|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
1-887 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1669.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 1 MQNNPYP--TSELKiEGQTFKFYNLVELFGDKVTRLPYSIRILLEQAVRNCDGFNVKKEDVERILNWEETSKKDTEVAFK 78
Cdd:PTZ00092 11 SRPNPFEkvLKTLK-DGGSYKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 79 PARVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRFLKW 158
Cdd:PTZ00092 90 PARVLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 159 GSSAFKNFEIVPPGSGIVHQVNLEYLARVVFEKDSLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTSMVL 238
Cdd:PTZ00092 170 GSKAFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 239 PQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDY 318
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 319 LKQTGRSEEKCSLITQYLKAAHLFY-EESQTTFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEFTQGLTAPVSFKGF 397
Cdd:PTZ00092 330 LKQTGRSEEKVELIEKYLKANGLFRtYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 398 NV---KAAQDVEFQYQGQKYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVTQYY 474
Cdd:PTZ00092 410 GIpeeKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 475 KAAGLDVFLDQLGFHNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVAFAL 554
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYAL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 555 AGRMDIDFESEPIG-VVNGQSVFLKDIWPTRDEIKQLEDQVVQPQMFIQTYQQIKQGTKNWNELQVPKDQLYQWDQQSTY 633
Cdd:PTZ00092 570 AGRVNIDFETEPLGsDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTY 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 634 IHHPPYFQGLSLELPVINPVTNAYCLAVFGDSITTDHIqSSWQYFCKTVLLVDIFKERGVAQKDFNTYGARRGNDEIMVR 713
Cdd:PTZ00092 650 IHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHI-SPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVR 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 714 GTFANVRIKNKMLqGKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISY 793
Cdd:PTZ00092 729 GTFANIRLINKLC-GKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESF 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 794 ERIHRSNLAGMGVLPLEFTNGQTPESLGLTGHELFTLNVNKDNIKVNQivEVVVKKSDDTTfnFNTLLRLDTDVELEYYK 873
Cdd:PTZ00092 808 ERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSGELKPGQ--DVTVKTDTGKT--FDTILRIDTEVEVEYFK 883
|
890
....*....|....
gi 145521803 874 HGGILQYVLRKILK 887
Cdd:PTZ00092 884 HGGILQYVLRKLVK 897
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-887 |
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: 1458.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 3 NNPYPT-SELKIEGQTFKFYNL--VELFGDKVTRLPYSIRILLEQAVRNCDGFNVKKEDVERILNWEETSKKDTEVAFKP 79
Cdd:COG1048 2 MDSFKArKTLTVGGKPYTYYSLpaLEEAGGDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 80 ARVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRFLKWG 159
Cdd:COG1048 82 ARVLMQDFTGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 160 SSAFKNFEIVPPGSGIVHQVNLEYLARVVFEKD----SLLYPDSVVGTDSHTTMINglgvlgwgvggIEAEANMLGECTS 235
Cdd:COG1048 162 QQAFDNFRVVPPGTGIVHQVNLEYLAFVVWTREedgeTVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQPVS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 236 MVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKT 315
Cdd:COG1048 242 MLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 316 IDYLKQTGRSEEKCSLITQYLKAAHLFYEESQTT--FSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEFTQGLTAPvs 393
Cdd:COG1048 322 LDYLRLTGRSEEQIELVEAYAKAQGLWRDPDAPEpyYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAP-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 394 fkgFNVKAAQDVEFQYQGQKYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVTQY 473
Cdd:COG1048 400 ---VGEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 474 YKAAGLDVFLDQLGFHNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVAFA 553
Cdd:COG1048 477 LERAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 554 LAGRMDIDFESEPIGV-VNGQSVFLKDIWPTRDEIKQLEDQVVQPQMFIQTYQQIKQGTKNWNELQVPKDQLYQWDQQST 632
Cdd:COG1048 557 LAGTVDIDLTTDPLGTdKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDST 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 633 YIHHPPYFQGLSLELPVINPVTNAYCLAVFGDSITTDHI-------QSS--WQYFcktvllvdifKERGVAQKDFNTYGA 703
Cdd:COG1048 637 YIRRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHIspagaikADSpaGRYL----------LEHGVEPKDFNSYGS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 704 RRGNDEIMVRGTFANVRIKNKMLQGKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQ 783
Cdd:COG1048 707 RRGNHEVMMRGTFANIRIKNLLAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 784 GVKAVIAISYERIHRSNLAGMGVLPLEFTNGQTPESLGLTGHELFTLNVNKDNIKVNQIVEVVVKKSDDTTFNFNTLLRL 863
Cdd:COG1048 787 GVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIEGLDEGLAPGKTVTVTATRADGSTEEFPVLHRI 866
|
890 900
....*....|....*....|....
gi 145521803 864 DTDVELEYYKHGGILQYVLRKILK 887
Cdd:COG1048 867 DTPVEVEYYRAGGILQYVLRQLLA 890
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
1-887 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1454.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 1 MQNNPYPT-SELKIEGQTFKFYNLVEL----FGDkVTRLPYSIRILLEQAVRNCDGFNVKKEDVERILNWEETSKKDTEV 75
Cdd:PRK09277 2 SSTDSFKArKTLEVGGKSYDYYSLRALeakgLGD-ISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 76 AFKPARVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRF 155
Cdd:PRK09277 81 PFRPARVVMQDFTGVPAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 156 LKWGSSAFKNFEIVPPGSGIVHQVNLEYLARVVFEK---DSLLYPDSVVGTDSHTTMINglgvlgwgvggIEAEANMLGE 232
Cdd:PRK09277 161 LKWGQKAFDNFRVVPPGTGICHQVNLEYLAPVVWTRedgELVAYPDTLVGTDSHTTMINglgvlgwgvggIEAEAAMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 233 CTSMVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVD 312
Cdd:PRK09277 241 PSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 313 NKTIDYLKQTGRSEEKCSLITQYLKAAHLFYEESQT-TFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEFTQglTAP 391
Cdd:PRK09277 321 EETLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLEEpVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK--SAE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 392 VSFKGFNVKAAQdvefqyQGQKYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVT 471
Cdd:PRK09277 399 LGVQGFGLDEAE------EGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 472 QYYKAAGLDVFLDQLGFHNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVA 551
Cdd:PRK09277 473 DYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 552 FALAGRMDIDFESEPIGV-VNGQSVFLKDIWPTRDEIKQLEDQVVQPQMFIQTYQQIKQGTKNWNELQVPKDQLYQWDQQ 630
Cdd:PRK09277 553 YALAGTVDIDLEKDPLGTdKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPD 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 631 STYIHHPPYFQGLSLELPVINPVTNAYCLAVFGDSITTDHIQSS---------WQYfcktvLLvdifkERGVAQKDFNTY 701
Cdd:PRK09277 633 STYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAgaikadspaGKY-----LL-----EHGVEPKDFNSY 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 702 GARRGNDEIMVRGTFANVRIKNKMLQGKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPY 781
Cdd:PRK09277 703 GSRRGNHEVMMRGTFANIRIRNEMVPGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTR 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 782 LQGVKAVIAISYERIHRSNLAGMGVLPLEFTNGQTPESLGLTGHELFTLnVNKDNIKVNQIVEVVVKKSDDTTFNFNTLL 861
Cdd:PRK09277 783 LLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDI-EGLEDLKPGATVTVVITRADGEVVEFPVLC 861
|
890 900
....*....|....*....|....*.
gi 145521803 862 RLDTDVELEYYKHGGILQYVLRKILK 887
Cdd:PRK09277 862 RIDTAVEVDYYRNGGILQYVLRDLLA 887
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
3-887 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1283.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 3 NNPYP---TSELKIEGQTF-KFYNLVELFGDKVTRLPYSIRILLEQAVRNCDGFNVKKEDVERILNWEETSKKDTEVAFK 78
Cdd:PLN00070 42 ENPFKgilTSLPKPGGGEFgKYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 79 PARVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRFLKW 158
Cdd:PLN00070 122 PARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 159 GSSAFKNFEIVPPGSGIVHQVNLEYLARVVFEKDSLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTSMVL 238
Cdd:PLN00070 202 GSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 239 PQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDY 318
Cdd:PLN00070 282 PGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 319 LKQTGRSEEKCSLITQYLKAAHLF--YEESQ--TTFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEFTQGLTAPVSF 394
Cdd:PLN00070 362 LKLTGRSDETVAMIEAYLRANKMFvdYNEPQqeRVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGF 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 395 KGFNV-KAAQD--VEFQYQGQKYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVT 471
Cdd:PLN00070 442 KGFAVpKEAQSkvAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVT 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 472 QYYKAAGLDVFLDQLGFHNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVA 551
Cdd:PLN00070 522 KYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVA 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 552 FALAGRMDIDFESEPIGV-VNGQSVFLKDIWPTRDEIKQLEDQVVQPQMFIQTYQQIKQGTKNWNELQVPKDQLYQWDQQ 630
Cdd:PLN00070 602 YALAGTVDIDFEKEPIGTgKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 631 STYIHHPPYFQGLSLELPVINPVTNAYCLAVFGDSITTDHIqSSWQYFCKTVLLVDIFKERGVAQKDFNTYGARRGNDEI 710
Cdd:PLN00070 682 STYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHI-SPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEI 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 711 MVRGTFANVRIKNKMLQGKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIA 790
Cdd:PLN00070 761 MARGTFANIRIVNKLLKGEVGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIA 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 791 ISYERIHRSNLAGMGVLPLEFTNGQTPESLGLTGHELFTLNV--NKDNIKVNQIVEVVVkksdDTTFNFNTLLRLDTDVE 868
Cdd:PLN00070 841 KSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLpsNISEIKPGQDVTVTT----DNGKSFTCTLRFDTEVE 916
|
890
....*....|....*....
gi 145521803 869 LEYYKHGGILQYVLRKILK 887
Cdd:PLN00070 917 LAYFDHGGILPYVIRNLIK 935
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
1-887 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1273.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 1 MQNNPYPT-SELKIEGQTFKFYNLVELF---GDKVTRLPYSIRILLEQAVRNCDGFNVKKEDVERILNWEETSKKDTEVA 76
Cdd:PRK12881 1 MAHNLHKTlKEFDVGGKTYKFYSLPALGkelGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 77 FKPARVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRFL 156
Cdd:PRK12881 81 FVPARVVMQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 157 KWGSSAFKNFEIVPPGSGIVHQVNLEYLARVVFEK----DSLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGE 232
Cdd:PRK12881 161 KWGMQAFDNFRVVPPGTGIMHQVNLEYLARVVHTKeddgDTVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 233 CTSMVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVD 312
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 313 NKTIDYLKQTGRSEEKCSLITQYLKAAHLFYEESQT-TFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEFTQGLTAP 391
Cdd:PRK12881 321 EQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKAEpRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 392 VSFKGFNVKAAQDVEfqyqgqkYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVT 471
Cdd:PRK12881 401 VAENGFAKKAQTSNG-------VDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 472 QYYKAAGLDVFLDQLGFHNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVA 551
Cdd:PRK12881 474 EYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVA 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 552 FALAGRMDIDFESEPIGV-VNGQSVFLKDIWPTRDEIKQLEDQVVQPQMFIQTYQQIKQGTKNWNELQVPKDQLYQWDQQ 630
Cdd:PRK12881 554 YALAGTVRRDLMTEPLGKgKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPK 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 631 STYIHHPPYFQGLSLELPVINPVTNAYCLAVFGDSITTDHIqSSWQYFCKTVLLVDIFKERGVAQKDFNTYGARRGNDEI 710
Cdd:PRK12881 634 STYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHI-SPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEV 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 711 MVRGTFANVRIKNKMLQGKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIA 790
Cdd:PRK12881 713 MMRGTFANVRIKNLMIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIA 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 791 ISYERIHRSNLAGMGVLPLEFTNGQTPESLGLTGHELFTLNVNKDNIKVNQIVEVVVKKSDDTTFNFNTLLRLDTDVELE 870
Cdd:PRK12881 793 ESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEGLPGEIKPRQDVTLVIHRADGSTERVPVLCRIDTPIEVD 872
|
890
....*....|....*..
gi 145521803 871 YYKHGGILQYVLRKILK 887
Cdd:PRK12881 873 YYKAGGILPYVLRQLLA 889
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
16-886 |
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: 1251.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 16 QTFKFYNLVELF--GDKVTRLPYSIRILLEQAVRNCDGFNVKKEDVERILNWEETSKKDTEVAFKPARVILQDFTGVPLV 93
Cdd:TIGR01341 1 KTYYYYSLKALEesGGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 94 VDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRFLKWGSSAFKNFEIVPPGS 173
Cdd:TIGR01341 81 VDLAAMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 174 GIVHQVNLEYLARVVF--EKDSLL--YPDSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTSMVLPQVVGFKLTGQ 249
Cdd:TIGR01341 161 GIIHQVNLEYLATVVFkaEVDGELtaYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 250 LSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDYLKQTGRSEEKC 329
Cdd:TIGR01341 241 LQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 330 SLITQYLKAAHLFYEES-QTTFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEFTQGLTAPVSFKGFNVKaAQDVEFQ 408
Cdd:TIGR01341 321 ELVEKYARAQGLFYDDSeEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLR-KEPLKKK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 409 YQGQKYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVTQYYKAAGLDVFLDQLGF 488
Cdd:TIGR01341 400 VNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELGF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 489 HNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVAFALAGRMDIDFESEPIG 568
Cdd:TIGR01341 480 NLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPIG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 569 V-VNGQSVFLKDIWPTRDEIKQLEDQVVQPQMFIQTYQQIKQGTKNWNELQVPKDQLYQWDQQSTYIHHPPYFQGLSLEL 647
Cdd:TIGR01341 560 TdKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQDP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 648 PVINPVTNAYCLAVFGDSITTDHIqSSWQYFCKTVLLVDIFKERGVAQKDFNTYGARRGNDEIMVRGTFANVRIKNKMLQ 727
Cdd:TIGR01341 640 EEVEDIKGARILLLLGDSITTDHI-SPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMVK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 728 GKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISYERIHRSNLAGMGVL 807
Cdd:TIGR01341 719 GKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGVI 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 808 PLEFTNGQTPESLGLTGHElfTLNVNKD-NIKVNQIVEVVVKKSDDTTFNFNTLLRLDTDVELEYYKHGGILQYVLRKIL 886
Cdd:TIGR01341 799 PLQFPQGEDAETLGLTGDE--TIDIDGIkDLKPGKEVTVTFTNSKGEKITFKCVLRIDTEVELDYYKHGGILQYVLRKFL 876
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
81-558 |
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: 721.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 81 RVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSVQVDFHGNQNAREQNEQTEFERNLERFRFLKWGS 160
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 161 SAFKNFEIVPPGSGIVHQVNLEYLARVVF----EKDSLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTSM 236
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 237 VLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDnkti 316
Cdd:cd01586 161 LLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 317 dylkqtgrseekcslitqylkaahlfyeesqttfSDTLELDLSTIQPCVAGPKRPQDRVNLsqlkqeftqgltapvsfkg 396
Cdd:cd01586 237 ----------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 397 fnvkaaqdvefqyqgqkyslnHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGLAIRPYIKTSLSPGSQCVTQYYKA 476
Cdd:cd01586 264 ---------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 477 AGLDVFLDQLGFHNTGYGCMTCIGNSGPIDQAVSETVSNNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVAFALAG 556
Cdd:cd01586 323 SGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAG 402
|
..
gi 145521803 557 RM 558
Cdd:cd01586 403 TV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
60-556 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 600.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 60 ERILNWEETSKKDTEVAFKPARVILQDFTGVPLVVDLAAMRSQAQAMGKDPQLINPLCPVDLVIDHSvqvdfhgnQNARE 139
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 140 QNEQTEFERNLERFRFLKWGSSAFkNFEIVPPGSGIVHQVNLEYLarvvfekdsLLYPD-SVVGTDSHTTMINglgvlgw 218
Cdd:pfam00330 73 KNIEDEISRNKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEYG---------LALPGmTIVGTDSHTTTHGglgalaf 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 219 gvggIEAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNM 298
Cdd:pfam00330 143 gvggSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 299 APEYGATMGFFPVDNKTIDYLKQTGRSEEKCslITQYLKAAHLFYEESQT--TFSDTLELDLSTIQPCVAGPKRPQDRVN 376
Cdd:pfam00330 223 AIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPgaEYDKVVEIDLSTIEPMVTGPTRPQDAVP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 377 LSQL-KQEFTQGLTAPVSFKgfnvkaaqDVEFQYQGQKYSLNHGSVVIAAITSCTNTSNPGVMLAAGLVaKKAVQAGLAI 455
Cdd:pfam00330 301 LSELvPDPFADAVKRKAAER--------ALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 456 RPYIKTSLSPGSQCVTQYYKAAGLDVFLDQLGFHNTGYGCMTCIGNSGPIDqavsetvsNNDlvvAAVLSGNRNFEGRVH 535
Cdd:pfam00330 372 APGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP--------PGE---RCVSSSNRNFEGRQG 440
|
490 500
....*....|....*....|.
gi 145521803 536 PITRAnYLASPPLVVAFALAG 556
Cdd:pfam00330 441 PGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
661-830 |
3.39e-84 |
|
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: 266.83 E-value: 3.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 661 VFGDSITTDHIqSSWQYFCKTVLLVDIFKERGVAQKDFNTYGARRGNDEIMVRGTFANVRIKNKMLQGKECPNTIYVPTG 740
Cdd:cd01580 1 LLGDSVTTDHI-SPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 741 EVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISYERIHRSNLAGMGVLPLEFTNGQTPESL 820
Cdd:cd01580 80 EVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSL 159
|
170
....*....|
gi 145521803 821 GLTGHELFTL 830
Cdd:cd01580 160 GLTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
81-556 |
2.73e-81 |
|
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: 267.44 E-value: 2.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 81 RVILQDFTGVPLVVDLAAMRsqaqAMGKdpqlINPLCPVDLVIDHSVQVDFHgnqnareqneqtefeRNLERFRFLKWGS 160
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILA----ALGK----VADPSQIACVHDHAVQLEKP---------------VNNEGHKFLSFFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 161 safKNFEI--VPPGSGIVHQVNLEYLArvvfekdslLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTSMVL 238
Cdd:cd01351 58 ---ALQGIafYRPGVGIIHQIMVENLA---------LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 239 PQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDY 318
Cdd:cd01351 126 PEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKW 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 319 LKQTGRSEEKcslITQYLKAAHLFYEEsQTTFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLKQEftqgltapvsfkgfn 398
Cdd:cd01351 206 LEATGRPLLK---NLWLAFPEELLADE-GAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEGT--------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 399 vkaaqdvefqyqgqkyslnhgSVVIAAITSCTNtSNPGVMLAAGLVAKKAVQAglairPYIKTSLSPGSQCVTQYYKAAG 478
Cdd:cd01351 267 ---------------------KIDQVLIGSCTN-NRYSDMLAAAKLLKGAKVA-----PGVRLIVTPGSRMVYATLSREG 319
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145521803 479 LDVFLDQLGFHNTGYGCMTCIGNSGPIdqavsetvsnNDLVVAAVLSGNRNFEGRVHPITRANYLASPPLVVAFALAG 556
Cdd:cd01351 320 YYEILVDSGARILPPGCGPCMGNGARL----------VADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAG 387
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
59-884 |
5.46e-74 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 255.46 E-value: 5.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 59 VERILN---WEETSKKDTEVAFKPARVILQDFTGVPlvvdlaAMRsQAQAMGKDpQLINPLcpvdlvidhSVQ-VDfHgn 134
Cdd:PRK07229 6 TEKILYahlVEGELEPGEEIAIRIDQTLTQDATGTM------AYL-QFEAMGLD-RVKTEL---------SVQyVD-H-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 135 qnareQNEQTEFErNLERFRFLKwgsSAFKNFEIV--PPGSGIVHQVNLEYLARvvfekdsllyP-DSVVGTDSHTT--- 208
Cdd:PRK07229 66 -----NLLQADFE-NADDHRFLQ---SVAAKYGIYfsKPGNGICHQVHLERFAF----------PgKTLLGSDSHTPtag 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 209 ---MInglgvlgwgvgGI-----EAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLtctEMLRKKKV---VGKFV 277
Cdd:PRK07229 127 glgML-----------AIgagglDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL---ELLRRLTVkggVGKII 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 278 EFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDYLKQTGRSEEKCSLitqylkaahlfYEESQTTFSDTLELD 357
Cdd:PRK07229 193 EYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKAQGREDDWVEL-----------LADPDAEYDEVIEID 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 358 LSTIQPCVAGPkrpqdrvnlsqlkqeFTQGLTAPVS-FKGFNVkaaqdvefqYQGqkyslnhgsvviaAITSCTNTSNPG 436
Cdd:PRK07229 262 LSELEPLIAGP---------------HSPDNVVPVSeVAGIKV---------DQV-------------LIGSCTNSSYED 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 437 VMLAAGLVAKKAVQAglairpyiKTSL--SPGSQCVtqYYKAA---GLDVFLDqLG--FHNTGygCMTCIGnsgpIDQA- 508
Cdd:PRK07229 305 LMRAASILKGKKVHP--------KVSLviNPGSRQV--LEMLArdgALADLIA-AGarILENA--CGPCIG----MGQAp 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 509 VSETVSnndlvvaaVLSGNRNFEGRV-HPITRAnYLASPPLVVAFALAGRMDiDfesepigvvngqsvflkdiwPTRDEI 587
Cdd:PRK07229 368 ATGNVS--------LRTFNRNFPGRSgTKDAQV-YLASPETAAASALTGVIT-D--------------------PRTLAL 417
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 588 KQLEDQVVQ-PQMFIQTYQQIKQGTKNWNELQVPKDqlyqwdqqsTYIHHPPYFQGL--SLELPVinpvtnaycLAVFGD 664
Cdd:PRK07229 418 ENGEYPKLEePEGFAVDDAGIIAPAEDGSDVEVVRG---------PNIKPLPLLEPLpdLLEGKV---------LLKVGD 479
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 665 SITTDHIQSSwqyfcktvllvdifkergvaqkdfntyGAR----RGN-DEImvrgtfANvriknkmlqgkecpntiYVPT 739
Cdd:PRK07229 480 NITTDHIMPA---------------------------GAKwlpyRSNiPNI------SE-----------------FVFE 509
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 740 GEVVAIYDAAEKYLHSnqqtIVIGGAEYGSGSSRDWAAKGP-YLqGVKAVIAISYERIHRSNLAGMGVLPLEFTNGQTPE 818
Cdd:PRK07229 510 GVDNTFPERAKEQGGG----IVVGGENYGQGSSREHAALAPrYL-GVKAVLAKSFARIHKANLINFGILPLTFADPADYD 584
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145521803 819 SLGLtGHELFTLNVnKDNIKvNQIVEVVVKKSDDTtfnFNTLLRLdTDVELEYYKHGGILQYVLRK 884
Cdd:PRK07229 585 KIEE-GDVLEIEDL-REFLP-GGPLTVVNVTKDEE---IEVRHTL-SERQIEILLAGGALNLIKKK 643
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
143-556 |
5.94e-46 |
|
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: 169.55 E-value: 5.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 143 QTEFeRNLERFRFLKwgsSAFKNFEIV--PPGSGIVHQVNLEYLARvvfekdsllyP-DSVVGTDSHTTMINGLGVLGWG 219
Cdd:cd01585 40 QTDF-ENADDHRFLQ---TVAARYGIYfsRPGNGICHQVHLERFAV----------PgKTLLGSDSHTPTAGGLGMLAIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 220 VGGIEAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLtctEMLRKKKV---VGKFVEFYGPGVSTLSLADRATVS 296
Cdd:cd01585 106 AGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATIT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 297 NMAPEYGATMGFFPVDNKTIDYLKQTGRSEEkcsliTQYLKAahlfyeESQTTFSDTLELDLSTIQPCVAGPKRPQdrvn 376
Cdd:cd01585 183 NMGAELGATTSIFPSDERTREFLAAQGREDD-----WVELAA------DADAEYDEEIEIDLSELEPLIARPHSPD---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 377 lsqlkqeftqgltapvsfkgfNVKAAQDVEfqyqGQKyslnhgsVVIAAITSCTNTSNPGVMLAAGLVAKKAVQaglair 456
Cdd:cd01585 248 ---------------------NVVPVREVA----GIK-------VDQVAIGSCTNSSYEDLMTVAAILKGRRVH------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 457 PYIKTSLSPGSQCVTQYYKAAGLDVFLDQLGFHNTGYGCMTCIGnsgpIDQA-VSETVSnndlvvaaVLSGNRNFEGRVH 535
Cdd:cd01585 290 PHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIG----MGQApPTGGVS--------VRTFNRNFEGRSG 357
|
410 420
....*....|....*....|.
gi 145521803 536 PITRANYLASPPLVVAFALAG 556
Cdd:cd01585 358 TKDDLVYLASPEVAAAAALTG 378
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
118-558 |
5.78e-44 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 164.54 E-value: 5.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 118 PVDLVIDHSVQVDFHGNQNAREQNEQteferNLERFRFLkwgSSAFKNFEI--VPPGSGIVHQVNLEYLArvvfekdsll 195
Cdd:cd01584 27 PSTIHCDHLIEAQVGGEKDLKRAKDI-----NKEVYDFL---ASAGAKYGIgfWKPGSGIIHQIVLENYA---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 196 YPDS-VVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVG 274
Cdd:cd01584 89 FPGLlMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 275 KFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDYLKQTGRSEekcslITQYLK--AAHLFYEESQTTFSD 352
Cdd:cd01584 169 AIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAE-----IADLADefKDDLLVADEGAEYDQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 353 TLELDLSTIQPCVAGPkrpqdrvnlsqlkqeFTQGLTAPVSFKGFNVKAaqdvefqyqgQKYSLNhgsVVIAAITSCTNT 432
Cdd:cd01584 244 LIEINLSELEPHINGP---------------FTPDLATPVSKFKEVAEK----------NGWPLD---LRVGLIGSCTNS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 433 SNPGVMLAAGlVAKKAVQAGLaiRPYIKTSLSPGSQCVTQYYKAAGLDVFLDQLGFHNTGYGCMTCIG--NSGPIDQAVS 510
Cdd:cd01584 296 SYEDMGRAAS-IAKQALAHGL--KCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGqwDRKDIKKGEK 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 145521803 511 ETVsnndlvvaaVLSGNRNFEGR--VHPITRAnYLASPPLVVAFALAGRM 558
Cdd:cd01584 373 NTI---------VTSYNRNFTGRndANPATHA-FVASPEIVTAMAIAGTL 412
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
689-814 |
2.65e-43 |
|
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: 153.29 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 689 KERGVAQKDFNTYGARRGNDEIMVRGTFANVRIKNKMLQGKECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYG 768
Cdd:pfam00694 6 KLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIGGKNFG 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 145521803 769 SGSSRDWAAKGPYLQGVKAVIAISYERIHRSNLAGMGVLPLEFTNG 814
Cdd:pfam00694 86 CGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
81-557 |
1.83e-38 |
|
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: 148.64 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 81 RVILQDFTGvPLVVDlaAMRsqaqAMGK----DPQLInplcpVdLVIDHSVQVDfhgNQNAREQneQTEFERNLERF--R 154
Cdd:COG0065 30 LHLVHDVTS-PQAFE--GLR----EAGGrkvwDPDRI-----V-AVFDHNVPTK---DPKSAEQ--VKTLREFAKEFgiT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 155 FLKWGSSafknfeivppgsGIVHQVNLEY-LARvvfekdsllyP-DSVVGTDSHTTM----------INGLgvlgwgvgg 222
Cdd:COG0065 92 FFDVGDP------------GICHVVLPEQgLVL----------PgMTIVGGDSHTCThgafgafafgIGTT--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 223 iEAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLtctEMLRKKKV---VGKFVEFYGPGVSTLSLADRATVSNMA 299
Cdd:COG0065 141 -DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLIL---AIIGKIGAdgaTGKAIEFAGEAIRALSMEERMTLCNMA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 300 PEYGATMGFFPVDNKTIDYLKQTGRSEEKcslitqYLKA---AHlfyeesqttFSDTLELDLSTIQPCVAGPKRPQDRVN 376
Cdd:COG0065 217 IEAGAKAGIIAPDETTFEYLKGRPFAPWR------TLKSdedAV---------YDKEVEIDASDLEPQVAWPHSPDNVVP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 377 LSQLKqeftqgltapvsfkgfnvkaaqDVEFQYqgqkyslnhgsvviAAITSCTNtsnpgvmlaaG----LVAKKAVQAG 452
Cdd:COG0065 282 VSELE----------------------GIKIDQ--------------VFIGSCTN----------GriedLRAAAEILKG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 453 LAIRPYIKTSLSPGSQCVTQYYKAAGLD-VFLDQlGFHNTGYGCMTCIGnsGPIDQAVSETVsnndlvvaAVLSGNRNFE 531
Cdd:COG0065 316 RKVAPGVRAIVVPGSQEVYRQAEAEGLDeIFIEA-GAEWREPGCGMCLG--MNMGVLAPGER--------CASTSNRNFE 384
|
490 500
....*....|....*....|....*.
gi 145521803 532 GRVHPITRANYLASPPLVVAFALAGR 557
Cdd:COG0065 385 GRMGSPGSRTYLASPATAAASAIAGR 410
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
81-557 |
3.21e-37 |
|
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: 144.25 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 81 RVILQDFTGvPLVVdlAAMRsqaQAMGK---DPQLINplcpvdLVIDHSVQVDfhgNQNAREQNEqtEFERNLERFRFlk 157
Cdd:cd01583 1 LHLVHDVTS-PQAF--EGLR---EAGREkvwDPEKIV------AVFDHNVPTP---DIKAAEQVK--TLRKFAKEFGI-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 158 wgssafKNFEIVppGSGIVHQVNLE-YLARvvfekdsllyP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEANMLGECTS 235
Cdd:cd01583 62 ------NFFDVG--RQGICHVILPEkGLTL----------PgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLW 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 236 MVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKT 315
Cdd:cd01583 124 FRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 316 IDYLKQTGRSEEKcslitqylkaahLFYEESQTTFSDTLELDLSTIQPCVAGPKRPQdrvnlsqlkqeftqgltapvsfk 395
Cdd:cd01583 204 FEYLKGRGKAYWK------------ELKSDEDAEYDKVVEIDASELEPQVAWPHSPD----------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 396 gfNVKAAQDVEfqyqGQKyslnhgsVVIAAITSCTNTSNPGVMLAAGLVAKKAVQaglairPYIKTSLSPGSQCVtqyYK 475
Cdd:cd01583 249 --NVVPVSEVE----GIK-------IDQVFIGSCTNGRLEDLRAAAEILKGRKVA------DGVRLIVVPASQRV---YK 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 476 AA---GLD-VFLDqLGFHNTGYGCMTCIGnsGPIDqavsetVSNNDLVVAAvlSGNRNFEGRVHPITRANYLASPPLVVA 551
Cdd:cd01583 307 QAekeGLIeIFIE-AGAEVRPPGCGACLG--GHMG------VLAPGERCVS--TSNRNFKGRMGSPGARIYLASPATAAA 375
|
....*.
gi 145521803 552 FALAGR 557
Cdd:cd01583 376 SAITGE 381
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
121-557 |
9.85e-32 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 128.76 E-value: 9.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 121 LVIDHSVQVDfhgNQNAREQNEQT-EF--ERNLERFrflkwgssafknFEIvppGSGIVHQVNLEY-LARvvfekdslly 196
Cdd:PRK00402 61 IVFDHFVPAK---DIKSAEQQKILrEFakEQGIPNF------------FDV---GEGICHQVLPEKgLVR---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 197 P-DSVVGTDSHTT----------------MinglgvlgwgvggieAEANMLGECTSMVlPQVVGFKLTGQLSAHISATDL 259
Cdd:PRK00402 113 PgDVVVGADSHTCtygalgafatgmgstdM---------------AAAMATGKTWFKV-PETIKVVLEGKLPPGVTAKDV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 260 VLtctEMLRKKKVVG---KFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTIDYLKQTGRSEEKcslitqyl 336
Cdd:PRK00402 177 IL---HIIGDIGVDGatyKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKERAGRDYK-------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 337 kaahLFYEESQTTFSDTLELDLSTIQPCVAGPKRPQdrvnlsqlkqeftqgltapvsfkgfNVKAAQDVEfqyqGQKysl 416
Cdd:PRK00402 246 ----PWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPD-------------------------NVKPVSEVE----GTK--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 417 nhgsVVIAAITSCTNtsnpGVM----LAAglvakkAVQAGLAIRPYIKTSLSPGSQCVtqyYKAA---GL-DVFLDqLGF 488
Cdd:PRK00402 290 ----VDQVFIGSCTN----GRLedlrIAA------EILKGRKVAPGVRLIVIPASQKI---YLQAlkeGLiEIFVD-AGA 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145521803 489 HNTGYGCMTCIGNS----GPIDQAVSETvsnndlvvaavlsgNRNFEGRV-HPiTRANYLASPPLVVAFALAGR 557
Cdd:PRK00402 352 VVSTPTCGPCLGGHmgvlAPGEVCLSTT--------------NRNFKGRMgSP-ESEVYLASPAVAAASAVTGK 410
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
82-558 |
2.46e-25 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 109.46 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 82 VILQDFTGvPLVVDlaAMRSQAQAMGKDPQLINplcpvdLVIDHSVQVdfhgnqNAREQNEQTEFERnlerfRFLKwgSS 161
Cdd:TIGR01343 28 AMVHDITA-PLAIK--TLEEYGIDKVWNPEKIV------IVFDHQVPA------DTIKAAEMQKLAR-----EFVK--KQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 162 AFKNFeiVPPGSGIVHQVnleylarvvFEKDSLLYP-DSVVGTDSHTTMINGLGVLGWGVGGIE-AEANMLGEcTSMVLP 239
Cdd:TIGR01343 86 GIKYF--YDVGEGICHQV---------LPEKGLVKPgDLVVGADSHTCTYGAFGAFATGMGSTDmAYAIATGK-TWFKVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 240 QVVGFKLTGQLSAHISATDLVLtctEMLRKKKVVG---KFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTI 316
Cdd:TIGR01343 154 ETIRVNITGKLNPGVTAKDVIL---EVIGEIGVDGatyMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 317 DYLKQTGRSEEKcslITQYLKAAHlFYEEsqttfsdtLELDLSTIQPCVAGPKRPQdrvnlsqlkqeftqgltapvsfkg 396
Cdd:TIGR01343 231 QYLKERRKEPFR---VYKSDEDAE-YAKE--------IEIDASQIEPVVACPHNVD------------------------ 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 397 fNVKAAQDVEfqyqgqkyslnHGSVVIAAITSCTNTSNPGVMLAAGLVAKKAVQaglairPYIKTSLSPGSQCV-TQYYK 475
Cdd:TIGR01343 275 -NVKPVSEVE-----------GTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVA------PDVRLIVIPASRAVyLQALK 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 476 AAGLDVFLDqlgfhntgYGCMTCIGNSGPIDQAVSETVSNNDLVVAavlSGNRNFEGRVHPITRANYLASPPLVVAFALA 555
Cdd:TIGR01343 337 EGLIEIFVK--------AGAVVSTPGCGPCLGSHQGVLAPGEVCIS---TSNRNFKGRMGHPNAEIYLASPATAAASAVK 405
|
...
gi 145521803 556 GRM 558
Cdd:TIGR01343 406 GYI 408
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
81-557 |
3.75e-23 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 103.83 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 81 RVILQDFTGVPLVVDLAA----MRSQAQAMGkdpqlinplcpvdlVIDHSVQVDFHGNQNAREQNEQ---TEFERNLERF 153
Cdd:PRK12466 30 RHLLNEYTSPQAFSGLRArgrtVRRPDLTLA--------------VVDHVVPTRPGRDRGITDPGGAlqvDYLRENCADF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 154 rflkwgssAFKNFEIVPPGSGIVHqvnleylarVVFEKDSLLYPDSVVGT-DSHTTM----------INGLgvlgwgvgg 222
Cdd:PRK12466 96 --------GIRLFDVDDPRQGIVH---------VVAPELGLTLPGMVIVCgDSHTTTygalgalafgIGTS--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 223 iEAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEY 302
Cdd:PRK12466 150 -EVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 303 GATMGFFPVDNKTIDYLKqtGRseekcsliTQYLKAAHL---------FYEESQTTFSDTLELDLSTIQPCVAGPKRPQD 373
Cdd:PRK12466 229 GARGGLIAPDETTFDYLR--GR--------PRAPKGALWdaalaywrtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 374 RVNLS-----------QLKQEFTQ------GLTAPVSFKGFNVKAAqdveFqyqgqkyslnhgsvviaaITSCTNTSNPG 436
Cdd:PRK12466 299 AVPITgrvpdpaaeadPARRAAMEraldymGLTPGTPLAGIPIDRV----F------------------IGSCTNGRIED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 437 VMLAAglvakkAVQAGLAIRPYIKTSLSPGSQCVTQYYKAAGLD-VFLDQlGFHNTGYGCMTCIGnsgpidqavsetvsN 515
Cdd:PRK12466 357 LRAAA------AVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLArIFIAA-GFEWREPGCSMCLA--------------M 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 145521803 516 NDLVVAA----VLSGNRNFEGRVHPITRAnYLASPPLVVAFALAGR 557
Cdd:PRK12466 416 NDDVLAPgercASTTNRNFEGRQGPGART-HLMSPAMVAAAAVAGH 460
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
143-558 |
1.54e-21 |
|
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: 97.30 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 143 QTEFERNLERFRFLKwgSSAFKN-FEIVPPGSGIVHQVNLEylarvvfekDSLLYPDSV-VGTDSHTTMINGLGVLGWGV 220
Cdd:cd01582 38 QNKSEKNLKKYKNIE--SFAKKHgIDFYPAGRGIGHQIMIE---------EGYAFPGTLaVASDSHSNMYGGVGCLGTPI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 221 GGIEAEANMLGECTSMVLPQVVGFKLTGQLSAHISATDLVLTCTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAP 300
Cdd:cd01582 107 VRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 301 EYGATMGFFPVDNKtidylkqtgrseekcslitqylkaaHLFyeesqttfsdtleLDLSTIQPCVAGPkrpqDRVNLSQL 380
Cdd:cd01582 187 EWGALSGLFPTDAK-------------------------HLI-------------LDLSTLSPYVSGP----NSVKVSTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 381 KQEFTQgltapvsfkgfnvkaaQDVEFQYqgqkyslnhgsvviAAITSCTNTSNPGVMLAAGLV-AKKAVQAGLAIRPYI 459
Cdd:cd01582 225 LKELEA----------------QNIKINK--------------AYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 460 KTSLSPGSQCVTQYYKAAGLDVFLDQLGFHNTGYGCMTCIG-NSG---PIDQAVSETvsnndlvvaavlsgNRNFEGRVH 535
Cdd:cd01582 275 EFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGlGQGllePGEVGISAT--------------NRNFKGRMG 340
|
410 420
....*....|....*....|...
gi 145521803 536 PITRANYLASPPLVVAFALAGRM 558
Cdd:cd01582 341 STEALAYLASPAVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
760-830 |
2.66e-19 |
|
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: 83.29 E-value: 2.66e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145521803 760 IVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISYERIHRSNLAGMGVLPLEFTNGQtpESLGLTGHELFTL 830
Cdd:cd00404 18 VVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE--DYLKLHTGDELDI 86
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
233-557 |
5.01e-17 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 84.79 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 233 CTSMVLPQVVGFKLTGQLSAHISATDLVLtctEMLRKKKV---VGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFF 309
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIIL---AIIGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 310 PVDNKTIDYLKqtGR----SEEKCSLITQYLKAahlFYEESQTTFSDTLELDLSTIQPCVAGPKRPQDRVNLSQLkqeft 385
Cdd:PRK05478 234 APDETTFEYLK--GRpfapKGEDWDKAVAYWKT---LKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGK----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 386 qgLTAPVSFKGFNVKAAQDVEFQYQGqkysLNHG------SVVIAAITSCTNTSNPGVMLAAGLVAKKAVQAGlairpyI 459
Cdd:PRK05478 304 --VPDPEDFADPVKRASAERALAYMG----LKPGtpitdiKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPG------V 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 460 KTSLSPGSQCVTQYYKAAGLD-VFLDQlGFHNTGYGCMTCIGnsgpidqavsetvSNNDLVVA---AVLSGNRNFEGRVH 535
Cdd:PRK05478 372 RALVVPGSGLVKAQAEAEGLDkIFIEA-GFEWREPGCSMCLA-------------MNPDKLPPgerCASTSNRNFEGRQG 437
|
330 340
....*....|....*....|..
gi 145521803 536 PITRaNYLASPPLVVAFALAGR 557
Cdd:PRK05478 438 KGGR-THLVSPAMAAAAAITGH 458
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
758-813 |
1.72e-15 |
|
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: 73.63 E-value: 1.72e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 145521803 758 QTIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISYERIHRSNLAGMGVLPLEFTN 813
Cdd:cd01579 49 PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFAD 104
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
713-813 |
6.56e-14 |
|
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: 69.80 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 713 RGTFANvrIKNKMLQG------KECPNTIYVPTGEVVAIYDAAEKYLHSNQQTIVIGGAEYGSGSSRDWAAKGPYLQGVK 786
Cdd:cd01578 21 RGHLDN--ISNNLLIGainaenGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGR 98
|
90 100
....*....|....*....|....*..
gi 145521803 787 AVIAISYERIHRSNLAGMGVLPLEFTN 813
Cdd:cd01578 99 AIITKSFARIHETNLKKQGLLPLTFAD 125
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
760-880 |
1.61e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 57.89 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 760 IVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISYERIHRSNLAGMGVLPleFTNGQTPESLgltghelftlnvnKDNIKV 839
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDAL-------------EDGDEV 116
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 145521803 840 NQIVEVVVKKSDDTTFNfntlLRLDTDVELEYYKHGGILQY 880
Cdd:PRK14023 117 ELDLETGVLTRGGETFQ----LRPPPEFLLEALKEGSILEY 153
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
751-810 |
6.66e-09 |
|
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: 53.75 E-value: 6.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145521803 751 KYLHSnqqtIVIGGAEYGSGSSR---DWAAKGpylQGVKAVIAISYERIHRSNLAGMGVLPLE 810
Cdd:cd01577 15 RFLGD----IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVT 70
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
169-371 |
1.09e-07 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 55.79 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 169 VPPGSGIVHQVNLEYLARVvfekdsllyPDSVVGTDSHT------TMinglgvlgwgvgGI-----EAEANMLGECTSMV 237
Cdd:PRK11413 123 VPPHIAVIHQYMREMMAGG---------GKMILGSDSHTrygalgTM------------AVgegggELVKQLLNDTYDID 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 238 LPQVVGFKLTGQLSAHISATDLVLT-CTEMLRKKKVVGKFVEFYGPGVSTLSLADRATVSNMAPEYGATMGFFPVDNKTI 316
Cdd:PRK11413 182 YPGVVAVYLTGKPAPGVGPQDVALAiIGAVFKNGYVKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVH 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 145521803 317 DYLKQTGRSEEKCSlitqyLKAAHLFYeesqttFSDTLELDLSTIQPCVAGPKRP 371
Cdd:PRK11413 262 NWLALHGRGQDYCE-----LNPQPMAY------YDGCISVDLSAIKPMIALPFHP 305
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
759-810 |
4.26e-07 |
|
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: 51.33 E-value: 4.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 145521803 759 TIVIGGAEYGSGSSRD---WAAKGpYlqGVKAVIAISYERIHRSNLAGMGVLPLE 810
Cdd:COG0066 66 DILVAGRNFGCGSSREhapWALKD-Y--GFRAVIAPSFADIFYRNAINNGLLPIE 117
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
760-885 |
7.27e-06 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 47.13 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145521803 760 IVIGGAEYGSGSSRD---WAAKGpylQGVKAVIAISYERIHRSNLAGMGvLPleftngqtpeslgltgheLFTLNVNKDN 836
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIG-LP------------------VLECDEAVDK 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 145521803 837 IKVNQIVEV------VVKKSDDTTFNFNTLlrldTDVELEYYKHGGILQYVLRKI 885
Cdd:PRK00439 109 IEDGDEVEVdletgvITNLTTGEEYKFKPI----PEFMLEILKAGGLIEYLKKKG 159
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
759-810 |
3.26e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.39 E-value: 3.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 145521803 759 TIVIGGAEYGSGSSRDWAAKGPYLQGVKAVIAISYERI-HRSNLAGMGVLPLE 810
Cdd:PLN00072 131 SIIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIfFRNSVATGEVYPLE 183
|
|
| |
