|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
1-751 |
0e+00 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 1643.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 1 MIKLSEKGVFLASNNEIIAEEHFTGEIKKEEAKKGTIAWSILSSHNTSGNMDKLKIKFDSLASHDITFVGIVQTAKASGM 80
Cdd:PRK11413 1 MIKLSEKGVYLASGNEIIAEEHFTGEIKKEEAKKGTIAWSILSSHNTSGNMDKLKIKFDSLASHDITFVGIIQTAKASGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 81 ERFPLPYVLTNCHNSLCAVGGTINGDDHVFGLSAAQRYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHTRYGALGTM 160
Cdd:PRK11413 81 ERFPLPYVLTNCHNSLCAVGGTINEDDHVFGLSAAQKYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHTRYGALGTM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 161 AVGEGGGELVKQLLNDTWDIDYPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGYVKNKVMEFVGPGVSALSTDFRNSV 240
Cdd:PRK11413 161 AVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVKNKVMEFVGPGVSALSTDFRNGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 241 DVMTTETTCLSSVWQTDEEVHNWLALHGRGQDYCQLNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDTLNQNLTD 320
Cdd:PRK11413 241 DVMTTETTCLSSIWQTDEEVHNWLALHGRGQDYCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 321 ILREIEIESERVAHGKAKLSLLDKVENGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLAVYPSSQPVFMDL 400
Cdd:PRK11413 321 ILREVEIESERVAHGKAKLSLLDKIENGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLSVYPSSQPVFMDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 401 AKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNGLSIRHTTRNFPNREGSKPANGQMSAVALMDARSIAATAANGGYLT 480
Cdd:PRK11413 401 AKKGVVADLMGAGAIIRTAFCGPCFGAGDTPANNGLSIRHTTRNFPNREGSKPANGQMSAVALMDARSIAATAANGGYLT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 481 SASELDCWDNVPEYAFDVTPYKNRVYQGFVKGATQQPLIYGPNIKDWPELGALTDNIVLKVCSKILDEVTTTDELIPSGE 560
Cdd:PRK11413 481 SATELDCWDNVPEYAFDVTPYKNRVYQGFGKGATQQPLIYGPNIKDWPEMGALTDNILLKVCSKILDPVTTTDELIPSGE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 561 TSSYRSNPIGLAEFTLSRRDPGYVGRSKATAELENQRLAGNVSELTEVFARIKQIAGQEHIDPLQTEIGSMVYAVKPGDG 640
Cdd:PRK11413 561 TSSYRSNPLGLAEFTLSRRDPGYVGRSKAVAELENQRLAGNVSELTEVFARIKQIAGQEHIDPLQTEIGSMVYAVKPGDG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 641 SAREQAASCQRVIGGLANIAEEYATKRYRSNVINWGMLPLQMAEVPTFEVGDYIYIPGIKAALDNPGTTFKGYVIHEDAP 720
Cdd:PRK11413 641 SAREQAASCQRVLGGLANIAEEYATKRYRSNVINWGMLPFQMAEEPTFEVGDYIYIPGIRAALDNPGTTFKGYVIHEDAP 720
|
730 740 750
....*....|....*....|....*....|.
gi 1344182769 721 VTEITLYMESLTAEEREIIKAGSLINFNKNR 751
Cdd:PRK11413 721 VTEITLYMESLTAEEREIIKAGCLINYNKNR 751
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
41-470 |
9.38e-113 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 349.41 E-value: 9.38e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 41 ILSSHNTSGNMDKLKIKFDSLASHDITFVGIVQTAKASGMERFPLPYVlTNCHNSLCAVG---------------GTING 105
Cdd:pfam00330 3 IWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGT-PATIDHLVPTDlvidhapdaldknieDEISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 106 DDHVFGL--SAAQRYGGIFVPPHIAVIHQYMREM-MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTWDID 181
Cdd:pfam00330 82 NKEQYDFleWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTtHGGLGALAFGVGGSEAEHVLATQPLEMK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 182 YPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVH 261
Cdd:pfam00330 162 KPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGT-GKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 262 NWLALHGR-----GQDYCQ------LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDTLNQNLTDilREIEIESE 330
Cdd:pfam00330 241 EYLRATGRpeapkGEAYDKavawktLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPFA--DAVKRKAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 331 RVAHGKAKLSLLDKVENGrlKVQQGIIAGCSGGNYENVIAAANALR-----GQSCGNDtFSLAVYPSSQPVFMDLAKKGV 405
Cdd:pfam00330 319 ERALEYMGLGPGTPLSDG--KVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPG-VKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1344182769 406 VADLIGAGAIIRTAFCGPCFGAGDTPINNGLSIRHTTRNFPNREGsKPANGQMSAVALMDARSIA 470
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIGNSDRLPPGERCVSSSNRNFEGRQG-PGGRTHLASPALVAAAAIA 459
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
36-752 |
3.69e-97 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 314.39 E-value: 3.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 36 TIAWSILSSHNTSGNMDK---LKIKFDSLASHDITFVGIVQTAKASGMERFPLPYVLTNC-HNSLCAvgGTINGDDHVFG 111
Cdd:PRK07229 4 TLTEKILYAHLVEGELEPgeeIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYVdHNLLQA--DFENADDHRFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 112 LSAAQRYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHL 190
Cdd:PRK07229 82 QSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTpTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 191 TGKPAPYVGPQDVALAIIG--AVfKNGyvKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHG 268
Cdd:PRK07229 162 TGKLPPWVSAKDVILELLRrlTV-KGG--VGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKAQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 269 RGQDYCQLNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIdtlnqnltdilREIEieservahgkaklslldkveng 348
Cdd:PRK07229 239 REDDWVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPV-----------SEVA---------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 349 RLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTfSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAG 428
Cdd:PRK07229 286 GIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKV-SLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 429 DTPINNGLSIRHTTRNFPNRegskpaNGQMSAVALMDARSIAATAANGGYLTSASELDcWDNVPEYAFDVT---PYKNRV 505
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGR------SGTKDAQVYLASPETAAASALTGVITDPRTLA-LENGEYPKLEEPegfAVDDAG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 506 YQGFVKGATQQPLIYGPNIKDWPELGALTDNIVLKVCSKILDEVtTTDELIPSG-ETSSYRSNPIGLAEFTLSRRDPGYV 584
Cdd:PRK07229 438 IIAPAEDGSDVEVVRGPNIKPLPLLEPLPDLLEGKVLLKVGDNI-TTDHIMPAGaKWLPYRSNIPNISEFVFEGVDNTFP 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 585 GRSKATaelenqrlAGNVseltevfarikqIAGQEHidplqteigsmvYavkpGDGSAREQAASCQRVIGGLANIAEEYA 664
Cdd:PRK07229 517 ERAKEQ--------GGGI------------VVGGEN------------Y----GQGSSREHAALAPRYLGVKAVLAKSFA 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 665 tkR-YRSNVINWGMLPLQMAEVPT---FEVGDYIYIPGIKAALdnPGTTFKGYVIHEDapvTEITLYMEsLTAEEREIIK 740
Cdd:PRK07229 561 --RiHKANLINFGILPLTFADPADydkIEEGDVLEIEDLREFL--PGGPLTVVNVTKD---EEIEVRHT-LSERQIEILL 632
|
730
....*....|..
gi 1344182769 741 AGSLINFNKNRQ 752
Cdd:PRK07229 633 AGGALNLIKKKL 644
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
77-477 |
3.12e-67 |
|
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: 226.95 E-value: 3.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 77 ASGMERFPLPYVLTNC-HNSLCAvgGTINGDDHVFGLSAAQRYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHT-RY 154
Cdd:cd01585 19 AMGVDRVRTELSVSYVdHNTLQT--DFENADDHRFLQTVAARYGIYFSRPGNGICHQVHLERFAVPGKTLLGSDSHTpTA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 155 GALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALST 234
Cdd:cd01585 97 GGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGV-GKIFEYTGPGVATLSV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 235 DFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHGRGQDYCQLNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIdtl 314
Cdd:cd01585 176 PERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPV--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 315 nqnltdilREIeieservahgkaklslldkvenGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTfSLAVYPSSQ 394
Cdd:cd01585 253 --------REV----------------------AGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHV-SMVVAPGSK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 395 PVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNGLSIRHTTRNFPNREGSKPAngqmsAVALMDARSIAATAA 474
Cdd:cd01585 302 QVLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTGGVSVRTFNRNFEGRSGTKDD-----LVYLASPEVAAAAAL 376
|
...
gi 1344182769 475 NGG 477
Cdd:cd01585 377 TGV 379
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
60-473 |
6.80e-47 |
|
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: 171.53 E-value: 6.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 60 SLASHDITFVGIVQTAKASGMERFPLPYVLTNC-HNSLCAVGGTINGDDHVFGLSAAQRYGGIFVPPHIAVIHQYMREMM 138
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGKVADPSQIACvHDHAVQLEKPVNNEGHKFLSFFAALQGIAFYRPGVGIIHQIMVENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 139 AGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGyV 217
Cdd:cd01351 81 ALPGDLLVGSDSHTTsYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG-V 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 218 KNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHGR-------GQDYCQLNPQPMAYYDGCISV 290
Cdd:cd01351 160 LNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRpllknlwLAFPEELLADEGAEYDQVIEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 291 DLSAIKPMIALPFHPSNVYEIdtlnqnltdilreieieservahgkaklslldkVENGRLKVQQGIIAGCSGGNYENVIA 370
Cdd:cd01351 240 DLSELEPDISGPNRPDDAVSV---------------------------------SEVEGTKIDQVLIGSCTNNRYSDMLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 371 AANALRGQScGNDTFSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNG-LSIRHTTRNFPNRE 449
Cdd:cd01351 287 AAKLLKGAK-VAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGeVGVSSGNRNFPGRL 365
|
410 420
....*....|....*....|....
gi 1344182769 450 GSKPANGQMSAVALMDARSIAATA 473
Cdd:cd01351 366 GTYERHVYLASPELAAATAIAGKI 389
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
129-485 |
3.56e-40 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 153.02 E-value: 3.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 129 VIHQYMREM-MAGGGKMILGSDSHT-RYGALGTMAVGEGGGEL-VKQLLNDTWdIDYPGVVAVHLTGKPAPYVGPQDVAL 205
Cdd:PRK00402 100 ICHQVLPEKgLVRPGDVVVGADSHTcTYGALGAFATGMGSTDMaAAMATGKTW-FKVPETIKVVLEGKLPPGVTAKDVIL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 206 AIIGAVFKNG--YvknKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHgRGQDYCQLNPQPMAY 283
Cdd:PRK00402 179 HIIGDIGVDGatY---KALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER-AGRDYKPWKSDEDAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 284 YDGCISVDLSAIKPMIALPFHPSNVYEIDtlnqnltdilreieieservahgkaklslldkvENGRLKVQQGIIAGCSGG 363
Cdd:PRK00402 255 YEEVYEIDLSKLEPQVAAPHLPDNVKPVS---------------------------------EVEGTKVDQVFIGSCTNG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 364 NYENVIAAANALRGQSCGNDTfSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNGLSIRHTT- 442
Cdd:PRK00402 302 RLEDLRIAAEILKGRKVAPGV-RLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTn 380
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1344182769 443 RNFPNREGSKPangqmSAVALMDARSIAATAANgGYLTSASEL 485
Cdd:PRK00402 381 RNFKGRMGSPE-----SEVYLASPAVAAASAVT-GKITDPREV 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
129-476 |
3.76e-40 |
|
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: 151.96 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 129 VIHQYMREM-MAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLL-NDTWdIDYPGVVAVHLTGKPAPYVGPQDVAL 205
Cdd:cd01583 71 ICHVILPEKgLTLPGMTIVGGDSHTcTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 206 AIIGaVFKNGYVKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLAlhGRGQDYCQ-LNPQPMAYY 284
Cdd:cd01583 150 YIIG-KIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLK--GRGKAYWKeLKSDEDAEY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 285 DGCISVDLSAIKPMIALPFHPSNVYEIDtlnqnltdilreieieservahgkaklslldkvENGRLKVQQGIIAGCSGGN 364
Cdd:cd01583 227 DKVVEIDASELEPQVAWPHSPDNVVPVS---------------------------------EVEGIKIDQVFIGSCTNGR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 365 YENVIAAANALRGQSCgNDTFSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNG-LSIRHTTR 443
Cdd:cd01583 274 LEDLRAAAEILKGRKV-ADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGeRCVSTSNR 352
|
330 340 350
....*....|....*....|....*....|...
gi 1344182769 444 NFPNREGSKPAngqmsAVALMDARSIAATAANG 476
Cdd:cd01583 353 NFKGRMGSPGA-----RIYLASPATAAASAITG 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
129-485 |
1.59e-39 |
|
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: 151.34 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 129 VIHQYMREM-MAGGGKMILGSDSHT-RYGALGTMAVGEGGGE----LVKQllnDTWdIDYPGVVAVHLTGKPAPYVGPQD 202
Cdd:COG0065 100 ICHVVLPEQgLVLPGMTIVGGDSHTcTHGAFGAFAFGIGTTDvahvLATG---TLW-FKVPETMRIEVTGKLPPGVTAKD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 203 VALAIIGAVFKNGyVKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLAlhGRG-QDYCQLNPQPM 281
Cdd:COG0065 176 LILAIIGKIGADG-ATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLK--GRPfAPWRTLKSDED 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 282 AYYDGCISVDLSAIKPMIALPFHPSNVYEIDTLnqnltdilreieieservahgkaklslldkvenGRLKVQQGIIAGCS 361
Cdd:COG0065 253 AVYDKEVEIDASDLEPQVAWPHSPDNVVPVSEL---------------------------------EGIKIDQVFIGSCT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 362 GGNYENVIAAANALRGQSCgNDTFSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNG-LSIRH 440
Cdd:COG0065 300 NGRIEDLRAAAEILKGRKV-APGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGeRCAST 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1344182769 441 TTRNFPNREGSKpangqMSAVALMDARSIAATAANgGYLTSASEL 485
Cdd:COG0065 379 SNRNFEGRMGSP-----GSRTYLASPATAAASAIA-GRITDPREL 417
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
102-454 |
2.85e-30 |
|
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: 124.09 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 102 TINGDDHVFGLSAAQRYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTWDI 180
Cdd:cd01584 51 DINKEVYDFLASAGAKYGIGFWKPGSGIIHQIVLENYAFPGLLMIGTDSHTpNAGGLGGIAIGVGGADAVDVMAGIPWEL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 181 DYPGVVAVHLTGKPAPYVGPQDVALAIIGAV-FKNGyvKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEE 259
Cdd:cd01584 131 KCPKVIGVKLTGKLSGWTSPKDVILKVAGILtVKGG--TGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNER 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 260 VHNWLALHGRGQ--------DYCQLNPQPMAYYDGCISVDLSAIKPMIALPFHPSnvyeidtlnqnltdilreieieser 331
Cdd:cd01584 209 MKKYLKATGRAEiadladefKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPD------------------------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 332 VAHGKAKLSLLDKVENGRLKVQQGIIAGCSGGNYENV-----IAAANALRGQSCGNDtfsLAVYPSSQPVFMDLAKKGVV 406
Cdd:cd01584 264 LATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMgraasIAKQALAHGLKCKSI---FTITPGSEQIRATIERDGLL 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1344182769 407 ADLIGAGAIIRTAFCGPCFGAGD-TPINNGL--SIRHT-TRNFPNREGSKPA 454
Cdd:cd01584 341 QTFRDAGGIVLANACGPCIGQWDrKDIKKGEknTIVTSyNRNFTGRNDANPA 392
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
113-470 |
7.26e-20 |
|
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: 91.91 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 113 SAAQRYGGIFVPPHIAVIHQYM-REMMAGGGKMILGSDSHTR-YGALGTMavgegGGELVKQLLNDTWDI-----DYPGV 185
Cdd:cd01582 53 SFAKKHGIDFYPAGRGIGHQIMiEEGYAFPGTLAVASDSHSNmYGGVGCL-----GTPIVRTDAAAIWATgqtwwQIPPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 186 VAVHLTGKPAPYVGPQDVALAIIGAvFKNGYVKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDeevhnwlA 265
Cdd:cd01582 128 AKVELKGQLPKGVTGKDVIVALCGL-FNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD-------A 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 266 LHgrgqdycqlnpqpmayydgcISVDLSAIKPMIALPfhpsnvyeidtlnqnltdilreieiESERVAhgkaklSLLDKV 345
Cdd:cd01582 200 KH--------------------LILDLSTLSPYVSGP-------------------------NSVKVS------TPLKEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 346 ENGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLA------VYPSSQPVFMDLAKKGVVADLIGAGAIIRTA 419
Cdd:cd01582 229 EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIPVApgvefyVAAASSEVQAAAEKNGDWQTLLEAGATPLPA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1344182769 420 FCGPCFGAGDTPINNG-LSIRHTTRNFPNREGSKPANGQMSAVALMDARSIA 470
Cdd:cd01582 309 GCGPCIGLGQGLLEPGeVGISATNRNFKGRMGSTEALAYLASPAVVAASAIS 360
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
113-305 |
6.99e-15 |
|
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: 78.61 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 113 SAAQRYGGI-FVPPHIAVIHQ----YM----------REMMAGGGKMIlGSDSHT-RYGALGTMAVGEGGGELVKQLLND 176
Cdd:COG1048 160 WGQQAFDNFrVVPPGTGIVHQvnleYLafvvwtreedGETVAYPDTLV-GTDSHTtMINGLGVLGWGVGGIEAEAAMLGQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 177 TWDIDYPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGyVKNKVMEFVGPGVSALS-TDfRNSVDVMTTE--TTClsSV 253
Cdd:COG1048 239 PVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKG-VVGKFVEFFGPGLASLSlAD-RATIANMAPEygATC--GF 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1344182769 254 WQTDEEVHNWLALHGRGQD-------YCQLN------PQPMAYYDGCISVDLSAIKPMIALPFHP 305
Cdd:COG1048 315 FPVDEETLDYLRLTGRSEEqielveaYAKAQglwrdpDAPEPYYSDVLELDLSTVEPSLAGPKRP 379
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
123-448 |
5.10e-14 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 76.12 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 123 VPPHIAVIHQYMREMMA--------GGGK-----MILGSDSHTRY-GALGTMAVGEGG--------GELVKQLLndtwdi 180
Cdd:PRK12881 173 VPPGTGIMHQVNLEYLArvvhtkedDGDTvaypdTLVGTDSHTTMiNGIGVLGWGVGGieaeavmlGQPVYMLI------ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 181 dyPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGyVKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEV 260
Cdd:PRK12881 247 --PDVVGVELTGKLREGVTATDLVLTVTEMLRKEG-VVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQT 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 261 HNWLALHGRGQDYCQL------------NPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDTLNQNLTDILREIEIE 328
Cdd:PRK12881 324 LDYLRLTGRTEAQIALveayakaqglwgDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 329 SERVAHGKAKLSlldkvenGRLKVQQGIIAG---CSG-GNYENVIAA------ANALRGQSCGNDTFSLAvyPSSQPVFM 398
Cdd:PRK12881 404 NGFAKKAQTSNG-------VDLPDGAVAIAAitsCTNtSNPSVLIAAgllakkAVERGLTVKPWVKTSLA--PGSKVVTE 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1344182769 399 DLAKKGVVADLIGAGAIIrTAF-CGPCFG-AG--DTPINNGLSIRHTT--------RNFPNR 448
Cdd:PRK12881 475 YLERAGLLPYLEKLGFGI-VGYgCTTCIGnSGplTPEIEQAITKNDLVaaavlsgnRNFEGR 535
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
551-698 |
2.25e-13 |
|
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: 67.08 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 551 TTDELIPSG-ETSSYRSNPIGLAEFTLSRRDPGYVGRSKATAelenqrlAGNVseltevfarikqIAGQEHidplqteig 629
Cdd:cd01579 7 TTDHIMPAGaKVLPLRSNIPAISEFVFHRVDPTFAERAKAAG-------PGFI------------VGGENY--------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1344182769 630 smvyavkpGDGSAREQAASCQRVIGGLANIAEEYAtKRYRSNVINWGMLPLQMAE---VPTFEVGDYIYIPG 698
Cdd:cd01579 59 --------GQGSSREHAALAPMYLGVRAVLAKSFA-RIHRANLINFGILPLTFADeddYDRFEQGDQLELPL 121
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
142-473 |
2.43e-12 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 69.93 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 142 GKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHLTGKPAPYVGPQDVALAII---GAVFKNGYv 217
Cdd:PRK12466 123 GMVIVCGDSHTtTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIariGADGATGY- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 218 knkVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLAlhGRGQ------------DYCQLNPQPMAYYD 285
Cdd:PRK12466 202 ---AIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLR--GRPRapkgalwdaalaYWRTLRSDADAVFD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 286 GCISVDLSAIKPMIALPFHPSNVYEIDtlnQNLTDilREIEIESERVAHGKAKLSLLDkVENGR----LKVQQGIIAGCS 361
Cdd:PRK12466 277 REVEIDAADIAPQVTWGTSPDQAVPIT---GRVPD--PAAEADPARRAAMERALDYMG-LTPGTplagIPIDRVFIGSCT 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 362 GGNYENVIAAANALRGQSCGNDTFSLAVyPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNGLSIRHT 441
Cdd:PRK12466 351 NGRIEDLRAAAAVLRGRKVAPGVRAMVV-PGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCAST 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1344182769 442 T-RNFPNREGS-------KPANGQMSAVA--LMDARSIAATA 473
Cdd:PRK12466 430 TnRNFEGRQGPgarthlmSPAMVAAAAVAghITDVRSLLQAG 471
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
123-305 |
3.01e-11 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 67.07 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 123 VPPHIAVIHQ----YMRE--MMAGGGKMIL------GSDSHTRY-GALGTMAVGEGG--------GELVKQLLndtwdid 181
Cdd:PRK09277 174 VPPGTGICHQvnleYLAPvvWTREDGELVAypdtlvGTDSHTTMiNGLGVLGWGVGGieaeaamlGQPSSMLI------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 182 yPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNSVDVMTTE--TTClsSVWQTDEE 259
Cdd:PRK09277 247 -PEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVV-GKFVEFFGEGLASLSLADRATIANMAPEygATC--GFFPIDEE 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1344182769 260 VHNWLALHGRGQDYCQL------------NPQPMAYYDGCISVDLSAIKPMIALPFHP 305
Cdd:PRK09277 323 TLDYLRLTGRDEEQVALveayakaqglwrDPLEEPVYTDVLELDLSTVEPSLAGPKRP 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
123-323 |
6.70e-11 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 65.80 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 123 VPPHIAVIHQ----YM-REMMAGGGKM----ILGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHLTG 192
Cdd:PTZ00092 180 VPPGSGIVHQvnleYLaRVVFNKDGLLypdsVVGTDSHTTMiNGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 193 KPAPYVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHGRGQD 272
Cdd:PTZ00092 260 KLSEHVTATDLVLTVTSMLRKRGVV-GKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1344182769 273 YCQL------------NPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDTLNQNLTDILR 323
Cdd:PTZ00092 339 KVELiekylkanglfrTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLS 401
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
123-305 |
3.36e-10 |
|
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: 62.71 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 123 VPPHIAVIHQYMREMMA--------GGGKM-----ILGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAV 188
Cdd:cd01586 89 VPPGTGIIHQVNLEYLArvvftseeDGDGVaypdsVVGTDSHTTMiNGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 189 HLTGKPAPYVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVhnwlalhg 268
Cdd:cd01586 169 KLTGKLRPGVTATDLVLTVTQMLRKVGVV-GKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV-------- 239
|
170 180 190
....*....|....*....|....*....|....*..
gi 1344182769 269 rgqdycqlnpqpmayydgcISVDLSAIKPMIALPFHP 305
Cdd:cd01586 240 -------------------VELDLSTVEPSVSGPKRP 257
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
123-305 |
6.54e-10 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 62.90 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 123 VPPHIAVIHQYMREMMA-----GGGKM----ILGSDSHTRY-GALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHLTG 192
Cdd:PLN00070 212 VPPGSGIVHQVNLEYLGrvvfnTDGILypdsVVGTDSHTTMiDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 193 KPAPYVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHGRGQD 272
Cdd:PLN00070 292 KLRDGVTATDLVLTVTQMLRKHGVV-GKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDE 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1344182769 273 -------YCQLN--------PQPMAYYDGCISVDLSAIKPMIALPFHP 305
Cdd:PLN00070 371 tvamieaYLRANkmfvdynePQQERVYSSYLELDLEDVEPCISGPKRP 418
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
638-684 |
6.34e-05 |
|
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: 43.51 E-value: 6.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1344182769 638 GDGSAREQAASCQRVIGGLANIAEEYAtKRYRSNVINWGMLPLQMAE 684
Cdd:pfam00694 85 GCGSSREHAAWALRDLGIKAVIAESFA-RIHRNNLIKNGLLPLEFPE 130
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
635-751 |
3.65e-04 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 41.74 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 635 VKPGD----------GSAREQAASCQRVIGGLANIAEEYATKRYRsNVINWGmLPLqmAEVPT----FEVGDYIYI---P 697
Cdd:PRK00439 46 VKPGDiivagknfgcGSSREHAPIALKAAGVSAVIAKSFARIFYR-NAINIG-LPV--LECDEavdkIEDGDEVEVdleT 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1344182769 698 GIKAALDNpGTTFKGyvihedAPVTEitlYMesltaeeREIIKAGSLINFNKNR 751
Cdd:PRK00439 122 GVITNLTT-GEEYKF------KPIPE---FM-------LEILKAGGLIEYLKKK 158
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
619-698 |
6.88e-04 |
|
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: 39.37 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344182769 619 EHIDPlqTEIGSMVYAVKPGDGSAREQAASCQRVIGGLANIAEEYAtKRYRSNVINWGMLPLQ---MAEVPTFEVGDYIY 695
Cdd:cd00404 9 DHISP--AGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFA-RIFFRNLVDQGLLPLEfadPEDYLKLHTGDELD 85
|
...
gi 1344182769 696 IPG 698
Cdd:cd00404 86 IYP 88
|
|
| |
