRIV 480
Cdd:PRK09277 398 ELGVQGFGLDEAEEGEDY------ELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 481 TEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRANFLASPPLVV 560
Cdd:PRK09277 472 TDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 561 AYAIAGNITRDLMTEPVGKGKDGYDIYLGDIWPTSDEIHALLKFALDPKKFEDNYSKLTKKGDLWSKIEGETGQVYDW-P 639
Cdd:PRK09277 552 AYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWdP 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 640 KSTYIAEPPFFgHDFSMEPAAsIPTVQGARALGIFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADFNSYGSRRGNH 719
Cdd:PRK09277 632 DSTYIRNPPYF-EGMLAEPGP-VRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNH 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 720 DVMMRGTFANVRIKNLMIPakadgtRVEGGLTIHQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQL 799
Cdd:PRK09277 710 EVMMRGTFANIRIRNEMVP------GVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 800 LGVKAVIARSFERIHRSNLVGMGVLPLQFKGADSVQSLGITGEETYDIEGLgDDFKPQQDVTLVIHRKNGETTRVPVLLR 879
Cdd:PRK09277 784 LGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGL-EDLKPGATVTVVITRADGEVVEFPVLCR 862
|
890 900
....*....|....*....|....*.
gi 500211529 880 IDTPIEVDYYKHGGILPFVLRSLLAA 905
Cdd:PRK09277 863 IDTAVEVDYYRNGGILQYVLRDLLAS 888
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-905 |
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: 1627.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 3 HNLHKTLKEFDSGSGKGKFYSLPQLGKELKtKIERLPVSIRIVLESVLRNYDGKKITEEHIEQLANWQPTAKRVDEIPFV 82
Cdd:COG1048 2 MDSFKARKTLTVGGKPYTYYSLPALEEAGG-DISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 83 VSRVVLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFMKW 162
Cdd:COG1048 81 PARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 163 GMQAFDTFKVVPPGVGIVHQVNLEYLARGVHKKADGGDTVYYPDTLVGTDSHTTMINgigvvgwgvggiEAEAGMLGQPV 242
Cdd:COG1048 161 GQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGETVAYPDTLVGTDSHTTMINglgvlgwgvggiEAEAAMLGQPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 243 YFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEK 322
Cdd:COG1048 241 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 323 TIEYFEGTGRTKAEIAAFENYFKAQKLFGIPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIGNVKSTFTELFSKPV 402
Cdd:COG1048 321 TLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 403 AENGFAKKAEDLNAQyttsnGVDVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIKTSLAPGSRIVTE 482
Cdd:COG1048 401 GEELDKPVRVEVDGE-----EFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 483 YLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRANFLASPPLVVAY 562
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAY 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 563 AIAGNITRDLMTEPVGKGKDGYDIYLGDIWPTSDEIHALLKFALDPKKFEDNYSKLTKKGDLWSKIEGETGQVYDW-PKS 641
Cdd:COG1048 556 ALAGTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWdPDS 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 642 TYIAEPPFFgHDFSMEPAAsIPTVQGARALGIFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADFNSYGSRRGNHDV 721
Cdd:COG1048 636 TYIRRPPFF-EGLQLEPEP-FKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEV 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 722 MMRGTFANVRIKNLMIPakadgtRVEGGLTIHQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQLLG 801
Cdd:COG1048 714 MMRGTFANIRIKNLLAP------GTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLG 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 802 VKAVIARSFERIHRSNLVGMGVLPLQFKGADSVQSLGITGEETYDIEGLGDDFKPQQDVTLVIHRKNGETTRVPVLLRID 881
Cdd:COG1048 788 VKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAPGKTVTVTATRADGSTEEFPVLHRID 867
|
890 900
....*....|....*....|....
gi 500211529 882 TPIEVDYYKHGGILPFVLRSLLAA 905
Cdd:COG1048 868 TPVEVEYYRAGGILQYVLRQLLAA 891
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
7-905 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1292.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 7 KTLKEfdsgSGKGKFYSLPQLGKElktKIERLPVSIRIVLESVLRNYDGKKITEEHIEQLANWQPTAKRVDEIPFVVSRV 86
Cdd:PTZ00092 21 KTLKD----GGSYKYYSLNELHDP---RLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPARV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 87 VLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFMKWGMQA 166
Cdd:PTZ00092 94 LLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSKA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 167 FDTFKVVPPGVGIVHQVNLEYLARGVHKKadggDTVYYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLT 246
Cdd:PTZ00092 174 FKNLLIVPPGSGIVHQVNLEYLARVVFNK----DGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 247 PDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEKTIEY 326
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 327 FEGTGRTKAEIAAFENYFKAQKLFGiPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIGNVKSTFTELFSKPVAENG 406
Cdd:PTZ00092 330 LKQTGRSEEKVELIEKYLKANGLFR-TYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 407 FAKKAEDLNAQYT-TSNG--VDVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIKTSLAPGSRIVTEY 483
Cdd:PTZ00092 409 FGIPEEKHEKKVKfTYKGkeYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKY 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 484 LTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRANFLASPPLVVAYA 563
Cdd:PTZ00092 489 LEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYA 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 564 IAGNITRDLMTEPVGKGKDGYDIYLGDIWPTSDEIHALLKFALDPKKFEDNYSKLTKKGDLWSKIEGETGQVYDW-PKST 642
Cdd:PTZ00092 569 LAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWdEKST 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 643 YIAEPPFFgHDFSMEPaASIPTVQGARALGIFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADFNSYGSRRGNHDVM 722
Cdd:PTZ00092 649 YIHNPPFF-QTMELEP-PPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVM 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 723 MRGTFANVRIKNLMIPAKadgtrveGGLTIHQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQLLGV 802
Cdd:PTZ00092 727 VRGTFANIRLINKLCGKV-------GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGV 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 803 KAVIARSFERIHRSNLVGMGVLPLQFKGADSVQSLGITGEETYDIEGLGDDFKPQQDVTlvIHRKNGETtrVPVLLRIDT 882
Cdd:PTZ00092 800 KAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQDVT--VKTDTGKT--FDTILRIDT 875
|
890 900
....*....|....*....|...
gi 500211529 883 PIEVDYYKHGGILPFVLRSLLAA 905
Cdd:PTZ00092 876 EVEVEYFKHGGILQYVLRKLVKG 898
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
18-903 |
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: 1249.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 18 KGKFYSLPQLGKELKtKIERLPVSIRIVLESVLRNYDGKKITEEHIEQLANWQPTAKRVDEIPFVVSRVVLQDFTGVPLL 97
Cdd:TIGR01341 2 TYYYYSLKALEESGG-KISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 98 ADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFMKWGMQAFDTFKVVPPGV 177
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 178 GIVHQVNLEYLARGVHKKADGGDTVYYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKGK 257
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFKAEVDGELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 258 LREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEKTIEYFEGTGRTKAEI 337
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 338 AAFENYFKAQKLFGiPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIGNVKSTFTELFSKPVAENGFAKKAEDLNAQ 417
Cdd:TIGR01341 321 ELVEKYARAQGLFY-DDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 418 YTTSNGVdVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIKTSLAPGSRIVTEYLTKTGLLPYLAKLG 497
Cdd:TIGR01341 400 VNGQNKQ-LEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 498 FEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRANFLASPPLVVAYAIAGNITRDLMTEPV 577
Cdd:TIGR01341 479 FNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 578 GKGKDGYDIYLGDIWPTSDEIHALLKFALDPKKFEDNYSKLTKKGDLWSKIEGETGQVYDW-PKSTYIAEPPFFgHDFSM 656
Cdd:TIGR01341 559 GTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWdEKSTYIRLPPFF-EEMKQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 657 EPAASIPtVQGARALGIFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADFNSYGSRRGNHDVMMRGTFANVRIKNLM 736
Cdd:TIGR01341 638 DPEEVED-IKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLM 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 737 IPAKadgtrvEGGLTIHQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRS 816
Cdd:TIGR01341 717 VKGK------EGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRS 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 817 NLVGMGVLPLQFKGADSVQSLGITGEETYDIEGLGdDFKPQQDVTLVIHRKNGETTRVPVLLRIDTPIEVDYYKHGGILP 896
Cdd:TIGR01341 791 NLVGMGVIPLQFPQGEDAETLGLTGDETIDIDGIK-DLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQ 869
|
....*..
gi 500211529 897 FVLRSLL 903
Cdd:TIGR01341 870 YVLRKFL 876
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
4-905 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1104.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 4 NLHKTLKEFDSGSgKGKFYSLPQLGKelkTKIERLPVSIRIVLESVLRNYDGKKITEEHIEQLANWQPTAKRVDEIPFVV 83
Cdd:PLN00070 47 GILTSLPKPGGGE-FGKYYSLPALND---PRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 84 SRVVLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFMKWG 163
Cdd:PLN00070 123 ARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 164 MQAFDTFKVVPPGVGIVHQVNLEYLARGVHKKadggDTVYYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVY 243
Cdd:PLN00070 203 STAFQNMLVVPPGSGIVHQVNLEYLGRVVFNT----DGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 244 FLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEKT 323
Cdd:PLN00070 279 MVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 324 IEYFEGTGRTKAEIAAFENYFKAQKLFgipkagdIDYTKTVT---------LDLATVAPSLAGPKRPQDRIEIGNVKSTF 394
Cdd:PLN00070 359 LQYLKLTGRSDETVAMIEAYLRANKMF-------VDYNEPQQervyssyleLDLEDVEPCISGPKRPHDRVPLKEMKADW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 395 TELFSKPVAENGFA--KKAEDLNAQYTTsNG--VDVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIK 470
Cdd:PLN00070 432 HSCLDNKVGFKGFAvpKEAQSKVAKFSF-HGqpAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 471 TSLAPGSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRA 550
Cdd:PLN00070 511 TSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRA 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 551 NFLASPPLVVAYAIAGNITRDLMTEPVGKGKDGYDIYLGDIWPTSDEIHALLKFALDPKKFEDNYSKLTKKGDLWSKIEG 630
Cdd:PLN00070 591 NYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSV 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 631 ETGQVYDW-PKSTYIAEPPFFgHDFSMEPAASIPtVQGARALGIFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADF 709
Cdd:PLN00070 671 PSGTLYSWdPKSTYIHEPPYF-KNMTMSPPGPHG-VKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDF 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 710 NSYGSRRGNHDVMMRGTFANVRIKNLMIPAKAdgtrveGGLTIHQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSS 789
Cdd:PLN00070 749 NSYGSRRGNDEIMARGTFANIRIVNKLLKGEV------GPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSS 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 790 RDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKGADSVQSLGITGEETYDIEGLGD--DFKPQQDVTLVIhrK 867
Cdd:PLN00070 823 RDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPSNisEIKPGQDVTVTT--D 900
|
890 900 910
....*....|....*....|....*....|....*...
gi 500211529 868 NGETtrVPVLLRIDTPIEVDYYKHGGILPFVLRSLLAA 905
Cdd:PLN00070 901 NGKS--FTCTLRFDTEVELAYFDHGGILPYVIRNLIKQ 936
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
85-568 |
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: 709.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 85 RVVLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSVQIDYFRQKDALDLNMKLEFQRNNERYQFMKWGM 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 165 QAFDTFKVVPPGVGIVHQVNLEYLARGVHKKADGGDTVYYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYF 244
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 245 LTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDekti 324
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 325 eyfegtgrtkaeiaafenyfkaqklfgipkagdidyTKTVTLDLATVAPSLAGPKRPQDRIEIgnvkstftelfskpvae 404
Cdd:cd01586 237 ------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 405 ngfakkaedlnaqyttsngvdvkNGDVLIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLTVAPHIKTSLAPGSRIVTEYL 484
Cdd:cd01586 264 -----------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 485 TKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPELNEAITKNDIVAAAVLSGNRNFEARIHPNIRANFLASPPLVVAYAI 564
Cdd:cd01586 321 EASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYAL 400
|
....
gi 500211529 565 AGNI 568
Cdd:cd01586 401 AGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
78-566 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 598.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 78 EIPFVVSRVVLQDFTGVPLLADIAAMRGVAQRSGKDPKKIEPLVPVDLVVDHSvqidyfrqKDALDLNMKLEFQRNNERY 157
Cdd:pfam00330 15 SLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALDKNIEDEISRNKEQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 158 QFMKWGMQAFDtFKVVPPGVGIVHQVNLEYLargvhkkadggdtVYYPD-TLVGTDSHTTMINgigvvgwgvggiEAEAG 236
Cdd:pfam00330 87 DFLEWNAKKFG-IRFVPPGQGIVHQVGLEYG-------------LALPGmTIVGTDSHTTTHGglgalafgvggsEAEHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 237 MLGQPVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGF 316
Cdd:pfam00330 153 LATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 317 FPVDEKTIEYFEGTGRTKAEIAafENYFKAQKLFGIPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIgnvkstfTE 396
Cdd:pfam00330 233 FPPDETTFEYLRATGRPEAPKG--EAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPL-------SE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 397 LFSKPVAENGFAKKAEDLNAQYTTSNGVDVKNGDVLIAAITSCTNTSNPSVLLAAGLLaKKAVEAGLTVAPHIKTSLAPG 476
Cdd:pfam00330 304 LVPDPFADAVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASVVPG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 477 SRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPelNEAItkndivaaaVLSGNRNFEARIHPNIRAnFLASP 556
Cdd:pfam00330 383 SEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--GERC---------VSSSNRNFEGRQGPGGRT-HLASP 450
|
490
....*....|
gi 500211529 557 PLVVAYAIAG 566
Cdd:pfam00330 451 ALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
673-849 |
7.65e-106 |
|
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: 324.23 E-value: 7.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 673 IFGDSVTTDHISPAGSIKEDSPAGKWLKENGVQKADFNSYGSRRGNHDVMMRGTFANVRIKNLMIPakadgtRVEGGLTI 752
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVP------GTEGGTTH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 753 HQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKGAD 832
Cdd:cd01580 75 HPPTGEVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGE 154
|
170
....*....|....*..
gi 500211529 833 SVQSLGITGEETYDIEG 849
Cdd:cd01580 155 NADSLGLTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-568 |
9.63e-90 |
|
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: 290.17 E-value: 9.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 85 RVVLQDFTGVPLLADIAAMRGvaqrsgkdPKKIEPLVPVDLVVDHSVQidyfrqkdaldlnmkLEFQRNNERYQFMKWgm 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAA--------LGKVADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 165 qAFDTFKV--VPPGVGIVHQVNLEYLArgvhkkadggdtvYYPDTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPV 242
Cdd:cd01351 56 -FAALQGIafYRPGVGIIHQIMVENLA-------------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 243 YFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEK 322
Cdd:cd01351 122 WLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 323 TIEYFEGTGRTKAEIAAFENYFKaqklfgIPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIgnvkstftelfskpv 402
Cdd:cd01351 202 TLKWLEATGRPLLKNLWLAFPEE------LLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSV--------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 403 aengfakkaedlnaqyttsngVDVKNGDVLIAAITSCTNtSNPSVLLAAGLLAKKAVeagltVAPHIKTSLAPGSRIVTE 482
Cdd:cd01351 261 ---------------------SEVEGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 483 YLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPElneaitkndiVAAAVLSGNRNFEARIHPNIRANFLASPPLVVAY 562
Cdd:cd01351 314 TLSREGYYEILVDSGARILPPGCGPCMGNGARLVAD----------GEVGVSSGNRNFPGRLGTYERHVYLASPELAAAT 383
|
....*.
gi 500211529 563 AIAGNI 568
Cdd:cd01351 384 AIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
57-902 |
4.42e-84 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 283.19 E-value: 4.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 57 KITEEHIeqlanWQPTAKRVDEIPFVVSRVVLQDFTGVPLLADIAAMrgvaqrsGKDPkkieplVPVDLVVDHsvqIDYf 136
Cdd:PRK07229 8 KILYAHL-----VEGELEPGEEIAIRIDQTLTQDATGTMAYLQFEAM-------GLDR------VKTELSVQY---VDH- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 137 rqkdaldlNMKLEFQRNNERYQFMkwgMQAFDTFKVV--PPGVGIVHQVNLEYLARgvhkkadggdtvyyP-DTLVGTDS 213
Cdd:PRK07229 66 --------NLLQADFENADDHRFL---QSVAAKYGIYfsKPGNGICHQVHLERFAF--------------PgKTLLGSDS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 214 HTT------MIngigvvGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKGKLREGVTATDLVLtitEMLRKEKV---VGKF 284
Cdd:PRK07229 121 HTPtagglgML------AIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL---ELLRRLTVkggVGKI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 285 VEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEKTIEYFEGTGRTK--AEIAAFEnyfkaqklfgipkagDIDYTK 362
Cdd:PRK07229 192 IEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKAQGREDdwVELLADP---------------DAEYDE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 363 TVTLDLATVAPSLAGPKRPqdrieiGNVkstftelfsKPVAEngFAKKAedlnaqyttsngVDVkngdvliAAITSCTNT 442
Cdd:PRK07229 257 VIEIDLSELEPLIAGPHSP------DNV---------VPVSE--VAGIK------------VDQ-------VLIGSCTNS 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 443 SNPSVLLAAGLLAKKaveaglTVAPHIKTSLAPGSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDltPElnea 522
Cdd:PRK07229 301 SYEDLMRAASILKGK------KVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQA--PA---- 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 523 iTKNDIVAaavlSGNRNFEARI-HPNIRAnFLASPPLVVAYAIAGNIT--RDLMTEpvgkgkdgydiyLGDiWPTSDEih 599
Cdd:PRK07229 369 -TGNVSLR----TFNRNFPGRSgTKDAQV-YLASPETAAASALTGVITdpRTLALE------------NGE-YPKLEE-- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 600 allkfaldPKKFEDNYSKLTKKGDLWSKIEGETGqvydwPKstyIAEPPFFghdfsmEPaasIPTVQGARALGIFGDSVT 679
Cdd:PRK07229 428 --------PEGFAVDDAGIIAPAEDGSDVEVVRG-----PN---IKPLPLL------EP---LPDLLEGKVLLKVGDNIT 482
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 680 TDHISPAGSikedspagKWLKengvqkadfnsYgsrRGNhdvmmrgtfanvriknlmIPAKADGTrveggltihqpsgeq 759
Cdd:PRK07229 483 TDHIMPAGA--------KWLP-----------Y---RSN------------------IPNISEFV--------------- 507
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 760 LSIYDAAM-KYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFkgADsvqslg 838
Cdd:PRK07229 508 FEGVDNTFpERAKEQGGGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTF--AD------ 579
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500211529 839 itgEETYD---------IEGLgDDFKPQQDVTLVIHRKNgetTRVPVLLRIdTPIEVDYYKHGGILPFVLRSL 902
Cdd:PRK07229 580 ---PADYDkieegdvleIEDL-REFLPGGPLTVVNVTKD---EEIEVRHTL-SERQIEILLAGGALNLIKKKL 644
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
175-568 |
1.01e-49 |
|
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: 180.34 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 175 PGVGIVHQVNLEYLARgvhkkadggdtvyyP-DTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVE 253
Cdd:cd01585 66 PGNGICHQVHLERFAV--------------PgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 254 LKGKLREGVTATDLVLtitEMLRKEKV---VGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEKTIEYFEGT 330
Cdd:cd01585 132 LTGELPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 331 GRtkaeiaafENYFkaqklfgIPKAGDID--YTKTVTLDLATVAPSLAGPKRPqdrieiGNVkstftelfsKPVAENGFA 408
Cdd:cd01585 209 GR--------EDDW-------VELAADADaeYDEEIEIDLSELEPLIARPHSP------DNV---------VPVREVAGI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 409 KKAEdlnaqyttsngvdvkngdvliAAITSCTNTSNPSVLLAAGLLakkaveAGLTVAPHIKTSLAPGSRIVTEYLTKTG 488
Cdd:cd01585 259 KVDQ---------------------VAIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAPGSKQVLEMLARNG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 489 LLPYLAKLGFEVAAYGCTTCIGNAGdlTPELNeaitkndivAAAVLSGNRNFEARIHPNIRANFLASPPLVVAYAIAGNI 568
Cdd:cd01585 312 ALADLLAAGARILESACGPCIGMGQ--APPTG---------GVSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-568 |
2.58e-46 |
|
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: 171.47 E-value: 2.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 85 RVVLQDFTG-VPLLADIAAMRgvaqrsgkdPKkiePLVPVDLVVDHSVQIDYFRQKDaldlnMKLEFQRNNERYQFM--- 160
Cdd:cd01584 1 RVAMQDATAqMALLQFMSSGL---------PK---VAVPSTIHCDHLIEAQVGGEKD-----LKRAKDINKEVYDFLasa 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 161 --KWGMQAFdtfkvvPPGVGIVHQVNLEYLArgvhkkadggdtvyYPDTL-VGTDSHTTMINGIGVVGWGVGGIEAEAGM 237
Cdd:cd01584 64 gaKYGIGFW------KPGSGIIHQIVLENYA--------------FPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 238 LGQPVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFF 317
Cdd:cd01584 124 AGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 318 PVDEKTIEYFEGTGRtkAEIAAFENYFKAQKLFGIPKAgdiDYTKTVTLDLATVAPSLAGPkrpqdrieignvkstFTEL 397
Cdd:cd01584 204 PYNERMKKYLKATGR--AEIADLADEFKDDLLVADEGA---EYDQLIEINLSELEPHINGP---------------FTPD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 398 FSKPVAEngFAKKAEdlnaqyttsngvdvKNG---DVLIAAITSCTNTSNPSVLLAAGlLAKKAVEAGLTVAphIKTSLA 474
Cdd:cd01584 264 LATPVSK--FKEVAE--------------KNGwplDLRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTIT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 475 PGSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIG--NAGDLTPElneaiTKNDIVAaavlSGNRNFEARIHPNIRA-N 551
Cdd:cd01584 325 PGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGqwDRKDIKKG-----EKNTIVT----SYNRNFTGRNDANPAThA 395
|
490
....*....|....*..
gi 500211529 552 FLASPPLVVAYAIAGNI 568
Cdd:cd01584 396 FVASPEIVTAMAIAGTL 412
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
695-829 |
3.34e-46 |
|
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: 161.38 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 695 AGKWLKENGVQKADFNSYGSRRGNHDVMMRGTFANVRIKNLMIPAKadgtrvEGGLTIHQPSGEQLSIYDAAMKYVGAGT 774
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGW------RYGKVRYLPDGENPDFYDAAMRYKQHGA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 500211529 775 PTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFK 829
Cdd:pfam00694 75 PIVVIGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFP 129
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
75-572 |
6.84e-45 |
|
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: 167.51 E-value: 6.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 75 RVDEIPFV-VSRVVLQDFTGvPLLADIAAMRGVaqRSGKDPKKIeplvpVdLVVDHSVQ---IDYFRQKDALDLNMKlef 150
Cdd:COG0065 19 EPGEIVLLyIDLHLVHDVTS-PQAFEGLREAGG--RKVWDPDRI-----V-AVFDHNVPtkdPKSAEQVKTLREFAK--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 151 qrnneryqfmKWGMQAFDTFKVvppgvGIVHQVNLEY-LARgvhkkadggdtvyyP-DTLVGTDSHTTM----------I 218
Cdd:COG0065 87 ----------EFGITFFDVGDP-----GICHVVLPEQgLVL--------------PgMTIVGGDSHTCThgafgafafgI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 219 NgigvvgwgvgGIEAEAGMLGQPVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLP 298
Cdd:COG0065 138 G----------TTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSME 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 299 DRATIGNMAPEYGATMGFFPVDEKTIEYFEGTGRTKAEIaafenyFKAQKlfgipkagDIDYTKTVTLDLATVAPSLAGP 378
Cdd:COG0065 208 ERMTLCNMAIEAGAKAGIIAPDETTFEYLKGRPFAPWRT------LKSDE--------DAVYDKEVEIDASDLEPQVAWP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 379 KRPqdrieiGNVkstftelfsKPVAEngfakkAEDLNaqyttsngVDVkngdvliAAITSCTNtsnpSVL----LAAGLL 454
Cdd:COG0065 274 HSP------DNV---------VPVSE------LEGIK--------IDQ-------VFIGSCTN----GRIedlrAAAEIL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 455 akkaveAGLTVAPHIKTSLAPGSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNAGDLTPElneaitkNDIVAAavl 534
Cdd:COG0065 314 ------KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAP-------GERCAS--- 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 500211529 535 SGNRNFE-------ARIHpniranfLASPPLVVAYAIAGNIT--RDL 572
Cdd:COG0065 378 TSNRNFEgrmgspgSRTY-------LASPATAAASAIAGRITdpREL 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
85-568 |
3.11e-43 |
|
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: 161.59 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 85 RVVLQDFTGvPLLADIAAMRGVaqRSGKDPKKIEplvpvdLVVDHSVQIDyfRQKDALDLNMKLEFQRnneryqfmKWGM 164
Cdd:cd01583 1 LHLVHDVTS-PQAFEGLREAGR--EKVWDPEKIV------AVFDHNVPTP--DIKAAEQVKTLRKFAK--------EFGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 165 QAFDtfkvvPPGVGIVHQVNLE-YLARgvhkkadggdtvyyP-DTLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPV 242
Cdd:cd01583 62 NFFD-----VGRQGICHVILPEkGLTL--------------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 243 YFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEK 322
Cdd:cd01583 123 WFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDET 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 323 TIEYFEgtGRTKAeiaafenYFKAqklfgIPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEIGNVkstftelfsKPV 402
Cdd:cd01583 203 TFEYLK--GRGKA-------YWKE-----LKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEV---------EGI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 403 AengfakkaedlnaqyttsngVDVkngdvliAAITSCTNTSNPSVLLAAGLLAKKaveaglTVAPHIKTSLAPGSRIVTE 482
Cdd:cd01583 260 K--------------------IDQ-------VFIGSCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPASQRVYK 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 483 YLTKTGLLPYLAKLGFEVAAYGCTTCIG-NAGDLTPelneaitkNDIVAAavlSGNRNFEARI-HPNIRaNFLASPPLVV 560
Cdd:cd01583 307 QAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAP--------GERCVS---TSNRNFKGRMgSPGAR-IYLASPATAA 374
|
....*...
gi 500211529 561 AYAIAGNI 568
Cdd:cd01583 375 ASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
176-573 |
1.62e-31 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 128.37 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 176 GVGIVHQVNLEY-LARGvhkkadgGDTVyypdtlVGTDSHTT----------------MingigvvgwgvggieAEAGML 238
Cdd:PRK00402 97 GEGICHQVLPEKgLVRP-------GDVV------VGADSHTCtygalgafatgmgstdM---------------AAAMAT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 239 GQpVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFP 318
Cdd:PRK00402 149 GK-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 319 VDEKTIEYFEgtGRTKAEIaafeNYFKAQKlfgipkagDIDYTKTVTLDLATVAPSLAGPKRPQdrieigNVkstftelf 398
Cdd:PRK00402 228 PDEKTLEYLK--ERAGRDY----KPWKSDE--------DAEYEEVYEIDLSKLEPQVAAPHLPD------NV-------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 399 sKPVAEngfakkaedlnaqyttsngvdVKNGDVLIAAITSCTNTSNPSVLLAAGLLAKKaveaglTVAPHIKTSLAPGSR 478
Cdd:PRK00402 280 -KPVSE---------------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGR------KVAPGVRLIVIPASQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 479 IVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIG-NAGDLTPelneaitknDIVAAAvlSGNRNFEARI-HPNIRAnFLASP 556
Cdd:PRK00402 332 KIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGgHMGVLAP---------GEVCLS--TTNRNFKGRMgSPESEV-YLASP 399
|
410
....*....|....*....
gi 500211529 557 PLVVAYAIAGNIT--RDLM 573
Cdd:PRK00402 400 AVAAASAVTGKITdpREVL 418
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
247-573 |
7.55e-25 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 109.05 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 247 PDVVGVELKGKLREGVTATDLVLTItemLRKEKV---VGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDEKT 323
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 324 IEYFEgtGRTKA-EIAAFE---NYFKAqklfgIPKAGDIDYTKTVTLDLATVAPSLAGPKRPQDRIEI-GNVKStfTELF 398
Cdd:PRK05478 240 FEYLK--GRPFApKGEDWDkavAYWKT-----LKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIdGKVPD--PEDF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 399 SKPVAENGFAKKAE--DLNA-QYTTSNGVDVkngdvliAAITSCTNtSNPSVLLAAGLLAKkaveaGLTVAPHIKTSLAP 475
Cdd:PRK05478 311 ADPVKRASAERALAymGLKPgTPITDIKIDK-------VFIGSCTN-SRIEDLRAAAAVVK-----GRKVAPGVRALVVP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 476 GSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIG-NAGDLTPelneaitkNDIVAAavlSGNRNFEARIHPNIRaNFLA 554
Cdd:PRK05478 378 GSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLPP--------GERCAS---TSNRNFEGRQGKGGR-THLV 445
|
330 340
....*....|....*....|.
gi 500211529 555 SPPLVVAYAIAGNIT--RDLM 573
Cdd:PRK05478 446 SPAMAAAAAITGHFVdvRELL 466
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
174-568 |
7.75e-25 |
|
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: 107.31 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 174 PPGVGIVHQVNLEylargvhkkadggDTVYYPDTL-VGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGV 252
Cdd:cd01582 64 PAGRGIGHQIMIE-------------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 253 ELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPVDektieyfegtgr 332
Cdd:cd01582 131 ELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD------------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 333 tkaeiaafenyfkaqklfgipkagdidyTKTVTLDLATVAPSLAGPKrpqdrieigNVKstftelfskpvaengFAKKAE 412
Cdd:cd01582 199 ----------------------------AKHLILDLSTLSPYVSGPN---------SVK---------------VSTPLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 413 DLNAQyttsngvdvkngDVLI--AAITSCTNTSNPSVLLAAGLL-AKKAVEAGLTVAPHIKTSLAPGSRIVTEYLTKTGL 489
Cdd:cd01582 227 ELEAQ------------NIKInkAYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 490 LPYLAKLGFEVAAYGCTTCIG-NAGDLTPElneaitkndivAAAVLSGNRNFEARIHPNIRANFLASPPLVVAYAIAGNI 568
Cdd:cd01582 295 WQTLLEAGATPLPAGCGPCIGlGQGLLEPG-----------EVGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
83-572 |
1.09e-24 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 108.45 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 83 VSRVVLQDFTGVPLLADIAAmRGvaqRSGKDPKKieplvpVDLVVDHSVQIDYFRQKDALD---LNMKLEFQRNNERYqf 159
Cdd:PRK12466 28 IDRHLLNEYTSPQAFSGLRA-RG---RTVRRPDL------TLAVVDHVVPTRPGRDRGITDpggALQVDYLRENCADF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 160 mkwGMQAFDTFKvvpPGVGIVHQVNLEY-LARgvhkkadggdtvyyPD-TLVGTDSHTTMINGIGVVGWGVGGIEAEAGM 237
Cdd:PRK12466 96 ---GIRLFDVDD---PRQGIVHVVAPELgLTL--------------PGmVIVCGDSHTTTYGALGALAFGIGTSEVEHVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 238 LGQPVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVVGKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFF 317
Cdd:PRK12466 156 ATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 318 PVDEKTIEYFEGTGRTKAEiAAFENYFKA-QKLFGIPKAGdidYTKTVTLDLATVAPSLAGPKRPQDRIEI-GNVKstFT 395
Cdd:PRK12466 236 APDETTFDYLRGRPRAPKG-ALWDAALAYwRTLRSDADAV---FDREVEIDAADIAPQVTWGTSPDQAVPItGRVP--DP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 396 ELFSKPVAENGfAKKAEDlnaqYTtsngvDVKNG----DVLI--AAITSCTNtSNPSVLLAAGllakkAVEAGLTVAPHI 469
Cdd:PRK12466 310 AAEADPARRAA-MERALD----YM-----GLTPGtplaGIPIdrVFIGSCTN-GRIEDLRAAA-----AVLRGRKVAPGV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 470 KTSLAPGSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGnagdltpeLNEaitknDIVAA---AVLSGNRNFEARIHP 546
Cdd:PRK12466 374 RAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA--------MND-----DVLAPgerCASTTNRNFEGRQGP 440
|
490 500
....*....|....*....|....*...
gi 500211529 547 NIRANfLASPPLVVAYAIAGNIT--RDL 572
Cdd:PRK12466 441 GARTH-LMSPAMVAAAAVAGHITdvRSL 467
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
772-849 |
3.29e-20 |
|
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: 85.98 E-value: 3.29e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500211529 772 AGTPTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKgaDSVQSLGITGEETYDIEG 849
Cdd:cd00404 13 PAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFA--DPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
679-856 |
7.86e-18 |
|
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: 81.36 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 679 TTDHISPAGSikedspagkWLKengvqkadfnsygsrrgnhdvmMRGTFANVRiKNLMIPA------KADGTRvegglti 752
Cdd:cd01578 7 TTDHISAAGP---------WLK----------------------YRGHLDNIS-NNLLIGAinaengKANSVK------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 753 HQPSGEQLSIYDAAMKYVGAGTPTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFkgAD 832
Cdd:cd01578 48 NQVTGEYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTF--AD 125
|
170 180
....*....|....*....|....
gi 500211529 833 SVQSLGITGEETYDIEGLgDDFKP 856
Cdd:cd01578 126 PADYDKIHPDDKVDILGL-TDFAP 148
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
673-832 |
8.68e-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: 80.17 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 673 IFGDSVTTDHISPAGSikedspagKWLKengvqkadfnsygsRRGNHDVMMRGTFANVriknlmipakaDGTRVEgglti 752
Cdd:cd01579 1 KVGDNITTDHIMPAGA--------KVLP--------------LRSNIPAISEFVFHRV-----------DPTFAE----- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 753 hqpsgeqlsiydaAMKYVGAGtptVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKGAD 832
Cdd:cd01579 43 -------------RAKAAGPG---FIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADED 106
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
173-517 |
8.42e-13 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 72.35 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 173 VPPGVGIVHQVNLEYLARGvhkkadGGdtvyypdTLVGTDSHT------TMingigvvgwgvggIEAEAG------MLGQ 240
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG------GK-------MILGSDSHTrygalgTM-------------AVGEGGgelvkqLLND 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 241 PVYFLTPDVVGVELKGKLREGVTATDLVLTITEMLRKEKVV-GKFVEFFGEGTKSLSLPDRATIGNMAPEYGATMGFFPV 319
Cdd:PRK11413 177 TYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 320 DEKTIEYFEGTGRTKAeiaafenYfkaQKLfgipKAGDID-YTKTVTLDLATVAPSLAGPKRPQDRIEIGNVKSTFTELF 398
Cdd:PRK11413 257 DEEVHNWLALHGRGQD-------Y---CEL----NPQPMAyYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDIL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 399 SKPVAEngfAKKAEDLNAQYTTSNgvDVKNGDVLI--AAITSCTNTSNPSVLLAAGLLAKKAVEAGltvapHIKTSLAPG 476
Cdd:PRK11413 323 REVEIE---SERVAHGKAKLSLLD--KIENGRLKVqqGIIAGCSGGNYENVIAAANALRGQSCGND-----TFSLSVYPS 392
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 500211529 477 SRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGnAGDlTP 517
Cdd:PRK11413 393 SQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFG-AGD-TP 431
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
777-897 |
1.83e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 60.59 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 777 VVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPlqFKGADSVQSLGITGEETYDIEglgddfkp 856
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDEVELDLE-------- 121
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 500211529 857 qqdvTLVIHRkNGETTRvpvlLRIDTPIEVDYYKHGGILPF 897
Cdd:PRK14023 122 ----TGVLTR-GGETFQ----LRPPPEFLLEALKEGSILEY 153
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
776-826 |
4.02e-10 |
|
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: 57.21 E-value: 4.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 500211529 776 TVVFAGEEYGTGSSR---DWAAKGtqlLGVKAVIARSFERIHRSNLVGMGVLPL 826
Cdd:cd01577 19 DIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
768-827 |
9.07e-09 |
|
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: 56.33 E-value: 9.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 768 KYVGAgtpTVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQ 827
Cdd:COG0066 61 RYQGA---DILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE 117
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
777-826 |
7.44e-07 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 49.83 E-value: 7.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 500211529 777 VVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGvLPL 826
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV 99
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
175-568 |
8.75e-06 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 49.03 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 175 PGVGIVHQVnleyLARgvhkkadggdtVYYPDTL-VGTDSHTTM-INGIGVVGWGVGGIEAEAGMLGQPVyfltPDVVGV 252
Cdd:cd01581 91 PGDGVIHSW----LNR-----------MLLPDTVgTGGDSHTRFpIGISFPAGSGLVAFAAATGVMPLDM----PESVLV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 253 ELKGKLREGVTATDLV------------LTITEMLRKEKVVGKFVEFfgEGTKSLSLPDRATIGNMAPEYGATMGFFPVD 320
Cdd:cd01581 152 RFKGKMQPGITLRDLVnaipyyaiqqglLTVEKKGKKNVFNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVRLD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 321 EKT-IEY---------------FEGTGRTKAEIAAFENYFKAQKLFGiPKAgDIDYTKTVTLDLATVA-PSLAGPKRPQD 383
Cdd:cd01581 230 KEPvIEYlesnvvlmkimiangYDDARTLLRRIIAMEEWLANPPLLE-PDA-DAEYAAVIEIDLDDIKePILACPNDPDD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 384 rieignVKsTFTELFSKPVAEnGFakkaedlnaqyttsngvdvkngdvliaaITSC-TNTSNpsVLLAAGLLAKKAVEAG 462
Cdd:cd01581 308 ------VK-LLSEVAGKKIDE-VF----------------------------IGSCmTNIGH--FRAAAKILRGKEFKPT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500211529 463 LTVAphiktslAPGSRIVTEYLTKTGLLPYLAKLGFEVAAYGCTTCIGNagdltpelNEAITKNDIVAAavlSGNRNFEA 542
Cdd:cd01581 350 RLWV-------APPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGN--------QARVADGATVFS---TSTRNFDN 411
|
410 420
....*....|....*....|....*.
gi 500211529 543 RIHPNIRAnFLASPPLVVAYAIAGNI 568
Cdd:cd01581 412 RVGKGAEV-YLGSAELAAVCALLGRI 436
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
769-825 |
3.48e-05 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 45.50 E-value: 3.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500211529 769 YVGAgtpTVVFAGEEYGTGSSRD---WAakgtqLL--GVKAVIARSFERIHRSNLVGMGVLP 825
Cdd:PRK01641 65 YQGA---SILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
776-827 |
8.25e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 42.15 E-value: 8.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 500211529 776 TVVFAGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMG-VLPLQ 827
Cdd:PLN00072 131 SIIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| |
