|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
3-711 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1113.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSRVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTS 82
Cdd:PTZ00092 188 HQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 83 IDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYL 162
Cdd:PTZ00092 268 TDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEEKVELIEKYL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 163 KAVKLFRNDQNssgEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIVSIHY 242
Cdd:PTZ00092 348 KANGLFRTYAE---QIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGFGIPEEKHEKKVKFTY 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 243 EGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFE 322
Cdd:PTZ00092 425 KGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYLEKLGFY 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 323 IVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGT 402
Cdd:PTZ00092 505 TAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGRVNIDFETEPLGS 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 403 DPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPI 482
Cdd:PTZ00092 585 DKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTYIHNPPFFQTMELEPP 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 483 ALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFIGKP 562
Cdd:PTZ00092 665 PIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRGTFANIRLINKLCGKV 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 563 APKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQ 642
Cdd:PTZ00092 745 GPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQ 824
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 643 FLPGENADSLGLSGRETFSLTFPE-ELSPGITLNIQTSTGKVFSVIASFEDDVEITLYKHGGLLNFVARK 711
Cdd:PTZ00092 825 FLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGILQYVLRK 894
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
3-712 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1060.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSRVVFEEKD---LLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPF 79
Cdd:PRK09277 182 HQVNLEYLAPVVWTREDgelVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEG 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 80 VTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESME 159
Cdd:PRK09277 262 VTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEEQVALVE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 160 TYLKAVKLFRNDqnsSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQAclNEKVGFKGFQIAAEKqkdivs 239
Cdd:PRK09277 342 AYAKAQGLWRDP---LEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK--SAELGVQGFGLDEAE------ 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 240 ihyEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKL 319
Cdd:PRK09277 411 ---EGEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLPYLEAL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 320 GFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEP 399
Cdd:PRK09277 488 GFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDIDLEKDP 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 400 LGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTK 479
Cdd:PRK09277 568 LGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPYFEGMLA 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 480 EPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI 559
Cdd:PRK09277 648 EPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMV 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 560 -GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGI 638
Cdd:PRK09277 728 pGVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGV 807
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676318078 639 APLQFLPGENADSLGLSGRETFSLTFPEELSPG--ITLNIQTSTGKV--FSVIASFEDDVEITLYKHGGLLNFVARKF 712
Cdd:PRK09277 808 LPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGatVTVVITRADGEVveFPVLCRIDTAVEVDYYRNGGILQYVLRDL 885
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
3-712 |
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: 1049.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSRVVFEEKD----LLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNP 78
Cdd:COG1048 179 HQVNLEYLAFVVWTREEdgetVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 79 FVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESM 158
Cdd:COG1048 259 GVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIELV 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 159 ETYLKAVKLFRNDqnSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGfkgfqiaaEKQKDIV 238
Cdd:COG1048 339 EAYAKAQGLWRDP--DAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG--------EELDKPV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 239 SIHYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSK 318
Cdd:COG1048 409 RVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 319 LGFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTE 398
Cdd:COG1048 489 LGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLTTD 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 399 PLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLT 478
Cdd:COG1048 569 PLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEGLQ 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 479 KEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKF 558
Cdd:COG1048 649 LEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKNLL 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 559 I-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIG 637
Cdd:COG1048 729 ApGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMG 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 638 IAPLQFLPGENADSLGLSGRETFSLT-FPEELSPG--ITLNIQTSTGKV--FSVIASFEDDVEITLYKHGGLLNFVARKF 712
Cdd:COG1048 809 VLPLQFPEGESAESLGLTGDETFDIEgLDEGLAPGktVTVTATRADGSTeeFPVLHRIDTPVEVEYYRAGGILQYVLRQL 888
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
3-712 |
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: 954.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSRVVFEE----KDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNP 78
Cdd:TIGR01341 164 HQVNLEYLATVVFKAevdgELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 79 FVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESM 158
Cdd:TIGR01341 244 GVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVELV 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 159 ETYLKAVKLFRNDqnsSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIV 238
Cdd:TIGR01341 324 EKYARAQGLFYDD---SEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKKKV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 239 sihyEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSK 318
Cdd:TIGR01341 401 ----NGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 319 LGFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTE 398
Cdd:TIGR01341 477 LGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTE 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 399 PLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLT 478
Cdd:TIGR01341 557 PIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 479 KEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKF 558
Cdd:TIGR01341 637 QDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLM 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 559 I-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIG 637
Cdd:TIGR01341 717 VkGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMG 796
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676318078 638 IAPLQFLPGENADSLGLSGRETFSLTFPEELSPGITLNIQTSTGK----VFSVIASFEDDVEITLYKHGGLLNFVARKF 712
Cdd:TIGR01341 797 VIPLQFPQGEDAETLGLTGDETIDIDGIKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
3-713 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 942.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSRVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTS 82
Cdd:PLN00070 220 HQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 83 IDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYL 162
Cdd:PLN00070 300 TDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 163 KAVKLFRNDQNSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIVSIHY 242
Cdd:PLN00070 380 RANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVAKFSF 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 243 EGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFE 322
Cdd:PLN00070 460 HGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFH 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 323 IVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGT 402
Cdd:PLN00070 540 IVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGT 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 403 DPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPI 482
Cdd:PLN00070 620 GKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPP 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 483 ALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI-GK 561
Cdd:PLN00070 700 GPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLLkGE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 562 PAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPL 641
Cdd:PLN00070 780 VGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPL 859
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676318078 642 QFLPGENADSLGLSGRETFSLTFP---EELSPGITLNIQTSTGKVFSVIASFEDDVEITLYKHGGLLNFVARKFS 713
Cdd:PLN00070 860 CFKSGEDADTLGLTGHERYTIDLPsniSEIKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFDHGGILPYVIRNLI 934
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
3-712 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 931.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSRVVFEEKD----LLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNP 78
Cdd:PRK12881 181 HQVNLEYLARVVHTKEDdgdtVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLRE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 79 FVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESM 158
Cdd:PRK12881 261 GVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTEAQIALV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 159 ETYLKAVKLFRNDQNssgEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEkqkdiv 238
Cdd:PRK12881 341 EAYAKAQGLWGDPKA---EPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKAQ------ 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 239 sihyEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSK 318
Cdd:PRK12881 412 ----TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 319 LGFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTE 398
Cdd:PRK12881 488 LGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAYALAGTVRRDLMTE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 399 PLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLT 478
Cdd:PRK12881 568 PLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKSTYIRRPPFFDFSM 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 479 KEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKF 558
Cdd:PRK12881 648 GPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMMRGTFANVRIKNLM 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 559 I-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIG 637
Cdd:PRK12881 728 IpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMG 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 638 IAPLQFLPGENADSLGLSGRETFSLT-FPEELSPG--ITLNIQTSTGKV--FSVIASFEDDVEITLYKHGGLLNFVARKF 712
Cdd:PRK12881 808 VLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRqdVTLVIHRADGSTerVPVLCRIDTPIEVDYYKAGGILPYVLRQL 887
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
1-391 |
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: 564.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 1 MAHQINLEYLSRVVF----EEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSS 76
Cdd:cd01586 95 IIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 77 NPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDnvtlkhlehtgfskakle 156
Cdd:cd01586 175 RPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------------------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 157 smetylkavklfrndqnssgepeySQVIQINLNSIVPSVSGPKRPQDRVAVtdmksdfqaclnekvgfkgfqiaaekqkd 236
Cdd:cd01586 237 ------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----------------------------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 237 ivsihyegseyklsHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYL 316
Cdd:cd01586 264 --------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYL 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676318078 317 SKLGFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 391
Cdd:cd01586 330 EKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
3-389 |
2.28e-158 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 465.74 E-value: 2.28e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLsrvvfeekdLLFPD-SVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVT 81
Cdd:pfam00330 109 HQVGLEYG---------LALPGmTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 82 SIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLEsmETY 161
Cdd:pfam00330 180 AKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKG--EAY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 162 LKAVKLFRNDqnSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSD-FQACLNEKVGFKGfqiaaekqkdiVSI 240
Cdd:pfam00330 258 DKAVAWKTLA--SDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDpFADAVKRKAAERA-----------LEY 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 241 HYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLaKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLG 320
Cdd:pfam00330 325 MGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAG 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676318078 321 FEIVGYGCSICVGNTAPLSDavlnavkqGDlvtCGILSGNKNFEGRLCDCVRAnYLASPPLVVAYAIAG 389
Cdd:pfam00330 404 FEWRGPGCSMCIGNSDRLPP--------GE---RCVSSSNRNFEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
1-391 |
2.06e-127 |
|
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: 383.39 E-value: 2.06e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 1 MAHQINLEYLsrvvfeekdLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFV 80
Cdd:cd01351 71 IIHQIMVENL---------ALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 81 TSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLesmet 160
Cdd:cd01351 142 TGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKN----- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 161 ylkAVKLFRNDQNSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSdfqaclnekvgfkgfqiaaekqkdivsi 240
Cdd:cd01351 217 ---LWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG---------------------------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 241 hyegseyklshGSVVIAAVISCTNNCnPSVMLAAGLLAKKAVeaglrVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLG 320
Cdd:cd01351 266 -----------TKIDQVLIGSCTNNR-YSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYATLSREGYYEILVDSG 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676318078 321 FEIVGYGCSICVGNTAPLsdavlnavkqGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 391
Cdd:cd01351 329 ARILPPGCGPCMGNGARL----------VADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGKI 389
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
495-663 |
4.99e-110 |
|
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: 330.39 E-value: 4.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 495 YLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFIGKPAPKTIHFPS-GQ 573
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPtGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 574 TLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLG 653
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|
gi 1676318078 654 LSGRETFSLT 663
Cdd:cd01580 161 LTGEETYDII 170
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
3-711 |
2.84e-64 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 225.41 E-value: 2.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSrvvfeekdllFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVT 81
Cdd:PRK07229 101 HQVHLERFA----------FPgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 82 SIDVVLgitKHLRQVGVAG---KFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDnvtlkhlehtgfskaklESM 158
Cdd:PRK07229 171 AKDVIL---ELLRRLTVKGgvgKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSD-----------------ERT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 159 ETYLKA-------VKLFRNDqnssgEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKsdfqaclnekvgfkgfqiaa 231
Cdd:PRK07229 231 REFLKAqgreddwVELLADP-----DAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVA-------------------- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 232 ekqkdivsihyegseyklshGSVVIAAVI-SCTnncNPS---VMLAAGLLAKKaveaglRVKPyiRTSL--SPGSGMVTH 305
Cdd:PRK07229 286 --------------------GIKVDQVLIgSCT---NSSyedLMRAASILKGK------KVHP--KVSLviNPGSRQVLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 306 YLSSSGVLPYLSKLGFEIVGYGCSICVGNT-APLSDAVlnavkqgdlvtcgIL-SGNKNFEGR---LCDCVranYLASPP 380
Cdd:PRK07229 335 MLARDGALADLIAAGARILENACGPCIGMGqAPATGNV-------------SLrTFNRNFPGRsgtKDAQV---YLASPE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 381 LVVAYAIAGTVnidfqteplgTDPTGkniyLHDIWPSREEVHRVEEEHVILSMF-----KALKDKIEMGnkrwnsleaPD 455
Cdd:PRK07229 399 TAAASALTGVI----------TDPRT----LALENGEYPKLEEPEGFAVDDAGIiapaeDGSDVEVVRG---------PN 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 456 SVLFPwdlkstyircpsffdklTKEPiaLQAIENAHVLLYLGDSVTTDHISPAGsiarnsaaAKYLTNRGltprefnsyg 535
Cdd:PRK07229 456 IKPLP-----------------LLEP--LPDLLEGKVLLKVGDNITTDHIMPAG--------AKWLPYRS---------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 536 arrgndavmtrgtfaNIklfnkfigkpaPKTIHFpsgqtldVFEAA--ELYQ--KEGIPLIILAGKKYGSGNSRDWAAKG 611
Cdd:PRK07229 499 ---------------NI-----------PNISEF-------VFEGVdnTFPEraKEQGGGIVVGGENYGQGSSREHAALA 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 612 PYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLGLSgrETFSLTFPEELSPGITLNIQTST-GKVFSVIASF 690
Cdd:PRK07229 546 PRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEG--DVLEIEDLREFLPGGPLTVVNVTkDEEIEVRHTL 623
|
730 740
....*....|....*....|.
gi 1676318078 691 EDDvEITLYKHGGLLNFVARK 711
Cdd:PRK07229 624 SER-QIEILLAGGALNLIKKK 643
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
3-391 |
6.54e-43 |
|
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: 159.54 E-value: 6.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEylsRVVFEEKDLLfpdsvvGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTS 82
Cdd:cd01585 72 HQVHLE---RFAVPGKTLL------GSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 83 IDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLEsmetyL 162
Cdd:cd01585 143 KDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVE-----L 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 163 KAvklfrnDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDmksdfqaclnekvgfkgfqiaAEKQKdivsihy 242
Cdd:cd01585 218 AA------DADA----EYDEEIEIDLSELEPLIARPHSPDNVVPVRE---------------------VAGIK------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 243 egseyklshgsVVIAAVISCTNNCNPSVMLAAGLLakkaveAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFE 322
Cdd:cd01585 260 -----------VDQVAIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGAR 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 323 IVGYGCSICVG-NTAPLSDAVlnavkqgdlvtcGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 391
Cdd:cd01585 323 ILESACGPCIGmGQAPPTGGV------------SVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
517-646 |
2.51e-40 |
|
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: 144.05 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 517 AAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILA 595
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1676318078 596 GKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPG 646
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
3-390 |
3.84e-39 |
|
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: 149.90 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 3 HQINLEYLSrvvfeekdllFPDS-VVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVT 81
Cdd:cd01584 80 HQIVLENYA----------FPGLlMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 82 SIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETy 161
Cdd:cd01584 150 PKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEF- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 162 lkAVKLFRNDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQA---CLNEKVGFKGfqiaaekqkdiv 238
Cdd:cd01584 229 --KDDLLVADEGA----EYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKngwPLDLRVGLIG------------ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 239 sihyegseyklshgsvviaaviSCTNNCNPSVMLAAGlLAKKAVEAGLRVKpyIRTSLSPGSGMVTHYLSSSGVLPYLSK 318
Cdd:cd01584 291 ----------------------SCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTITPGSEQIRATIERDGLLQTFRD 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1676318078 319 LGFEIVGYGCSICVGNTAPlsdavlNAVKQGDLVTCgILSGNKNFEGRlCDCVRA--NYLASPPLVVAYAIAGT 390
Cdd:cd01584 346 AGGIVLANACGPCIGQWDR------KDIKKGEKNTI-VTSYNRNFTGR-NDANPAthAFVASPEIVTAMAIAGT 411
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
13-391 |
2.22e-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: 143.87 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 13 VVFEEKDLLFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITK 91
Cdd:cd01583 74 VILPEKGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 92 HLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFskaklesmetylKAVKLFRND 171
Cdd:cd01583 154 KIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK------------AYWKELKSD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 172 QNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDmksdfqaclnekvgfkgfqiaAEKQK-DIVSIhyeGseykls 250
Cdd:cd01583 222 EDA----EYDKVVEIDASELEPQVAWPHSPDNVVPVSE---------------------VEGIKiDQVFI---G------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 251 hgsvviaaviSCTNNCNPSVMLAAGLLAKKaveaglRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSI 330
Cdd:cd01583 268 ----------SCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGA 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676318078 331 CVGntapLSDAVLNAvkqGDLVtcgILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 391
Cdd:cd01583 332 CLG----GHMGVLAP---GERC---VSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
13-391 |
6.77e-35 |
|
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: 137.47 E-value: 6.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 13 VVFEEKDLLFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGItk 91
Cdd:COG0065 103 VVLPEQGLVLPgMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAI-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 92 hLRQVGVAG---KFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKaklesmetylkaVKLF 168
Cdd:COG0065 181 -IGKIGADGatgKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKGRPFAP------------WRTL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 169 RNDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSdfqaclnekvgfkgfqiaaekqkdiVSIHYegseyk 248
Cdd:COG0065 248 KSDEDA----VYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEG-------------------------IKIDQ------ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 249 lshgsvviaAVI-SCTNNcnpsvML-----AAGLLakkaveAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFE 322
Cdd:COG0065 293 ---------VFIgSCTNG-----RIedlraAAEIL------KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAE 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 323 IVGYGCSICVG-NTAPLSDavlnavkqGDLVtcgILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 391
Cdd:COG0065 353 WREPGCGMCLGmNMGVLAP--------GERC---ASTSNRNFEGRMGSPGSRTYLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
13-389 |
9.85e-27 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 113.35 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 13 VVFEEKDLLFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGItk 91
Cdd:PRK00402 103 QVLPEKGLVRPgDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHI-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 92 hLRQVGVAG---KFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEhtgfskaklesmETYLKAVKLF 168
Cdd:PRK00402 181 -IGDIGVDGatyKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLK------------ERAGRDYKPW 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 169 RNDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKsdfqaclNEKVgfkgfqiaaekqkDIVSIhyeGseyk 248
Cdd:PRK00402 248 KSDEDA----EYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVE-------GTKV-------------DQVFI---G---- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 249 lshgsvviaaviSCTNNCNPSVMLAAGLLAKKaveaglRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFeIVGY-G 327
Cdd:PRK00402 297 ------------SCTNGRLEDLRIAAEILKGR------KVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGA-VVSTpT 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1676318078 328 CSICVGNtaplSDAVLnavkqGDLVTCgILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAG 389
Cdd:PRK00402 358 CGPCLGG----HMGVL-----APGEVC-LSTTNRNFKGRMGSPESEVYLASPAVAAASAVTG 409
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
13-389 |
7.07e-25 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 108.45 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 13 VVFEEKDLLFPDSVVGT-DSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITK 91
Cdd:PRK12466 112 VVAPELGLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 92 HLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKlESMETYLKAVKLFRND 171
Cdd:PRK12466 192 RIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKG-ALWDAALAYWRTLRSD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 172 QNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQAclnekvgfkgfQIAAEKQKDIV-SIHYEGSEYKLS 250
Cdd:PRK12466 271 ADA----VFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAA-----------EADPARRAAMErALDYMGLTPGTP 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 251 HGSVVIAAVI--SCTNncnpsvmlaaG----LLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIV 324
Cdd:PRK12466 336 LAGIPIDRVFigSCTN----------GriedLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWR 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676318078 325 GYGCSICVGntaplsdavLNavkqGDLVTCG---ILSGNKNFEGRLCDCVRAnYLASPPLVVAYAIAG 389
Cdd:PRK12466 406 EPGCSMCLA---------MN----DDVLAPGercASTTNRNFEGRQGPGART-HLMSPAMVAAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
17-391 |
4.87e-19 |
|
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: 89.60 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 17 EKDLLFPDSV-VGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITKHLRQ 95
Cdd:cd01582 76 EEGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 96 VGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNvtlKHLehtgfskaklesmetylkavklfrndqnss 175
Cdd:cd01582 156 DQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA---KHL------------------------------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 176 gepeysqviQINLNSIVPSVSGPkrpqDRVAVTDMKSDFQaclnekvgfkgfqiaaekQKDIvsihyegseyklshgSVV 255
Cdd:cd01582 203 ---------ILDLSTLSPYVSGP----NSVKVSTPLKELE------------------AQNI---------------KIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 256 IAAVISCTNNCNPSVMLAAGLL-AKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSICVGN 334
Cdd:cd01582 237 KAYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1676318078 335 TAPLsdavlnaVKQGDLvtcGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 391
Cdd:cd01582 317 GQGL-------LEPGEV---GISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
590-652 |
8.85e-17 |
|
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: 75.97 E-value: 8.85e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1676318078 590 PLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSL 652
Cdd:cd00404 16 PGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKL 78
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
496-643 |
3.55e-16 |
|
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: 75.17 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 496 LGDSVTTDHISPAGsiarnsaaAKYLTNRgltprefnsygarrgndavmtrgtfANIKLFNKFIGKPAPKTIHfpsgqtl 575
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLR-------------------------SNIPAISEFVFHRVDPTFA------- 41
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676318078 576 dvfEAAelyqKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQF 643
Cdd:cd01579 42 ---ERA----KAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
26-201 |
3.29e-08 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 56.94 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 26 VVGTDSHiTMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITKHLRQVG-VAGKFVE 104
Cdd:PRK11413 145 ILGSDSH-TRYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGyVKNKVME 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 105 FFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLEsmetyLKAvklfrndqnssGEPE-YSQV 183
Cdd:PRK11413 224 FVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQDYCE-----LNP-----------QPMAyYDGC 287
|
170
....*....|....*...
gi 1676318078 184 IQINLNSIVPSVSGPKRP 201
Cdd:PRK11413 288 ISVDLSAIKPMIALPFHP 305
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
19-389 |
5.76e-08 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 55.58 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 19 DLLFPDSV-VGTDSHITMVNGLGiLGWGVGGIETEAVMLGLPvsLTLPEVVGCELTGSSNPFVTSIDVV-----LGITKH 92
Cdd:cd01581 102 RMLLPDTVgTGGDSHTRFPIGIS-FPAGSGLVAFAAATGVMP--LDMPESVLVRFKGKMQPGITLRDLVnaipyYAIQQG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 93 LRQVGVAGKFVEFFG-----SGVSQLSIVDRTTIANMCPEYGA-----ILSFFPV-----DNVTL-KHLEHTGFSKA--- 153
Cdd:cd01581 179 LLTVEKKGKKNVFNGrileiEGLPDLKVEQAFELTDASAERSAaactvRLDKEPVieyleSNVVLmKIMIANGYDDArtl 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 154 --KLESMETYLKAVKLFRNDQNSsgepEYSQVIQINLNSIV-PSVSGPKRPQDRVAVTdmksdfqACLNEKV--GFKGfq 228
Cdd:cd01581 259 lrRIIAMEEWLANPPLLEPDADA----EYAAVIEIDLDDIKePILACPNDPDDVKLLS-------EVAGKKIdeVFIG-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 229 iaaekqkdivsihyegseyklshgsvviaaviSCtnncnpsvMLAAGLLakKAVEAGLRVKPYIRTSL--SPGSGMVTHY 306
Cdd:cd01581 326 --------------------------------SC--------MTNIGHF--RAAAKILRGKEFKPTRLwvAPPTRMDWAI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 307 LSSSGVLPYLSKLGFEIVGYGCSICVGNTAPLSDavlnavkqGDLVtcgILSGNKNFEGRLCDCVRAnYLASPPLVVAYA 386
Cdd:cd01581 364 LQEEGYYSIFGDAGARTEMPGCSLCMGNQARVAD--------GATV---FSTSTRNFDNRVGKGAEV-YLGSAELAAVCA 431
|
...
gi 1676318078 387 IAG 389
Cdd:cd01581 432 LLG 434
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
592-641 |
2.81e-07 |
|
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: 48.74 E-value: 2.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1676318078 592 IILAGKKYGSGNSR---DWAAKGpylLGVKAVLAESYEKIHKDHLIGIGIAPL 641
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
592-652 |
1.73e-05 |
|
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: 46.32 E-value: 1.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1676318078 592 IILAGKKYGSGNSRD---WAAKGpylLGVKAVLAESYEKIHKDHLIGIGIAPLQfLPGENADSL 652
Cdd:COG0066 67 ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDAL 126
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
20-389 |
1.86e-05 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 48.00 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 20 LLFPDSV-VGTDSH------ITMVNGLGILGWGVG-GIeteavmlglpVSLTLPEVVGCELTGSSNPFVTSIDVVLGITK 91
Cdd:PLN00094 549 MLLPDTVgTGGDSHtrfpigISFPAGSGLVAFGAAtGV----------IPLDMPESVLVRFTGTMQPGITLRDLVHAIPY 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 92 HLRQVGV-----AGKFVEFFG-----SGVSQLSIVDRTTIANMCPEYGA-----------ILSFFPVDNVTLKHLEHTGF 150
Cdd:PLN00094 619 TAIQDGLltvekKGKKNVFSGrileiEGLPHLKCEQAFELSDASAERSAagctikldkepIIEYLNSNVVMLKWMIAEGY 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 151 SKAK-LE----SMETYLKAVKLFRNDQNSsgepEYSQVIQINLNSIV-PSVSGPKRPQDrvavtdmksdfQACLNEKVGF 224
Cdd:PLN00094 699 GDRRtLErriaRMQQWLADPELLEADPDA----EYAAVIEIDMDEIKePILCAPNDPDD-----------ARLLSEVTGD 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 225 KgfqiaaekqKDIVSIHyegseyklshgsvviaaviSCTNNCNPsvMLAAGLLAKKaVEAGLRVKPYIrtslSPGSGMVT 304
Cdd:PLN00094 764 K---------IDEVFIG-------------------SCMTNIGH--FRAAGKLLND-NLSQLPTRLWV----APPTKMDE 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 305 HYLSSSGVLPYLSKLGFEIVGYGCSICVGNTAPLSDAvlnavkqgdlvtCGILS-GNKNFEGRLCDcvRAN-YLASPPLV 382
Cdd:PLN00094 809 AQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARVAEK------------STVVStSTRNFPNRLGK--GANvYLASAELA 874
|
....*..
gi 1676318078 383 VAYAIAG 389
Cdd:PLN00094 875 AVAAILG 881
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
456-628 |
2.84e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 43.31 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 456 SVLFPWDLKSTYIRCPSFFDKLTKEPIALQAIenaHVLLY-LGDSVTTDHISPAGsiarnsaaakYLTNRGLTPREFNSY 534
Cdd:PLN00072 38 SSIFPFKPLTTSSGTSSPTISDSAESTSSTTF---HGLCFvVGDNIDTDQIIPAE----------YLTLVPSKPDEYEKL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 535 GArrgndavmtrgtFAniklfnkFIGKPAPKTIHFpsgqtldvFEAAELYQKEGIpliILAGKKYGSGNSRDWAakgPYL 614
Cdd:PLN00072 105 GS------------YA-------LIGLPAFYKTRF--------VEPGEMKTKYSI---IIGGENFGCGSSREHA---PVA 151
|
170
....*....|....*..
gi 1676318078 615 LG---VKAVLAESYEKI 628
Cdd:PLN00072 152 LGaagAKAVVAESYARI 168
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
592-711 |
4.51e-04 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 41.35 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676318078 592 IILAGKKYGSGNSRD---WAAKGpylLGVKAVLAESYEKIHKDHLIGIGIaPLqFLPGENADSLGlSGREtfsLTFpeEL 668
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGL-PV-LECDEAVDKIE-DGDE---VEV--DL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1676318078 669 SPGITLNIqtSTGKVFSVIASFEDDVEItlYKHGGLLNFVARK 711
Cdd:PRK00439 120 ETGVITNL--TTGEEYKFKPIPEFMLEI--LKAGGLIEYLKKK 158
|
|
| |
