|
Name |
Accession |
Description |
Interval |
E-value |
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-900 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1646.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 1 MPHNTFDTLKTFKIGKKTCQLYSLPALGKALGVDVQRLPVSIRIVLESVLRNCDGAKVTQEHVRQLANWQANAKREDEIP 80
Cdd:PRK12881 1 MAHNLHKTLKEFDVGGKTYKFYSLPALGKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 81 FVVARVVLQDFTGVPLLADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFM 160
Cdd:PRK12881 81 FVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 161 KWGMQAFDTFGVVPPGFGIVHQVNLEYLARGVHRDKNNG--VYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQ 238
Cdd:PRK12881 161 KWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKEDDGdtVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 239 PVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVD 318
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 319 ERTIDYFEGTGRTAEEIAALEAYFKAQKMFGVPKAkDINYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTELFSK 398
Cdd:PRK12881 321 EQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKA-EPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 399 PIAENGFNQPADklhqaytTSAGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVV 478
Cdd:PRK12881 400 PVAENGFAKKAQ-------TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 479 TEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVV 558
Cdd:PRK12881 473 TEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 559 AYALAGTVTRDLMTEPVGRGKNG-DVWLGDIWPSSEEIQALLKFAMNPTAFKENYSQVKsNPGKLWENIKGVTGETYNW- 636
Cdd:PRK12881 553 AYALAGTVRRDLMTEPLGKGKDGrPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVF-KGSELWAAIEAPDGPLYDWd 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 637 PESTYIAEPPFFEGFGMTPAAMPAVKGARALGIFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHE 716
Cdd:PRK12881 632 PKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 717 IMMRGTFANVRIKNLMIPARpdgsrfEGGETLFQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLL 796
Cdd:PRK12881 712 VMMRGTFANVRIKNLMIPGK------EGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLL 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 797 GVKAVIARSFERIHRSNLVGMGVLPLQFKGGDSAQSLGIVGNETFDVTGLEGGIKPMQDVTLTIHRADGSRQDVTVLLRI 876
Cdd:PRK12881 786 GVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVTLVIHRADGSTERVPVLCRI 865
|
890 900
....*....|....*....|....
gi 489906776 877 DTPIEVDYYQHGGILPFVLRQLLA 900
Cdd:PRK12881 866 DTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-901 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 1637.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 3 HNTFDTLKTFKIGKKTCQLYSLPALGKALGvDVQRLPVSIRIVLESVLRNCDGAKVTQEHVRQLANWQANAKREDEIPFV 82
Cdd:COG1048 2 MDSFKARKTLTVGGKPYTYYSLPALEEAGG-DISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 83 VARVVLQDFTGVPLLADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFMKW 162
Cdd:COG1048 81 PARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 163 GMQAFDTFGVVPPGFGIVHQVNLEYLARGVHRDKNNG--VYYPDSLVGTDSHTTMINgigvvgwgvggiEAEAGMLGQPV 240
Cdd:COG1048 161 GQQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREEDGetVAYPDTLVGTDSHTTMINglgvlgwgvggiEAEAAMLGQPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 241 YFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDER 320
Cdd:COG1048 241 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 321 TIDYFEGTGRTAEEIAALEAYFKAQKMFGVPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTELFSKPI 400
Cdd:COG1048 321 TLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 401 AEngfnqPADKLHQAYTTSAGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTE 480
Cdd:COG1048 401 GE-----ELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 481 YLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAY 560
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAY 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 561 ALAGTVTRDLMTEPVGRGKNG-DVWLGDIWPSSEEIQALLKFAMNPTAFKENYSQVkSNPGKLWENIKGVTGETYNW-PE 638
Cdd:COG1048 556 ALAGTVDIDLTTDPLGTDKDGkPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADV-FDGDERWQALEVPAGELYDWdPD 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 639 STYIAEPPFFEGFGMTPAAMPAVKGARALGIFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIM 718
Cdd:COG1048 635 STYIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVM 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 719 MRGTFANVRIKNLMIPARpdgsrfEGGETLFQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLGV 798
Cdd:COG1048 715 MRGTFANIRIKNLLAPGT------EGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGV 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 799 KAVIARSFERIHRSNLVGMGVLPLQFKGGDSAQSLGIVGNETFDVTGLEGGIKPMQDVTLTIHRADGSRQDVTVLLRIDT 878
Cdd:COG1048 789 KAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAPGKTVTVTATRADGSTEEFPVLHRIDT 868
|
890 900
....*....|....*....|...
gi 489906776 879 PIEVDYYQHGGILPFVLRQLLAA 901
Cdd:COG1048 869 PVEVEYYRAGGILQYVLRQLLAA 891
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-901 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1637.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 1 MPHNTFDTLKTFKIGKKTCQLYSLPALGKALGVDVQRLPVSIRIVLESVLRNCDGAKVTQEHVRQLANWQANAKREDEIP 80
Cdd:PRK09277 2 SSTDSFKARKTLEVGGKSYDYYSLRALEAKGLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 81 FVVARVVLQDFTGVPLLADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFM 160
Cdd:PRK09277 82 FRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 161 KWGMQAFDTFGVVPPGFGIVHQVNLEYLARGVH-RDKNNGVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQP 239
Cdd:PRK09277 162 KWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWtREDGELVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 240 VYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDE 319
Cdd:PRK09277 242 SSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 320 RTIDYFEGTGRTAEEIAALEAYFKAQKMFGVPkAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTElfSKP 399
Cdd:PRK09277 322 ETLDYLRLTGRDEEQVALVEAYAKAQGLWRDP-LEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK--SAE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 400 IAENGFNQPADKLHQAYTtsagtkVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVT 479
Cdd:PRK09277 399 LGVQGFGLDEAEEGEDYE------LPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 480 EYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVA 559
Cdd:PRK09277 473 DYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 560 YALAGTVTRDLMTEPVGRGKNG-DVWLGDIWPSSEEIQALLKFAMNPTAFKENYSQVKSNPgKLWENIKGVTGETYNW-P 637
Cdd:PRK09277 553 YALAGTVDIDLEKDPLGTDKDGnPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGD-ERWNAIEVPEGPLYDWdP 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 638 ESTYIAEPPFFEGFGMTPAAMPAVKGARALGIFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEI 717
Cdd:PRK09277 632 DSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 718 MMRGTFANVRIKNLMIPARpdgsrfEGGETLFQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLG 797
Cdd:PRK09277 712 MMRGTFANIRIRNEMVPGV------EGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLG 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 798 VKAVIARSFERIHRSNLVGMGVLPLQFKGGDSAQSLGIVGNETFDVTGLEgGIKPMQDVTLTIHRADGSRQDVTVLLRID 877
Cdd:PRK09277 786 VKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLE-DLKPGATVTVVITRADGEVVEFPVLCRID 864
|
890 900
....*....|....*....|....
gi 489906776 878 TPIEVDYYQHGGILPFVLRQLLAA 901
Cdd:PRK09277 865 TAVEVDYYRNGGILQYVLRDLLAS 888
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
4-901 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1278.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 4 NTFDT-LKTFKIGKkTCQLYSLPALGKAlgvDVQRLPVSIRIVLESVLRNCDGAKVTQEHVRQLANWQANAKREDEIPFV 82
Cdd:PTZ00092 14 NPFEKvLKTLKDGG-SYKYYSLNELHDP---RLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 83 VARVVLQDFTGVPLLADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFMKW 162
Cdd:PTZ00092 90 PARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 163 GMQAFDTFGVVPPGFGIVHQVNLEYLARGVHrdKNNGVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYF 242
Cdd:PTZ00092 170 GSKAFKNLLIVPPGSGIVHQVNLEYLARVVF--NKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 243 LTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTI 322
Cdd:PTZ00092 248 VLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 323 DYFEGTGRTAEEIAALEAYFKAQKMFgVPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTELFSKPIAE 402
Cdd:PTZ00092 328 DYLKQTGRSEEKVELIEKYLKANGLF-RTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 403 NGFNQPADKLHQAYT-TSAGTK--VKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVT 479
Cdd:PTZ00092 407 KGFGIPEEKHEKKVKfTYKGKEytLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 480 EYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVA 559
Cdd:PTZ00092 487 KYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVA 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 560 YALAGTVTRDLMTEPVGRGKNG-DVWLGDIWPSSEEIQALLKFAMNPTAFKENYSQVKSNpGKLWENIKGVTGETYNW-P 637
Cdd:PTZ00092 567 YALAGRVNIDFETEPLGSDKTGkPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQG-NKQWNELQVPKGKLYEWdE 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 638 ESTYIAEPPFFEGFGMTPAAMPAVKGARALGIFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEI 717
Cdd:PTZ00092 646 KSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEV 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 718 MMRGTFANVRIKNLMIPArpdgsrfEGGETLFQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLG 797
Cdd:PTZ00092 726 MVRGTFANIRLINKLCGK-------VGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQG 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 798 VKAVIARSFERIHRSNLVGMGVLPLQFKGGDSAQSLGIVGNETFDVTGLEGGIKPMQDVTLTihRADGSrqDVTVLLRID 877
Cdd:PTZ00092 799 VKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQDVTVK--TDTGK--TFDTILRID 874
|
890 900
....*....|....*....|....
gi 489906776 878 TPIEVDYYQHGGILPFVLRQLLAA 901
Cdd:PTZ00092 875 TEVEVEYFKHGGILQYVLRKLVKG 898
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
17-899 |
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: 1243.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 17 KTCQLYSLPALGKALGvDVQRLPVSIRIVLESVLRNCDGAKVTQEHVRQLANWQANAKREDEIPFVVARVVLQDFTGVPL 96
Cdd:TIGR01341 1 KTYYYYSLKALEESGG-KISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 97 LADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFMKWGMQAFDTFGVVPPG 176
Cdd:TIGR01341 80 VVDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 177 FGIVHQVNLEYLARGVHRDKNNG--VYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKG 254
Cdd:TIGR01341 160 TGIIHQVNLEYLATVVFKAEVDGelTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 255 KLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTIDYFEGTGRTAEE 334
Cdd:TIGR01341 240 KLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 335 IAALEAYFKAQKMFGvPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTELFSKPIAENGFN---QPADK 411
Cdd:TIGR01341 320 VELVEKYARAQGLFY-DDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTlrkEPLKK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 412 LHQAYTTsagtKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYL 491
Cdd:TIGR01341 399 KVNGQNK----QLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 492 EKLGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAYALAGTVTRDLM 571
Cdd:TIGR01341 475 EELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLY 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 572 TEPVGRGKNGD-VWLGDIWPSSEEIQALLKFAMNPTAFKENYSQV-KSNpgKLWENIKGVTGETYNW-PESTYIAEPPFF 648
Cdd:TIGR01341 555 TEPIGTDKDGKpVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIfEGN--ERWNSIKTPSGDTYSWdEKSTYIRLPPFF 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 649 EGFGMTPAAMPAVKGARALGIFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRI 728
Cdd:TIGR01341 633 EEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRI 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 729 KNLMIPARpdgsrfEGGETLFQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFER 808
Cdd:TIGR01341 713 KNLMVKGK------EGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFER 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 809 IHRSNLVGMGVLPLQFKGGDSAQSLGIVGNETFDVTGLEgGIKPMQDVTLTIHRADGSRQDVTVLLRIDTPIEVDYYQHG 888
Cdd:TIGR01341 787 IHRSNLVGMGVIPLQFPQGEDAETLGLTGDETIDIDGIK-DLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHG 865
|
890
....*....|.
gi 489906776 889 GILPFVLRQLL 899
Cdd:TIGR01341 866 GILQYVLRKFL 876
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
20-901 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1094.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 20 QLYSLPALGKAlgvDVQRLPVSIRIVLESVLRNCDGAKVTQEHVRQLANWQANAKREDEIPFVVARVVLQDFTGVPLLAD 99
Cdd:PLN00070 62 KYYSLPALNDP---RIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFKPARVLLQDFTGVPAVVD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 100 IAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFMKWGMQAFDTFGVVPPGFGI 179
Cdd:PLN00070 139 LACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 180 VHQVNLEYLARGVHrdKNNGVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKGKLRGG 259
Cdd:PLN00070 219 VHQVNLEYLGRVVF--NTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 260 VTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTIDYFEGTGRTAEEIAALE 339
Cdd:PLN00070 297 VTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 340 AYFKAQKMF---GVPKAKDInYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTELFSKPIAENGFNQPADKLHQAY 416
Cdd:PLN00070 377 AYLRANKMFvdyNEPQQERV-YSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 417 TTS---AGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYLEK 493
Cdd:PLN00070 456 KFSfhgQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 494 LGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAYALAGTVTRDLMTE 573
Cdd:PLN00070 536 QGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 574 PVGRGKNG-DVWLGDIWPSSEEIQALLKFAMNPTAFKENYSQV-KSNPgkLWENIKGVTGETYNW-PESTYIAEPPFFEG 650
Cdd:PLN00070 616 PIGTGKDGkDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAItKGNP--MWNQLSVPSGTLYSWdPKSTYIHEPPYFKN 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 651 FGMTPAAMPAVKGARALGIFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRIKN 730
Cdd:PLN00070 694 MTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVN 773
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 731 lmiparpdgsRFEGGE----TLFQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSF 806
Cdd:PLN00070 774 ----------KLLKGEvgpkTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSF 843
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 807 ERIHRSNLVGMGVLPLQFKGGDSAQSLGIVGNE--TFDVTGLEGGIKPMQDVTLTihrADGSRQdVTVLLRIDTPIEVDY 884
Cdd:PLN00070 844 ERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHEryTIDLPSNISEIKPGQDVTVT---TDNGKS-FTCTLRFDTEVELAY 919
|
890
....*....|....*..
gi 489906776 885 YQHGGILPFVLRQLLAA 901
Cdd:PLN00070 920 FDHGGILPYVIRNLIKQ 936
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
85-566 |
0e+00 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 687.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 85 RVVLQDFTGVPLLADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFQRNRERYQFMKWGM 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 165 QAFDTFGVVPPGFGIVHQVNLEYLARGVH--RDKNNGVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYF 242
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtsEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 243 LTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTI 322
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 323 dyfegtgrtaeeiaaleayfkaqkmfgvpkakdinytkllTLDLGTVAPSLAGPKRPQDRIEignvkntftelfskpiae 402
Cdd:cd01586 241 ----------------------------------------ELDLSTVEPSVSGPKRPQDRVP------------------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 403 ngfnqpadkLHqayttsagtkvknGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTEYL 482
Cdd:cd01586 263 ---------LH-------------GSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 483 TKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNEAILGNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAYAL 562
Cdd:cd01586 321 EASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYAL 400
|
....
gi 489906776 563 AGTV 566
Cdd:cd01586 401 AGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
69-564 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 595.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 69 WQANAKREDE--IPFVVARVVLQDFTGVPLLADIAAMRSVAAKMGKDPKRIEPLVPVDLVVDHsvmidyfgTKNALDLNM 146
Cdd:pfam00330 4 WDAHLVEELDgsLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDH--------APDALDKNI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 147 KLEFQRNRERYQFMKWGMQAFDtFGVVPPGFGIVHQVNLEYlargvhrdknnGVYYPD-SLVGTDSHTTMINgigvvgwg 225
Cdd:pfam00330 76 EDEISRNKEQYDFLEWNAKKFG-IRFVPPGQGIVHQVGLEY-----------GLALPGmTIVGTDSHTTTHGglgalafg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 226 vggiEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMA 305
Cdd:pfam00330 144 vggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 306 PEYGATMGFFPVDERTIDYFEGTGRtaEEIAALEAYFKAQKMFGVPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEI 385
Cdd:pfam00330 224 IEYGATAGLFPPDETTFEYLRATGR--PEAPKGEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 386 -GNVKNTFTELFSKPIAENGFNQPADKlhqayttsAGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLaKKAVEAGLKVP 464
Cdd:pfam00330 302 sELVPDPFADAVKRKAAERALEYMGLG--------PGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 465 KHIKTSLAPGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTAdlNEAIlgndlvcsaVLSGNRNFEARIHP 544
Cdd:pfam00330 373 PGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--GERC---------VSSSNRNFEGRQGP 441
|
490 500
....*....|....*....|
gi 489906776 545 NIKAnFLASPPLVVAYALAG 564
Cdd:pfam00330 442 GGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
669-845 |
7.85e-103 |
|
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: 316.53 E-value: 7.85e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 669 IFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRIKNLMIPARpdgsrfEGGETL 748
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGT------EGGTTH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 749 FQPTGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKGGD 828
Cdd:cd01580 75 HPPTGEVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGE 154
|
170
....*....|....*..
gi 489906776 829 SAQSLGIVGNETFDVTG 845
Cdd:cd01580 155 NADSLGLTGEETYDIIG 171
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
85-566 |
4.69e-85 |
|
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: 277.84 E-value: 4.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 85 RVVLQDFTGVPLLADIAAMRSvaakmgkdPKRIEPLVPVDLVVDHSVmidyfgtknaldlnmKLEFQRNRERYQFMKWgm 164
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAA--------LGKVADPSQIACVHDHAV---------------QLEKPVNNEGHKFLSF-- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 165 qAFDTFGV--VPPGFGIVHQVNLEYLArgvhrdknngvYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYF 242
Cdd:cd01351 56 -FAALQGIafYRPGVGIIHQIMVENLA-----------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 243 LTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTI 322
Cdd:cd01351 124 KKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 323 DYFEGTGRTAEEIAALEayfkaqkmFGVPKAKDIN--YTKLLTLDLGTVAPSLAGPKRPQDRIeignvkntftelfskPI 400
Cdd:cd01351 204 KWLEATGRPLLKNLWLA--------FPEELLADEGaeYDQVIEIDLSELEPDISGPNRPDDAV---------------SV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 401 AEngfnqpadklhqayttsagtkVKNGDILIAAITSCTNtSNPSVLLAAGLLAKKAveaglKVPKHIKTSLAPGSRVVTE 480
Cdd:cd01351 261 SE---------------------VEGTKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLIVTPGSRMVYA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 481 YLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNeailgndlvcSAVLSGNRNFEARIHPNIKANFLASPPLVVAY 560
Cdd:cd01351 314 TLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGE----------VGVSSGNRNFPGRLGTYERHVYLASPELAAAT 383
|
....*.
gi 489906776 561 ALAGTV 566
Cdd:cd01351 384 AIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
78-898 |
2.48e-84 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 283.96 E-value: 2.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 78 EIPFVVARVVLQDFTGVPlladiaAMRSVAAkMGKDPkrieplVPVDLVVDHsvmIDYfgtknaldlNMKLEFQRNRERY 157
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTM------AYLQFEA-MGLDR------VKTELSVQY---VDH---------NLLQADFENADDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 158 QFMkwgMQAFDTFGVV--PPGFGIVHQVNLEYLARgvhrdknngvyyP-DSLVGTDSHTT------MIngigvvGWGVGG 228
Cdd:PRK07229 79 RFL---QSVAAKYGIYfsKPGNGICHQVHLERFAF------------PgKTLLGSDSHTPtagglgML------AIGAGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 229 IEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLtitEMLRREKV---VGKFVEFCGEGTASLSVTDRATIGNMA 305
Cdd:PRK07229 138 LDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL---ELLRRLTVkggVGKIIEYFGPGVATLSVPERATITNMG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 306 PEYGATMGFFPVDERTIDYFEGTGR--TAEEIAALE-AYfkaqkmfgvpkakdinYTKLLTLDLGTVAPSLAGPKRPqdr 382
Cdd:PRK07229 215 AELGATTSIFPSDERTREFLKAQGRedDWVELLADPdAE----------------YDEVIEIDLSELEPLIAGPHSP--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 383 ieiGNVkntftelfsKPIAEngfnqpadklhqayttSAGTKVKNGdiliaAITSCTNTSNPSVLLAAGLLAKKAVeaglk 462
Cdd:PRK07229 276 ---DNV---------VPVSE----------------VAGIKVDQV-----LIGSCTNSSYEDLMRAASILKGKKV----- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 463 vpkHIKTSL--APGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNeailgndlvcsAVLSGNRNFEA 540
Cdd:PRK07229 318 ---HPKVSLviNPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQAPATGNV-----------SLRTFNRNFPG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 541 RI-HPNIKAnFLASPPLVVAYALAGTVT--RDLMTEpvgrgkNGDvwlgdiWPsseEIQALLKFAMNPTAF---KENYSQ 614
Cdd:PRK07229 384 RSgTKDAQV-YLASPETAAASALTGVITdpRTLALE------NGE------YP---KLEEPEGFAVDDAGIiapAEDGSD 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 615 VksnpgklwENIKGVTgetynwpestyIAEPPFFEGFgmtpaamPAVKGARALGIFGDSVTTDHISPAGSiketspagKW 694
Cdd:PRK07229 448 V--------EVVRGPN-----------IKPLPLLEPL-------PDLLEGKVLLKVGDNITTDHIMPAGA--------KW 493
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 695 LKengvmkadfnsYgsrRGNheimmrgtfanvriknlmIPARPDGSrFEGGETLFqptgeqmsiydaAMKYVAQGtSSVV 774
Cdd:PRK07229 494 LP-----------Y---RSN------------------IPNISEFV-FEGVDNTF------------PERAKEQG-GGIV 527
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 775 FGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKggDSAQSLGIVGNETFDVTGLEGGIkPMQ 854
Cdd:PRK07229 528 VGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFA--DPADYDKIEEGDVLEIEDLREFL-PGG 604
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 489906776 855 DVTLTIHRADgsrQDVTVLLRIdTPIEVDYYQHGGILPFVLRQL 898
Cdd:PRK07229 605 PLTVVNVTKD---EEIEVRHTL-SERQIEILLAGGALNLIKKKL 644
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
152-566 |
2.56e-48 |
|
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: 176.49 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 152 RNRERYQFMkwgMQAFDTFGVV--PPGFGIVHQVNLEYLARgvhrdknngvyyP-DSLVGTDSHTTMINGIGVVGWGVGG 228
Cdd:cd01585 44 ENADDHRFL---QTVAARYGIYfsRPGNGICHQVHLERFAV------------PgKTLLGSDSHTPTAGGLGMLAIGAGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 229 IEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLtitEMLRREKV---VGKFVEFCGEGTASLSVTDRATIGNMA 305
Cdd:cd01585 109 LDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATITNMG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 306 PEYGATMGFFPVDERTIDYFEGTGRTAE--EIAALEayfkaqkmfgvpkakDINYTKLLTLDLGTVAPSLAGPKRPqdri 383
Cdd:cd01585 186 AELGATTSIFPSDERTREFLAAQGREDDwvELAADA---------------DAEYDEEIEIDLSELEPLIARPHSP---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 384 eiGNVkntftelfsKPIAEngfnqpadklhqayttSAGTKVKNgdiliAAITSCTNTSNPSVLLAAGLLakkaveAGLKV 463
Cdd:cd01585 247 --DNV---------VPVRE----------------VAGIKVDQ-----VAIGSCTNSSYEDLMTVAAIL------KGRRV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 464 PKHIKTSLAPGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGdltADLNEAIlgndlvcsAVLSGNRNFEARIH 543
Cdd:cd01585 289 HPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---APPTGGV--------SVRTFNRNFEGRSG 357
|
410 420
....*....|....*....|...
gi 489906776 544 PNIKANFLASPPLVVAYALAGTV 566
Cdd:cd01585 358 TKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-565 |
4.38e-47 |
|
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: 173.78 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 85 RVVLQDFTgvpllADIAAMRSVAAKMGKdpkriePLVPVDLVVDHSVMIDYFGTKNaldlnMKLEFQRNRERYQFM---- 160
Cdd:cd01584 1 RVAMQDAT-----AQMALLQFMSSGLPK------VAVPSTIHCDHLIEAQVGGEKD-----LKRAKDINKEVYDFLasag 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 161 -KWGMqafdtfGVVPPGFGIVHQVNLEYLArgvhrdknngvyYPDSL-VGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQ 238
Cdd:cd01584 65 aKYGI------GFWKPGSGIIHQIVLENYA------------FPGLLmIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 239 PVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVD 318
Cdd:cd01584 127 PWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 319 ERTIDYFEGTGRtaEEIAALEAYFKAQKmfgVPKAKDINYTKLLTLDLGTVAPSLAGPkrpqdrieignvkntFTELFSK 398
Cdd:cd01584 207 ERMKKYLKATGR--AEIADLADEFKDDL---LVADEGAEYDQLIEINLSELEPHINGP---------------FTPDLAT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 399 PIAENGfnqpadklhqayttsaGTKVKNG---DILIAAITSCTNTSNPSVLLAAGlLAKKAVEAGLKvPKHIKTsLAPGS 475
Cdd:cd01584 267 PVSKFK----------------EVAEKNGwplDLRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLK-CKSIFT-ITPGS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 476 RVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTADLNEAilgndlvCSAVLSGNRNFEARIHPNIKA-NFLASP 554
Cdd:cd01584 328 EQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEK-------NTIVTSYNRNFTGRNDANPAThAFVASP 400
|
490
....*....|.
gi 489906776 555 PLVVAYALAGT 565
Cdd:cd01584 401 EIVTAMAIAGT 411
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
691-825 |
1.07e-44 |
|
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: 157.14 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 691 AGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRIKNLMIPARpdgsrfEGGETLFQPTGEQMSIYDAAMKYVAQGT 770
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGW------RYGKVRYLPDGENPDFYDAAMRYKQHGA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489906776 771 SSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFK 825
Cdd:pfam00694 75 PIVVIGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFP 129
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
69-570 |
7.99e-42 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 158.66 E-value: 7.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 69 WQANAKRE---DEIPFV-VARVVLQDFTGvPLLadIAAMRsvaaKMGK----DPKRIeplvpVdLVVDHSVmidyfGTKN 140
Cdd:COG0065 10 LARHAGREvepGEIVLLyIDLHLVHDVTS-PQA--FEGLR----EAGGrkvwDPDRI-----V-AVFDHNV-----PTKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 141 AldlnmklefqRNRERYQFM-----KWGMQAFDTFGVvppgfGIVHQVNLEylargvhrdknNGVYYP-DSLVGTDSHTT 214
Cdd:COG0065 72 P----------KSAEQVKTLrefakEFGITFFDVGDP-----GICHVVLPE-----------QGLVLPgMTIVGGDSHTC 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 215 M----------INgigvvgwgvgGIEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVE 284
Cdd:COG0065 126 ThgafgafafgIG----------TTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 285 FCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTIDYFEgtGRTAEEIAALEAyfkaqkmfgvpkAKDINYTKLLTL 364
Cdd:COG0065 196 FAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLK--GRPFAPWRTLKS------------DEDAVYDKEVEI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 365 DLGTVAPSLAGPKRPQDRIEIGNVKNTftelfskpiaengfnqpadKLHQAYttsagtkvkngdiliaaITSCTNtsnpS 444
Cdd:COG0065 262 DASDLEPQVAWPHSPDNVVPVSELEGI-------------------KIDQVF-----------------IGSCTN----G 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 445 VL----LAAGLLakkaveAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDltadlnea 520
Cdd:COG0065 302 RIedlrAAAEIL------KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMG-------- 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489906776 521 ILGNDLVCsaVLSGNRNFE-------ARIHpnikanfLASPPLVVAYALAGTVT--RDL 570
Cdd:COG0065 368 VLAPGERC--ASTSNRNFEgrmgspgSRTY-------LASPATAAASAIAGRITdpREL 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
85-566 |
2.59e-41 |
|
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: 156.20 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 85 RVVLQDFTGvPLLadIAAMRSVAAKMGKDPKRIEplvpvdLVVDHSVMIDyfGTKNALDLNMKLEFQRnreryqfmKWGM 164
Cdd:cd01583 1 LHLVHDVTS-PQA--FEGLREAGREKVWDPEKIV------AVFDHNVPTP--DIKAAEQVKTLRKFAK--------EFGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 165 QAFDTFGVvppgfGIVHQVNLEylargvhrdknNGVYYP-DSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFL 243
Cdd:cd01583 62 NFFDVGRQ-----GICHVILPE-----------KGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 244 TPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTID 323
Cdd:cd01583 126 VPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 324 YFEGTGRtaeeiaaleAYFKAqkmfgVPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTftelfskpiaen 403
Cdd:cd01583 206 YLKGRGK---------AYWKE-----LKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI------------ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 404 gfnqpadKLHQAYttsagtkvkngdiliaaITSCTNTSNPSVLLAAGLLAKKAVEAGlkvpkhIKTSLAPGSRVVTEYLT 483
Cdd:cd01583 260 -------KIDQVF-----------------IGSCTNGRLEDLRAAAEILKGRKVADG------VRLIVVPASQRVYKQAE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 484 KTGLLPYLEKLGFDVAAYGCTTCIGnagdltadLNEAILGNDLVCsaVLSGNRNFEARI-HPNIKaNFLASPPLVVAYAL 562
Cdd:cd01583 310 KEGLIEIFIEAGAEVRPPGCGACLG--------GHMGVLAPGERC--VSTSNRNFKGRMgSPGAR-IYLASPATAAASAI 378
|
....
gi 489906776 563 AGTV 566
Cdd:cd01583 379 TGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
176-571 |
1.78e-29 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 122.21 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 176 GFGIVHQVNLEY-LARgvhrdknngvyyP-DSLVGTDSHTT----------------MingigvvgwgvggieAEAGMLG 237
Cdd:PRK00402 97 GEGICHQVLPEKgLVR------------PgDVVVGADSHTCtygalgafatgmgstdM---------------AAAMATG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 238 QpVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPV 317
Cdd:PRK00402 150 K-TWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 318 DERTIDYFEgtGRTAEEIAALEAYfkaqkmfgvpkaKDINYTKLLTLDLGTVAPSLAGPKRPQdrieigNVkntftelfs 397
Cdd:PRK00402 229 DEKTLEYLK--ERAGRDYKPWKSD------------EDAEYEEVYEIDLSKLEPQVAAPHLPD------NV--------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 398 KPIAEngfnqpadklhqayttSAGTKVkngDilIAAITSCTNTSNPSVLLAAGLLAKKaveaglKVPKHIKTSLAPGSRV 477
Cdd:PRK00402 280 KPVSE----------------VEGTKV---D--QVFIGSCTNGRLEDLRIAAEILKGR------KVAPGVRLIVIPASQK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 478 VTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGdltadlneAILGNDLVCsaVLSGNRNFEARI-HPNIKAnFLASPPL 556
Cdd:PRK00402 333 IYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHM--------GVLAPGEVC--LSTTNRNFKGRMgSPESEV-YLASPAV 401
|
410
....*....|....*..
gi 489906776 557 VVAYALAGTVT--RDLM 571
Cdd:PRK00402 402 AAASAVTGKITdpREVL 418
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
174-566 |
1.81e-24 |
|
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: 106.16 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 174 PPGFGIVHQVNLEylargvhrdknNGVYYPDSL-VGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVEL 252
Cdd:cd01582 64 PAGRGIGHQIMIE-----------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 253 KGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDertidyfegtgrta 332
Cdd:cd01582 133 KGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD-------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 333 eeiaaleayfkaqkmfgvpkakdinyTKLLTLDLGTVAPSLAGPKRPQdrieignVKNTFTELFSKPIaengfnqpadKL 412
Cdd:cd01582 199 --------------------------AKHLILDLSTLSPYVSGPNSVK-------VSTPLKELEAQNI----------KI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 413 HQAYttsagtkvkngdiliaaITSCTNTSNPSVLLAAGLL-AKKAVEAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYL 491
Cdd:cd01582 236 NKAY-----------------LVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489906776 492 EKLGFDVAAYGCTTCIGNAGDLTADLNEAIlgndlvcSAVlsgNRNFEARI-HPNIKAnFLASPPLVVAYALAGTV 566
Cdd:cd01582 299 LEAGATPLPAGCGPCIGLGQGLLEPGEVGI-------SAT---NRNFKGRMgSTEALA-YLASPAVVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
245-571 |
7.57e-22 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 99.81 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 245 PDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDERTIDY 324
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEY 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 325 FEgtGR----TAEEIAALEAYFKAqkmfgVPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEI-GNVKNtfTELFSKP 399
Cdd:PRK05478 243 LK--GRpfapKGEDWDKAVAYWKT-----LKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIdGKVPD--PEDFADP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 400 IAengfnQPADKLHQAYTT-SAGTKVKNGDILIAAITSCTNtSNPSVLLAAGLLAKkaveaGLKVPKHIKTSLAPGSRVV 478
Cdd:PRK05478 314 VK-----RASAERALAYMGlKPGTPITDIKIDKVFIGSCTN-SRIEDLRAAAAVVK-----GRKVAPGVRALVVPGSGLV 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 479 TEYLTKTGLLPYLEKLGFDVAAYGCTTCIGnagdltadLNEAILGNDLVCSAvlSGNRNFE------ARIHpnikanfLA 552
Cdd:PRK05478 383 KAQAEAEGLDKIFIEAGFEWREPGCSMCLA--------MNPDKLPPGERCAS--TSNRNFEgrqgkgGRTH-------LV 445
|
330 340
....*....|....*....|.
gi 489906776 553 SPPLVVAYALAGTVT--RDLM 571
Cdd:PRK05478 446 SPAMAAAAAITGHFVdvRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
85-570 |
8.55e-22 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 99.59 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 85 RVVLQDFTGVPLLADIAAM-RSVAAkmgkdPKRieplvpVDLVVDHSVMIDYFGTKNALD---LNMKLEFQRNRERYqfm 160
Cdd:PRK12466 30 RHLLNEYTSPQAFSGLRARgRTVRR-----PDL------TLAVVDHVVPTRPGRDRGITDpggALQVDYLRENCADF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 161 kwGMQAFDTFGvvpPGFGIVHQVNLEYlargvhrdknnGVYYPDSLVGT-DSHTTMINGIGVVGWGVGGIEAEAGMLGQP 239
Cdd:PRK12466 96 --GIRLFDVDD---PRQGIVHVVAPEL-----------GLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 240 VYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDE 319
Cdd:PRK12466 160 LVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 320 RTIDYFEGTGRtAEEIAALE---AYFKAqkmfgVPKAKDINYTKLLTLDLGTVAPSLAGPKRPQDRIEI-GNVKNtfTEL 395
Cdd:PRK12466 240 TTFDYLRGRPR-APKGALWDaalAYWRT-----LRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPItGRVPD--PAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 396 FSKPIAENGFNQPADklhqaYT-TSAGTKVKNGDILIAAITSCTNtSNPSVLLAAGllakkAVEAGLKVPKHIKTSLAPG 474
Cdd:PRK12466 312 EADPARRAAMERALD-----YMgLTPGTPLAGIPIDRVFIGSCTN-GRIEDLRAAA-----AVLRGRKVAPGVRAMVVPG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 475 SRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGnagdltadLNEAILGNDLVCSAvlSGNRNFE------ARIHpnika 548
Cdd:PRK12466 381 SGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA--------MNDDVLAPGERCAS--TTNRNFEgrqgpgARTH----- 445
|
490 500
....*....|....*....|....
gi 489906776 549 nfLASPPLVVAYALAGTVT--RDL 570
Cdd:PRK12466 446 --LMSPAMVAAAAVAGHITdvRSL 467
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
675-847 |
1.32e-19 |
|
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: 86.37 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 675 TTDHISPAGSiketspagkWLKengvmkadfnsygsrrgnheimMRGTFANVRiKNLMIPArpdgSRFEGGET---LFQP 751
Cdd:cd01578 7 TTDHISAAGP---------WLK----------------------YRGHLDNIS-NNLLIGA----INAENGKAnsvKNQV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 752 TGEQMSIYDAAMKYVAQGTSSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKggDSAQ 831
Cdd:cd01578 51 TGEYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFA--DPAD 128
|
170
....*....|....*.
gi 489906776 832 SLGIVGNETFDVTGLE 847
Cdd:cd01578 129 YDKIHPDDKVDILGLT 144
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
769-845 |
2.80e-18 |
|
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: 80.20 E-value: 2.80e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489906776 769 GTSSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFKggDSAQSLGIVGNETFDVTG 845
Cdd:cd00404 14 AGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFA--DPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
669-825 |
4.82e-18 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 80.94 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 669 IFGDSVTTDHISPAGSiketspagKWLKengvmkadfnsygsRRGNHEIMMRGTFANVriknlmiparpdgsrfeggetl 748
Cdd:cd01579 1 KVGDNITTDHIMPAGA--------KVLP--------------LRSNIPAISEFVFHRV---------------------- 36
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489906776 749 fQPTgeqmsiYDAAMKYVAQGtssVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQFK 825
Cdd:cd01579 37 -DPT------FAERAKAAGPG---FIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFA 103
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
173-827 |
1.95e-12 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 71.19 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 173 VPPGFGIVHQVNLEYLARGvhrdknngvyyPDSLVGTDSHT------TMingigvvgwgvggIEAEAG------MLGQPV 240
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG-----------GKMILGSDSHTrygalgTM-------------AVGEGGgelvkqLLNDTY 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 241 YFLTPDVVGVELKGKLRGGVTATDLVLTIT-EMLRREKVVGKFVEFCGEGTASLSVTDRATIGNMAPEYGATMGFFPVDE 319
Cdd:PRK11413 179 DIDYPGVVAVYLTGKPAPGVGPQDVALAIIgAVFKNGYVKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 320 RTIDYFEGTGRtAEEIAALE----AYfkaqkmfgvpkakdinYTKLLTLDLGTVAPSLAGPKRPQDRIEIGNVKNTFTEL 395
Cdd:PRK11413 259 EVHNWLALHGR-GQDYCELNpqpmAY----------------YDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 396 FSKpiAENGFNQPADKlhqAYTTSAGTKVKNGDILI--AAITSCTNTSNPSVLLAAGLLAKKAVEAGlkvpkHIKTSLAP 473
Cdd:PRK11413 322 LRE--VEIESERVAHG---KAKLSLLDKIENGRLKVqqGIIAGCSGGNYENVIAAANALRGQSCGND-----TFSLSVYP 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 474 GSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGnAGDLTAdlNEAIlgndlvcsAVLSGNRNFEARIHPNIKANFLAS 553
Cdd:PRK11413 392 SSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFG-AGDTPA--NNGL--------SIRHTTRNFPNREGSKPANGQMSA 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 554 PPLVVAYALAGTVTRdlmtepvgrgkngdvwlGDIWPSSEEI---QALLKFAMNPTAFKENYSQ-----VKSNPGKLWEN 625
Cdd:PRK11413 461 VALMDARSIAATAAN-----------------GGYLTSATELdcwDNVPEYAFDVTPYKNRVYQgfgkgATQQPLIYGPN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 626 IKgvtgetyNWPEstyiaeppffegfgmtpaaMPAVKGARALGIFG---DSV-TTDHISPAGsikETSPagkwLKENGVM 701
Cdd:PRK11413 524 IK-------DWPE-------------------MGALTDNILLKVCSkilDPVtTTDELIPSG---ETSS----YRSNPLG 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 702 KADFNSygSRRgNHEIMMRGTfanvRIKNLMIpARPDGsRFEGGETLFQPTGEQMSIYDAAMKYVAQGtsSVVFGGEEyG 781
Cdd:PRK11413 571 LAEFTL--SRR-DPGYVGRSK----AVAELEN-QRLAG-NVSELTEVFARIKQIAGQEHIDPLQTEIG--SMVYAVKP-G 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 489906776 782 TGSSRDWAAKGTQLLGVKAVIARSF--ERiHRSNLVGMGVLPLQFKGG 827
Cdd:PRK11413 639 DGSAREQAASCQRVLGGLANIAEEYatKR-YRSNVINWGMLPFQMAEE 685
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
773-893 |
1.32e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 60.97 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 773 VVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLqfkggdsaqslgivgnETFDVTG-LEGGik 851
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPF----------------ESEEVVDaLEDG-- 113
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489906776 852 pmQDVTLTIHRADGSRQDVTVLLRIDTPIEVDYYQHGGILPF 893
Cdd:PRK14023 114 --DEVELDLETGVLTRGGETFQLRPPPEFLLEALKEGSILEY 153
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
767-822 |
4.08e-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: 4.08e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489906776 767 AQGTSSVVFGGEEYGTGSSR---DWAAKGtqlLGVKAVIARSFERIHRSNLVGMGVLPL 822
Cdd:cd01577 14 ARFLGDIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
670-865 |
1.49e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 54.83 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 670 FGDSVTTDHISPAGSIKETSPAgkwlkengvmkadfnsygsrrgnheimmrgTFAnvriKNLMIPARPDgsrfeggetlF 749
Cdd:PRK00439 7 FGDNIDTDVIIPARYLNTSDPQ------------------------------ELA----KHCMEDLDPE----------F 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 750 qptgeqmsiydaaMKYVAQGtsSVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGvLPL------- 822
Cdd:PRK00439 43 -------------AKKVKPG--DIIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPVlecdeav 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489906776 823 -QFKGGDSAQ---SLGIVGNETfdvTGLEGGIKPMQDVTLTIHRADG 865
Cdd:PRK00439 107 dKIEDGDEVEvdlETGVITNLT---TGEEYKFKPIPEFMLEILKAGG 150
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
772-823 |
1.70e-08 |
|
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: 55.56 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489906776 772 SVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMGVLPLQ 823
Cdd:COG0066 66 DILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE 117
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
764-856 |
2.03e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 47.16 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489906776 764 KYVAQGTS----SVVFGGEEYGTGSSRDWAAKGTQLLGVKAVIARSFERIHRSNLVGMG-VLPL--------QFKGGDSA 830
Cdd:PLN00072 119 RFVEPGEMktkySIIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPLesevriceECKTGDVV 198
|
90 100
....*....|....*....|....*....
gi 489906776 831 Q---SLGIVGNETfdvTGLEGGIKPMQDV 856
Cdd:PLN00072 199 TvelGNSVLINHT---TGKEYKLKPIGDA 224
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
768-821 |
1.87e-04 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 43.58 E-value: 1.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489906776 768 QGtSSVVFGGEEYGTGSSRD---WAakgtqLL--GVKAVIARSFERIHRSNLVGMGVLP 821
Cdd:PRK01641 66 QG-ASILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLP 118
|
|
| |
