|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
49-780 |
0e+00 |
|
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle]
Pssm-ID: 273561 [Multi-domain] Cd Length: 745 Bit Score: 1249.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 49 YKQNIEYVNIVRERLG-RPLTYAEKILYGHLDDPHG----QEIE--RGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQ 121
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 122 VAKPLTVHCDHLIQAQIGGEKDLKRAIDINKEVYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPN 201
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 202 AGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSA 281
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 282 TGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRDKIAQFAQ--LYHKDLLSADEGAEYDEIIEIDLNTLEPYVNGPFT 359
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKtgQYSFFKLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 360 PDLATPISKMKDVAVKNNWPLEVKVGLIGSCTNSSYEDMSRAASVVKDAATHGLKSKSIFTVTPGSEQIRATIARDGQLE 439
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 440 TFKEFGGTVLANACGPCIGQWDRQD-IKKGDKNTIVSSFNRNFTARNDGNPDTHSFVASPEITTAFAIAGDLRFNPLTDT 518
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 519 LKDKDGNEFMLKPPTGVGLPVKGYDPGENTYQAPPKD-RSSVTVQVSPTSDRLQLLKPFKAWDGKDAFDMPILIKSLGKT 597
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSpNPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 598 TTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKHHyTGEYAGVPDTARAYRDAGIRWVVIGGENFGEGSSRE 677
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDL-DGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 678 HAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYDKINPDDTIDILGLTTLAP---GKNLIMRVHPKEGEA 754
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 50306025 755 WETPLSHTFNAEQIEWFKAGSALNRL 780
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
65-786 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 934.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 65 RPLTYAEKILYGHLDDPhgqEIERGVSyLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPLTV-HCDHliqaqiggekD 143
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 144 LKRAIDINKEVYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSD 223
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 224 LAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 303
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 304 NKSMIDYLDATGRDKIAQfaqlyhkdLLSADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVAvknnwpleVK 383
Cdd:PRK07229 227 DERTREFLKAQGREDDWV--------ELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIK--------VD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 384 VGLIGSCTNSSYEDMSRAASVVKDaatHGLKSKSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGqwdrQ 463
Cdd:PRK07229 291 QVLIGSCTNSSYEDLMRAASILKG---KKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIG----M 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 464 DIKKGDKNTIVSSFNRNFTARNdGNPDTHSFVASPEITTAFAIAGDLRfNPLTDTLkdKDGNEFMLKPPtgvglpvKGYD 543
Cdd:PRK07229 364 GQAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRTLAL--ENGEYPKLEEP-------EGFA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 544 PGENTYQAPPKDRSSVTVQVSPTSDRLQLLKPFkawdgKDAFDMPILIKSLGKTTTDHISMAGP-WLKYRGHLENISNNY 622
Cdd:PRK07229 433 VDDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPL-----PDLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 623 MIGAINAENKKAncvkhhytgeyagvpdtarayRDAGiRWVVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHET 702
Cdd:PRK07229 508 FEGVDNTFPERA---------------------KEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKA 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 703 NLKKQGMLPLNFAEPAAYDKINPDDTIDILGLTTLAPGKNLIMRVHPKEgeaWETPLSHTFNAEQIEWFKAGSALNRLAN 782
Cdd:PRK07229 566 NLINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
....
gi 50306025 783 AKKA 786
Cdd:PRK07229 643 KLAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
99-510 |
0e+00 |
|
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: 837.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 99 RVACQDATAQMAILQFMSAGLPQVAKPLTVHCDHLIQAQIGGEKDLKRAIDINKEVYDFLATATAKYNMGFWKPGSGIIH 178
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 179 QIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGI 258
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 259 TTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRDKIAQFAQLYHKDLLSADEGAE 338
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKDDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 339 YDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVAVKNNWPLEVKVGLIGSCTNSSYEDMSRAASVVKDAATHGLKSKSI 418
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 419 FTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDRQDIKKGDKNTIVSSFNRNFTARNDGNPDTHSFVASP 498
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 50306025 499 EITTAFAIAGDL 510
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
67-779 |
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: 783.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 67 LTYAEKILYGHL---------DDPHGQEI------ERGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAK------- 124
Cdd:COG1048 36 LPYSLKILLENLlrnedgetvTEEDIKALanwlpkARGDDEIPFRPARVLMQDFTGVPAVVDLAAMRDAVARLggdpkki 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 125 ----PLTVHCDHLIQAQIGG-----EKDLKRAIDINKEVYDFLATATAKY-NMGFWKPGSGIIHQIVLENYAFP------ 188
Cdd:COG1048 116 nplvPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVVPPGTGIVHQVNLEYLAFVvwtree 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 189 -GALI------IGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTV 261
Cdd:COG1048 196 dGETVaypdtlVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 262 KGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRDK--IAQFAQLYHKDLLSADEGA-- 337
Cdd:COG1048 276 KGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEeqIELVEAYAKAQGLWRDPDApe 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 338 -EYDEIIEIDLNTLEPYVNGPFTPDLATPISKMK--------------------------DVAVKNNWpleVKVGLIGSC 390
Cdd:COG1048 356 pYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKeafraalaapvgeeldkpvrvevdgeEFELGHGA---VVIAAITSC 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 391 TNSSYEDMSRAASVV-KDAATHGLKSK--SIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDR----- 462
Cdd:COG1048 433 TNTSNPSVMIAAGLLaKKAVEKGLKVKpwVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppei 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 463 -QDIKKGD-KNTIVSSFNRNFTARNdGNPDTHSFVASPEITTAFAIAGDLRFNPLTDTL-KDKDGNEFMLKP--PTGVGL 537
Cdd:COG1048 513 sEAIEENDlVVAAVLSGNRNFEGRI-HPDVKANFLASPPLVVAYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEI 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 538 P------------VKGYD--------------PGENTYqapPKDRSSVTVQVSPTSDRLQLL-KPFkawdgKDAFDMPIL 590
Cdd:COG1048 592 PaavfkavtpemfRARYAdvfdgderwqalevPAGELY---DWDPDSTYIRRPPFFEGLQLEpEPF-----KDIKGARVL 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 591 IKSLGKTTTDHISMAGP-----------------------WLKYRGHLENISNNYMIGA--IN--AENKKANCVKHHYTG 643
Cdd:COG1048 664 AKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFANIriKNllAPGTEGGYTKHQPTG 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 644 EYAGVPDTARAYRDAGIRWVVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYDK- 722
Cdd:COG1048 744 EVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESl 823
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 723 -INPDDTIDILGLT-TLAPGKNLIMRVHPKEGEAWETPLSHTF-NAEQIEWFKAGSALNR 779
Cdd:COG1048 824 gLTGDETFDIEGLDeGLAPGKTVTVTATRADGSTEEFPVLHRIdTPVEVEYYRAGGILQY 883
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
71-508 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 583.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 71 EKILYGHLDDphgqEIERGVSYLklrPDRVACQDATAQMAILQFMSAGLP------QVAK-----PLTVHCDHliqAQIG 139
Cdd:pfam00330 1 EKIWDAHLVE----ELDGSLLYI---PDRVLMHDVTSPQAFVDLRAAGRAvrrpggTPATidhlvPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 140 GEKDLKRAIDINKEVYDFLATATAKYNMGFWKPGSGIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAV 218
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 219 DVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATT 298
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 299 SVFPFNKSMIDYLDATGRD---KIAQFAQLYHKDLLSADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVAV- 374
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRPeapKGEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPFa 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 375 -----------------KNNWPL---EVKVGLIGSCTNSSYEDMSRAASVVKDAATHGLKSKSI--FTVTPGSEQIRATI 432
Cdd:pfam00330 311 davkrkaaeraleymglGPGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPGvkASVVPGSEVVRAYA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50306025 433 ARDGQLETFKEFGGTVLANACGPCIGQWDRQDikkgDKNTIVSSFNRNFTARNdgNPDTHSFVASPEITTAFAIAG 508
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPALVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
99-510 |
1.54e-139 |
|
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: 417.28 E-value: 1.54e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 99 RVACQDATAQMAILQF-MSAGLPQVAKPLTVHCDHLIQAQIggekdlkrAIDINKEVYDFLATATAKYNMGFWKPGSGII 177
Cdd:cd01351 1 RVMLQDATGPMAMKAFeILAALGKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 178 HQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAG 257
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 258 ITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRDKIAQFAQLYhKDLLSADEGA 337
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAF-PEELLADEGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 338 EYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDvavknnwpLEVKVGLIGSCTNSSYEDMSRAASVVKDaatHGLKSKS 417
Cdd:cd01351 232 EYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKG---AKVAPGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 418 IFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDRqdiKKGDKNTIVSSFNRNFTARNDGNPDtHSFVAS 497
Cdd:cd01351 301 RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLAS 376
|
410
....*....|...
gi 50306025 498 PEITTAFAIAGDL 510
Cdd:cd01351 377 PELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
68-782 |
7.08e-139 |
|
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized. [Energy metabolism, TCA cycle]
Pssm-ID: 130409 [Multi-domain] Cd Length: 658 Bit Score: 425.17 E-value: 7.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 68 TYAEKILYGHL---DDPHGQEIergvsylKLRPDRVACQDATAQMAILQFMSAGLPQVAKPLTV-HCDHLIQaqiggEKD 143
Cdd:TIGR01342 1 TLAEKIIDDHLvegDLEPGEEI-------AIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAqYCDHNML-----QFD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 144 LKRAIDinkevYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSD 223
Cdd:TIGR01342 69 FKNADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 224 LAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 303
Cdd:TIGR01342 144 EAFYLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 304 NKSMIDYLDATGRDKiaQFAQLyhkdllSADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVavknnwplEVK 383
Cdd:TIGR01342 224 DDITEAWLAAFDRED--DFVDL------LADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIAGI--------EVD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 384 VGLIGSCTNSSYEDMSRAASVVKDAATHglkSKSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGqwdrQ 463
Cdd:TIGR01342 288 QVMIGSCTNGAFEDLLPAAKLLEGREVH---KDTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIG----I 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 464 DIKKGDKNTIVSSFNRNFTARNdGNPDTHSFVASPEITTAFAIAGDLrFNPltDTLKDKDGNefmLKPPtGVGLPVK--- 540
Cdd:TIGR01342 361 GFAPASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDP--RDLADDEGD---LEAI-GFEMGEKfpg 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 541 GYDPGEnTYQAPPKDRSSVTVQVSPTSDRLQLLKPFKAwdgkdAFDMPILIKSLGKTTTDHISMAGP-WLKYRGHLENIS 619
Cdd:TIGR01342 433 GYDAAD-IDIIPKEEREDDDIIKGPNIKPLPEFDPLGA-----DIEGETALIMEDNITTDHIIPAGAdILKFRSNIEAIS 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 620 nnymigainaenkkaNCVKHHYTGEYAgvpDTARAYRDAGIRWVVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARI 699
Cdd:TIGR01342 507 ---------------EFTLHRIDDEFA---ERAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARI 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 700 HETNLKKQGMLPLNFAEPAAYDKINPDDTIDILG--LTTLAPGKN-LIMRVHpkegEAWETPLSHTFNAEQIEWFKAGSA 776
Cdd:TIGR01342 569 HHANLFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDeFTINKN----DDEEALATLDASEREKEILAAGGK 644
|
....*.
gi 50306025 777 LNRLAN 782
Cdd:TIGR01342 645 LNLIKN 650
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
98-510 |
1.00e-118 |
|
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: 362.92 E-value: 1.00e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 98 DRVACQDATAQMAILQFMSAGLPQVAKPLTV-HCDH-LIQAqiggekDLKRAIDinkevYDFLATATAKYNMGFWKPGSG 175
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVsYVDHnTLQT------DFENADD-----HRFLQTVAARYGIYFSRPGNG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 176 IIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKL 255
Cdd:cd01585 70 ICHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 256 AGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRDKIAQfaqlyhkdLLSADE 335
Cdd:cd01585 150 LRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWV--------ELAADA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 336 GAEYDEIIEIDLNTLEPYVNGPFTPDLATPIskmKDVAvknnwPLEVKVGLIGSCTNSSYEDMSRAASVVKDAATHglkS 415
Cdd:cd01585 222 DAEYDEEIEIDLSELEPLIARPHSPDNVVPV---REVA-----GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVH---P 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 416 KSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDrqdiKKGDKNTIVSSFNRNFTARNdGNPDTHSFV 495
Cdd:cd01585 291 HVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYL 365
|
410
....*....|....*
gi 50306025 496 ASPEITTAFAIAGDL 510
Cdd:cd01585 366 ASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
592-740 |
3.81e-98 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 300.54 E-value: 3.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 592 KSLGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKHHYTGEYAGVPDTARAYRDAGIRWVVIGGENFG 671
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50306025 672 EGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYDKINPDDTIDILGLTTLAPG 740
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
96-781 |
5.71e-90 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 302.24 E-value: 5.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 96 RPDRVACQDATAQMAI--LQFMSAGL------PQVAKPLT---VHCDHLIQAQIGGEKD---LKRAIDI--NKEVYDFLA 159
Cdd:PRK12881 82 VPARVVMQDFTGVPALvdLAAMRDAAaeaggdPAKINPLVpvdLVVDHSVAVDYFGQKDaldLNMKIEFqrNAERYQFLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 160 TAT-AKYNMGFWKPGSGIIHQIVLE--------------NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMSDL 224
Cdd:PRK12881 162 WGMqAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTLV-GTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 225 AWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFN 304
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 305 KSMIDYLDATGRDK--IAQFAQlYHKDL-LSADEGAE--YDEIIEIDLNTLEPYVNGPFTP-------DLATPISKMKDV 372
Cdd:PRK12881 321 EQTLDYLRLTGRTEaqIALVEA-YAKAQgLWGDPKAEprYTRTLELDLSTVAPSLAGPKRPqdrialgNVKSAFSDLFSK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 373 AVKNNWPLE--------------VKVGLIGSCTNSSYEDMSRAASVV-KDAATHGLKSKS-IFT-VTPGSEQIRATIARD 435
Cdd:PRK12881 400 PVAENGFAKkaqtsngvdlpdgaVAIAAITSCTNTSNPSVLIAAGLLaKKAVERGLTVKPwVKTsLAPGSKVVTEYLERA 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 436 GQLETFKEFGGTVLANACGPCIGQWD------RQDIKKGD-KNTIVSSFNRNFTARNdgNPD-THSFVASPEITTAFAIA 507
Cdd:PRK12881 480 GLLPYLEKLGFGIVGYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRI--HPNiKANFLASPPLVVAYALA 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 508 GDLRFNPLTDTL-KDKDGNEFMLKP--PTG------VGLPVKGYDPGENTYQAPPKDR-----SSVTVQVSPTSDRLQLL 573
Cdd:PRK12881 558 GTVRRDLMTEPLgKGKDGRPVYLKDiwPSSaeidalVAFAVDPEDFRKNYAEVFKGSElwaaiEAPDGPLYDWDPKSTYI 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 574 K--PFkaWDGKDAFDMPIL-IKS------LGKT-TTDHIS---------MAGPWLKYRGHLENISNNY----------MI 624
Cdd:PRK12881 638 RrpPF--FDFSMGPAASIAtVKGarplavLGDSiTTDHISpagaikadsPAGKYLKENGVPKADFNSYgsrrgnhevmMR 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 625 GA------IN--AENKKANCVKHHYTGEYAGVPDTARAYRDAGIRWVVIGGENFGEGSSREHAALEPRFLGGFAIITKSF 696
Cdd:PRK12881 716 GTfanvriKNlmIPGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESF 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 697 ARIHETNLKKQGMLPLNF--AEPAAYDKINPDDTIDILGLTT-LAPGKNLIMRVHPKEGE--------AWETPlshtfna 765
Cdd:PRK12881 796 ERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLPGeIKPRQDVTLVIHRADGStervpvlcRIDTP------- 868
|
810
....*....|....*.
gi 50306025 766 EQIEWFKAGSALNRLA 781
Cdd:PRK12881 869 IEVDYYKAGGILPYVL 884
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
66-508 |
4.05e-88 |
|
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: 284.23 E-value: 4.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 66 PLTYAEKILYGHLddphGQEIERGvSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKP----LTVhcDHLIQAqigge 141
Cdd:COG0065 2 GMTLAEKILARHA----GREVEPG-EIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPdrivAVF--DHNVPT----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 142 KDLKRAIDInKEVYDFlataTAKYNMGFWKPGS-GIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVD 219
Cdd:COG0065 70 KDPKSAEQV-KTLREF----AKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 220 VM-SDLAWeLKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATT 298
Cdd:COG0065 145 VLaTGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 299 SVFPFNKSMIDYLDATGRdkiAQFAQLYhkdllsADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVavknnw 378
Cdd:COG0065 224 GIIAPDETTFEYLKGRPF---APWRTLK------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGI------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 379 plEVKVGLIGSCTNSSYEDMSRAASVVKdaathGLK-SKSI-FTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPC 456
Cdd:COG0065 289 --KIDQVFIGSCTNGRIEDLRAAAEILK-----GRKvAPGVrAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMC 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50306025 457 IGQwdRQDI-KKGDknTIVSSFNRNFTARNdGNPDTHSFVASPEITTAFAIAG 508
Cdd:COG0065 362 LGM--NMGVlAPGE--RCASTSNRNFEGRM-GSPGSRTYLASPATAAASAIAG 409
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
96-779 |
1.65e-87 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 295.49 E-value: 1.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 96 RPDRVACQDATAQMAI--LqfmsAGL---------------PQVAKPLTVhcDHLIQAQIGGEKD-LKRAIDI----NKE 153
Cdd:PRK09277 83 RPARVVMQDFTGVPAVvdL----AAMrdaiadlggdpakinPLVPVDLVI--DHSVQVDYFGTPDaFEKNVELeferNEE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 154 VYDFLA-TATAKYNMGFWKPGSGIIHQIVLE-------------NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVD 219
Cdd:PRK09277 157 RYQFLKwGQKAFDNFRVVPPGTGICHQVNLEylapvvwtredgeLVAYPDTLV-GTDSHTTMINGLGVLGWGVGGIEAEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 220 VMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKlagITTV---KGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGA 296
Cdd:PRK09277 236 AMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLT---VTEMlrkKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 297 TTSVFPFNKSMIDYLDATGRDK--IAQF-----AQ-LYHkdllSADEGAEYDEIIEIDLNTLEPYVNGP-------FTPD 361
Cdd:PRK09277 313 TCGFFPIDEETLDYLRLTGRDEeqVALVeayakAQgLWR----DPLEEPVYTDVLELDLSTVEPSLAGPkrpqdriPLSD 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 362 LATPISKMKDVAVKNNWPLEVKVGL-------------IGSCTNSSY-EDMSRAASVVKDAATHGLKSKSifTV----TP 423
Cdd:PRK09277 389 VKEAFAKSAELGVQGFGLDEAEEGEdyelpdgavviaaITSCTNTSNpSVMIAAGLLAKKAVEKGLKVKP--WVktslAP 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 424 GSEQIRATIARDGQLETFKEFGGTVLANACGPCIG---------QwdrQDIKKGD-KNTIVSSFNRNFTARNdgNPDTH- 492
Cdd:PRK09277 467 GSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGnsgplppeiE---KAINDNDlVVTAVLSGNRNFEGRI--HPLVKa 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 493 SFVASPEITTAFAIAGDLRFNPLTDTL-KDKDGNEFMLK--------------------------------PPTGVGLPV 539
Cdd:PRK09277 542 NYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKdiwpsdeeidavvakavkpemfrkeyadvfegDERWNAIEV 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 540 kgydPGENTYQAPPKdrsSVTVQvSPtsdrlqllkPFkaWDG--------KDAFDMPILIKsLG-KTTTDHISMAGP--- 607
Cdd:PRK09277 622 ----PEGPLYDWDPD---STYIR-NP---------PY--FEGmlaepgpvRDIKGARVLAL-LGdSITTDHISPAGAika 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 608 ------WLKYRGHLENISNNY---------MIGA----INAENKKANCV-----KHHYTGEYAGVPDTARAYRDAGIRWV 663
Cdd:PRK09277 682 dspagkYLLEHGVEPKDFNSYgsrrgnhevMMRGtfanIRIRNEMVPGVeggytRHFPEGEVMSIYDAAMKYKEEGTPLV 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 664 VIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYD--KINPDDTIDILGLTTLAPGK 741
Cdd:PRK09277 762 VIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGA 841
|
810 820 830
....*....|....*....|....*....|....*....
gi 50306025 742 NLIMRVHPKEGEAWETPLSHTFN-AEQIEWFKAGSALNR 779
Cdd:PRK09277 842 TVTVVITRADGEVVEFPVLCRIDtAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
66-508 |
1.08e-83 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 272.82 E-value: 1.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 66 PLTYAEKILYGHLDDPH--GQEIERGVsylklrpDRVACQDATAQMAILQFMSAGLPQVAKPLTVH--CDHLIQAqigge 141
Cdd:PRK00402 2 GMTLAEKILARHSGRDVspGDIVEAKV-------DLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 142 KDLKRAiDINKEVYDFLATATAKYnmgFWKPGSGIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGAD-AVD 219
Cdd:PRK00402 70 KDIKSA-EQQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCTYGALGAFATGMGSTDmAAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 220 VMSDLAWeLKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTS 299
Cdd:PRK00402 146 MATGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 300 VFPFNKSMIDYL-DATGRDkiaqFAQLYhkdllsADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVavknnw 378
Cdd:PRK00402 225 IFAPDEKTLEYLkERAGRD----YKPWK------SDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGT------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 379 plEVKVGLIGSCTNSSYEDMSRAASVVKDaatHGLKSKSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIG 458
Cdd:PRK00402 289 --KVDQVFIGSCTNGRLEDLRIAAEILKG---RKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLG 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 50306025 459 QwdRQDIkKGDKNTIVSSFNRNFTARNdGNPDTHSFVASPEITTAFAIAG 508
Cdd:PRK00402 364 G--HMGV-LAPGEVCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
99-508 |
1.82e-80 |
|
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: 262.90 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 99 RVACQDATAQMAILQFMSAGLPQVAKPLTVHC--DHLIQAqiggeKDLKRAIDINKEVYDFLATATAKYNMGfwkpGSGI 176
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT-----PDIKAAEQVKTLRKFAKEFGINFFDVG----RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 177 IHQIVLENYAF-PGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVM-SDLAWeLKAPKIMGVKLTGRMNGWTSPKDIILK 254
Cdd:cd01583 72 CHVILPEKGLTlPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLaTGKLW-FRVPETMRVNVEGKLPPGVTAKDVILY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 255 LAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRdkiAQFAQLYhkdllsAD 334
Cdd:cd01583 151 IIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK---AYWKELK------SD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 335 EGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDVavknnwplEVKVGLIGSCTNSSYEDMSRAASVVKDaatHGLK 414
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI--------KIDQVFIGSCTNGRLEDLRAAAEILKG---RKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 415 SKSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGqwdRQDIKKGDKNTIVSSFNRNFTARNdGNPDTHSF 494
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLG---GHMGVLAPGERCVSTSNRNFKGRM-GSPGARIY 366
|
410
....*....|....
gi 50306025 495 VASPEITTAFAIAG 508
Cdd:cd01583 367 LASPATAAASAITG 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
97-735 |
1.35e-72 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 254.94 E-value: 1.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 97 PDRVACQDATAQMAILQF--------MSAGLPQVAKPLT---VHCDHLIQAQIGG-----EKDLKRAIDINKEVYDFLA- 159
Cdd:PTZ00092 90 PARVLLQDFTGVPAVVDLaamrdamkRLGGDPAKINPLVpvdLVIDHSVQVDFSRspdalELNQEIEFERNLERFEFLKw 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 160 TATAKYNMGFWKPGSGIIHQIVLE----------NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELK 229
Cdd:PTZ00092 170 GSKAFKNLLIVPPGSGIVHQVNLEylarvvfnkdGLLYPDSVV-GTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 230 APKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMID 309
Cdd:PTZ00092 249 LPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 310 YLDATGRD--KIAQFAQLYHKDLLSADEGA--EYDEIIEIDLNTLEPYVNGP---------------FTPDLATPIS--- 367
Cdd:PTZ00092 329 YLKQTGRSeeKVELIEKYLKANGLFRTYAEqiEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGfkg 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 368 ------KMKDVAVKN----NWPLE---VKVGLIGSCTNSSYED-MSRAASVVKDAATHGLKSKSIF--TVTPGSEQIRAT 431
Cdd:PTZ00092 409 fgipeeKHEKKVKFTykgkEYTLThgsVVIAAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPYIktSLSPGSKVVTKY 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 432 IARDGQLETFKEFGGTVLANACGPCIGQWDRQD------IKkgDKNTIVSSF---NRNFTARNdgNPDTHS-FVASPEIT 501
Cdd:PTZ00092 489 LEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDpevseaIT--NNDLVAAAVlsgNRNFEGRV--HPLTRAnYLASPPLV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 502 TAFAIAGDLRFNPLTDTL-KDKDGNEFMLKP--PTG--VGLPVKGYDPGE----------------NTYQAP-----PKD 555
Cdd:PTZ00092 565 VAYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSReeIQALEAKYVKPEmfkevysnitqgnkqwNELQVPkgklyEWD 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 556 RSSVTVQVSPTSDRLQlLKPFKAWDGKDAFDMPILIKSLgktTTDHISMAG------PWLKY------------------ 611
Cdd:PTZ00092 645 EKSTYIHNPPFFQTME-LEPPPIKSIENAYCLLNLGDSI---TTDHISPAGniaknsPAAKYlmergverkdfntygarr 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 612 -------RGHLENIS-NNYMIGainaeNKKANCVkHHYTGEYAGVPDTARAYRDAGIRWVVIGGENFGEGSSREHAALEP 683
Cdd:PTZ00092 721 gndevmvRGTFANIRlINKLCG-----KVGPNTV-HVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGP 794
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 50306025 684 RFLGGFAIITKSFARIHETNLKKQGMLPLNFAepaaydkinPDDTIDILGLT 735
Cdd:PTZ00092 795 YLQGVKAVIAESFERIHRSNLVGMGILPLQFL---------NGENADSLGLT 837
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
68-508 |
6.79e-72 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 241.20 E-value: 6.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 68 TYAEKILYGHlddpHGQEIERGVSyLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPLTVHC--DHLIQAqiggeKDLK 145
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDL-IEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA-----DTIK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 146 RAiDINKEVYDFLATATAKYnmgFWKPGSGIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGAD-AVDVMSD 223
Cdd:TIGR01343 71 AA-EMQKLAREFVKKQGIKY---FYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDmAYAIATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 224 LAWeLKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 303
Cdd:TIGR01343 147 KTW-FKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 304 NKSMIDYLdatgrdkiaqfAQLYHKD--LLSADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMKDvavknnwpLE 381
Cdd:TIGR01343 226 DEKTIQYL-----------KERRKEPfrVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEG--------TE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 382 VKVGLIGSCTNSSYEDMSRAASVVKDaatHGLKSKSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQwd 461
Cdd:TIGR01343 287 IDQVFIGSCTNGRLEDLRVAAKILKG---RKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGS-- 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 50306025 462 RQDIkKGDKNTIVSSFNRNFTARNdGNPDTHSFVASPEITTAFAIAG 508
Cdd:TIGR01343 362 HQGV-LAPGEVCISTSNRNFKGRM-GHPNAEIYLASPATAAASAVKG 406
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
96-735 |
2.81e-60 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 220.06 E-value: 2.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 96 RPDRVACQDATAQMAILQFMS--------AGLPQVAKPLT---VHCDHLIQAQIGG-----EKDLKRAIDINKEVYDFLA 159
Cdd:PLN00070 121 KPARVLLQDFTGVPAVVDLACmrdamnnlGGDPNKINPLVpvdLVIDHSVQVDVARsenavQANMELEFQRNKERFAFLK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 160 -TATAKYNMGFWKPGSGIIHQIVLENYA----------FPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWEL 228
Cdd:PLN00070 201 wGSTAFQNMLVVPPGSGIVHQVNLEYLGrvvfntdgilYPDSVV-GTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 229 KAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMI 308
Cdd:PLN00070 280 VLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 309 DYLDATGR-DKIAQFAQLYHK------DLLSADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPISKMK----------- 370
Cdd:PLN00070 360 QYLKLTGRsDETVAMIEAYLRankmfvDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKadwhscldnkv 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 371 ------------DVAVKNNW---PLEVKVG-----LIGSCTNSSYED-MSRAASVVKDAATHGLKSKS-IFT-VTPGSEQ 427
Cdd:PLN00070 440 gfkgfavpkeaqSKVAKFSFhgqPAELRHGsvviaAITSCTNTSNPSvMLGAGLVAKKACELGLEVKPwIKTsLAPGSGV 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 428 IRATIARDGQLETFKEFGGTVLANACGPCI---GQWDRQDIKKGDKNTIVS----SFNRNFTARNdgNPDTHS-FVASPE 499
Cdd:PLN00070 520 VTKYLLKSGLQKYLNQQGFHIVGYGCTTCIgnsGELDESVASAITENDIVAaavlSGNRNFEGRV--HPLTRAnYLASPP 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 500 ITTAFAIAGDLRFNPLTDTL-KDKDGNEFMLK---PPTGVGLPVKGY----DPGENTYQAPPKDRSSVTVQVSPTSDRLq 571
Cdd:PLN00070 598 LVVAYALAGTVDIDFEKEPIgTGKDGKDVFFRdiwPSNEEVAEVVQSsvlpDMFKSTYEAITKGNPMWNQLSVPSGTLY- 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 572 llkpfkAWDGKDAF-DMPILIKSLGKT--------------------TTDHISMAG------PWLKY------------- 611
Cdd:PLN00070 677 ------SWDPKSTYiHEPPYFKNMTMSppgphgvkdaycllnfgdsiTTDHISPAGsihkdsPAAKYlmergvdrkdfns 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 612 ------------RGHLENIS--NNYMIGAINAENkkancvKHHYTGEYAGVPDTARAYRDAGIRWVVIGGENFGEGSSRE 677
Cdd:PLN00070 751 ygsrrgndeimaRGTFANIRivNKLLKGEVGPKT------VHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRD 824
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 50306025 678 HAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFaepaaydkiNPDDTIDILGLT 735
Cdd:PLN00070 825 WAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCF---------KSGEDADTLGLT 873
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
587-717 |
1.09e-59 |
|
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: 197.97 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 587 MPILIKSLGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKHHYTGEYAGVPDTARAYRDAGIRWVVIG 666
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 50306025 667 GENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEP 717
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
120-508 |
3.37e-52 |
|
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: 187.13 E-value: 3.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 120 PQVAKPLTVhcDHLIQAQIGG-----EKDLKRAIDINKEVYDFLATATAKY-NMGFWKPGSGIIHQIVLE---------- 183
Cdd:cd01586 35 PLIPVDLVI--DHSVQVDFYGtadalAKNMKLEFERNRERYEFLKWGQKAFkNLRVVPPGTGIIHQVNLEylarvvftse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 184 ----NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGIT 259
Cdd:cd01586 113 edgdGVAYPDSVV-GTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 260 TVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPfnksmIDyldatgrdkiaqfaqlyhkdllsadegaey 339
Cdd:cd01586 192 RKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFP-----VD------------------------------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 340 DEIIEIDLNTLEPYVNGPFTPDLATPISKmkdvavknnwplEVKVGLIGSCTNSSYED-MSRAASVVKDAATHGLKSKSI 418
Cdd:cd01586 237 TQVVELDLSTVEPSVSGPKRPQDRVPLHG------------SVVIAAITSCTNTSNPSvMLAAGLLAKKAVELGLKVKPY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 419 F--TVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIG------QWDRQDIKKGD-KNTIVSSFNRNFTARNdgNP 489
Cdd:cd01586 305 VktSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpEEVEEAIKENDlVVAAVLSGNRNFEGRI--HP 382
|
410 420
....*....|....*....|
gi 50306025 490 DTHS-FVASPEITTAFAIAG 508
Cdd:cd01586 383 LVRAnYLASPPLVVAYALAG 402
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
111-510 |
6.35e-40 |
|
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: 151.23 E-value: 6.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 111 ILQFMSAGLPQVAKPLTVHC--DHLIQAQigGEKDLKRaidinkevYDFLATATAKYNMGFWKPGSGIIHQIVLEN-YAF 187
Cdd:cd01582 12 ALKFMSIGATKIHNPDQIVMtlDHDVQNK--SEKNLKK--------YKNIESFAKKHGIDFYPAGRGIGHQIMIEEgYAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 188 PGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGK 267
Cdd:cd01582 82 PGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 268 IVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPfnksmidyLDAtgrdkiaqfaqlyhKDLLsadegaeydeiieIDL 347
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFP--------TDA--------------KHLI-------------LDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 348 NTLEPYVNGPFTPDLATPISKM--KDVAVKnnwplevKVGLIgSCTNSSYEDMSRAASVVKDAATHGLKSKSI----FTV 421
Cdd:cd01582 207 STLSPYVSGPNSVKVSTPLKELeaQNIKIN-------KAYLV-SCTNSRASDIAAAADVVKGKKEKNGKIPVApgveFYV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 422 TPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGqwdrqdIKKG---DKNTIVSSFNRNFTARNdGNPDTHSFVASP 498
Cdd:cd01582 279 AAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG------LGQGllePGEVGISATNRNFKGRM-GSTEALAYLASP 351
|
410
....*....|..
gi 50306025 499 EITTAFAIAGDL 510
Cdd:cd01582 352 AVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
172-510 |
3.84e-38 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 148.51 E-value: 3.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 172 PGSGIIHQIVLE-NYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKD 250
Cdd:PRK12466 105 PRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 251 IILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIDYLDATGRD-KIAQFAQ-LYHK 328
Cdd:PRK12466 185 LILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRApKGALWDAaLAYW 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 329 DLLSADEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPIS-------KMKDVAVKNNW-------------PLE---VKVG 385
Cdd:PRK12466 265 RTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpaAEADPARRAAMeraldymgltpgtPLAgipIDRV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 386 LIGSCTNSSYEDMSRAASVVKdaathGLKSKSIFT--VTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDrq 463
Cdd:PRK12466 345 FIGSCTNGRIEDLRAAAAVLR-----GRKVAPGVRamVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMND-- 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 50306025 464 DI-KKGDKntIVSSFNRNFTARNdgNPDTHSFVASPEITTAFAIAGDL 510
Cdd:PRK12466 418 DVlAPGER--CASTTNRNFEGRQ--GPGARTHLMSPAMVAAAAVAGHI 461
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
158-508 |
1.08e-37 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 147.19 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 158 LATATAKYNMGFWKPGS---GIIHQIVLENYA-FPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMSDLAWELKAPKI 233
Cdd:PRK05478 86 LEKNCKEFGITLFDLGDprqGIVHVVGPEQGLtLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 234 MGVKLTGRMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGA---------TTsvfpfn 304
Cdd:PRK05478 166 MKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 305 ksmIDYLDatGRD---KIAQF--AQLYHKDLLSaDEGAEYDEIIEIDLNTLEPYVNGPFTPDLATPIS-------KMKDV 372
Cdd:PRK05478 240 ---FEYLK--GRPfapKGEDWdkAVAYWKTLKS-DEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDgkvpdpeDFADP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 373 AVKNNW-------------PLE-VKVG--LIGSCTNSSYEDMSRAASVVKdaathGLK-SKSIFT-VTPGSEQIRATIAR 434
Cdd:PRK05478 314 VKRASAeralaymglkpgtPITdIKIDkvFIGSCTNSRIEDLRAAAAVVK-----GRKvAPGVRAlVVPGSGLVKAQAEA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 435 DGQLETFKEFG------GtvlanaCGPCIGQWDrqDIKKGDKNTiVSSFNRNFTARNDGNPDTHsfVASPEITTAFAIAG 508
Cdd:PRK05478 389 EGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERC-ASTSNRNFEGRQGKGGRTH--LVSPAMAAAAAITG 457
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
54-722 |
4.48e-28 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 120.88 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 54 EYVNIVRERLGRPLTYAEKILYGHLDDPHGQEiergvsyLKLRPDRVACQDATAqMAILQFMSA-GLPQVAKPLTVHCDH 132
Cdd:PRK11413 22 HFTGEIKKEEAKKGTIAWSILSSHNTSGNMDK-------LKIKFDSLASHDITF-VGIIQTAKAsGMERFPLPYVLTNCH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 133 LIQAQIGGEkdlkraidINKEVYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTpNAGGLGQLAIGV 212
Cdd:PRK11413 94 NSLCAVGGT--------INEDDHVFGLSAAQKYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 213 GGADAVDVMSDLAWELKAPKIMGVKLTGRMNGWTSPKDIILKLAGiTTVKGG--TGKIVEYFGDGVDTFSATGMGTICNM 290
Cdd:PRK11413 165 GGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIG-AVFKNGyvKNKVMEFVGPGVSALSTDFRNGVDVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 291 GAEIGATTSVFPFNKSMIDYLDATGRDKiaQFAQLYHKDLlsadegAEYDEIIEIDLNTLEPYVNGPFTPDLATPISK-- 368
Cdd:PRK11413 244 TTETTCLSSIWQTDEEVHNWLALHGRGQ--DYCELNPQPM------AYYDGCISVDLSAIKPMIALPFHPSNVYEIDEln 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 369 ------MKDVAVKN-----------------NWPLEVKVGLIGSCTNSSYEDMSRAASVvkdaathgLKSKSI------F 419
Cdd:PRK11413 316 qnltdiLREVEIEServahgkaklslldkieNGRLKVQQGIIAGCSGGNYENVIAAANA--------LRGQSCgndtfsL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 420 TVTPGSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDrqdiKKGDKNTIVSSFNRNFTARnDGNPDTHSFVASPE 499
Cdd:PRK11413 388 SVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGD----TPANNGLSIRHTTRNFPNR-EGSKPANGQMSAVA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 500 ITTAFAIAGDLrfnpltdtlkdkdGNEFMLKPPTGVGLP--VKGY----DPGEN-TYQAPPKDRSSVTVQVSPTsdrlql 572
Cdd:PRK11413 463 LMDARSIAATA-------------ANGGYLTSATELDCWdnVPEYafdvTPYKNrVYQGFGKGATQQPLIYGPN------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 573 lkpFKAWDGKDAFDMPILIKSLGK-----TTTDHISMAGPWLKYRGH-------------LENISNNYMIGAINAENKKA 634
Cdd:PRK11413 524 ---IKDWPEMGALTDNILLKVCSKildpvTTTDELIPSGETSSYRSNplglaeftlsrrdPGYVGRSKAVAELENQRLAG 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 635 NC--VKHHYT--GEYAGVPDTARAyrDAGIRWVVIGGENfGEGSSREHAALEPRFLGGFAIITKSFA-RIHETNLKKQGM 709
Cdd:PRK11413 601 NVseLTEVFAriKQIAGQEHIDPL--QTEIGSMVYAVKP-GDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGM 677
|
730
....*....|...
gi 50306025 710 LPLNFAEPAAYDK 722
Cdd:PRK11413 678 LPFQMAEEPTFEV 690
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
598-731 |
1.44e-27 |
|
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: 107.91 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 598 TTDHISMAGP-WLKYRGHLENISNNymigainaenkkancVKHHYTGEYagvPDTARAyRDAGIrwvVIGGENFGEGSSR 676
Cdd:cd01579 7 TTDHIMPAGAkVLPLRSNIPAISEF---------------VFHRVDPTF---AERAKA-AGPGF---IVGGENYGQGSSR 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 50306025 677 EHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYDKINPDDTIDI 731
Cdd:cd01579 65 EHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLEL 119
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
658-733 |
4.26e-26 |
|
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: 102.55 E-value: 4.26e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50306025 658 AGIRWVVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYDKINPDDTIDILG 733
Cdd:cd00404 13 PAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
596-733 |
1.03e-20 |
|
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: 90.03 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 596 KTTTDHISMAGP---------WLKYRGHLENISNNY---------MIGAINA---------ENKKANCVKHHYTGEYAGV 648
Cdd:cd01580 5 SVTTDHISPAGSiakdspagkYLAERGVKPRDFNSYgsrrgndevMMRGTFAnirlrnklvPGTEGGTTHHPPTGEVMSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 649 PDTARAYRDAGIRWVVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFA--EPAAYDKINPD 726
Cdd:cd01580 85 YDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPpgENADSLGLTGE 164
|
....*..
gi 50306025 727 DTIDILG 733
Cdd:cd01580 165 ETYDIIG 171
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
145-510 |
6.49e-17 |
|
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: 84.09 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 145 KRAIDINKEVYDFLATatakYNMGFWKPGSGIIHQiVLENYAFPGALIIGTDSHT--------PNAGGLGQLAIGVGgad 216
Cdd:cd01581 68 PVDVKTHRTLPDFISN----RGGVALRPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGLVAFAAATG--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 217 avdVMSdlaweLKAPKIMGVKLTGRMNGWTSPKDII-------LKLAGITTVKGG-----TGKIVEYfgDGVDTFSATGM 284
Cdd:cd01581 140 ---VMP-----LDMPESVLVRFKGKMQPGITLRDLVnaipyyaIQQGLLTVEKKGkknvfNGRILEI--EGLPDLKVEQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 285 GTICNMGAEIGATTSVFPFNK-SMIDYL----------------DA--TGRDKIAQFAQLYHKDLLSADEGAEYDEIIEI 345
Cdd:cd01581 210 FELTDASAERSAAACTVRLDKePVIEYLesnvvlmkimiangydDArtLLRRIIAMEEWLANPPLLEPDADAEYAAVIEI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 346 DLNTL-EPYVNGPFTPDLATPISKMKDVAVKNnwplevkvGLIGSC-TNSSyeDMSRAASVVKDAAThglkSKSIFTVTP 423
Cdd:cd01581 290 DLDDIkEPILACPNDPDDVKLLSEVAGKKIDE--------VFIGSCmTNIG--HFRAAAKILRGKEF----KPTRLWVAP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 424 GSEQIRATIARDGQLETFKEFGGTVLANACGPCIGQWDRqdIKKGDknTIVSSFNRNFTARNdgNPDTHSFVASPEITTA 503
Cdd:cd01581 356 PTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRV--GKGAEVYLGSAELAAV 429
|
....*..
gi 50306025 504 FAIAGDL 510
Cdd:cd01581 430 CALLGRI 436
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
171-510 |
1.50e-15 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 80.99 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 171 KPGSGIIHQiVLENYAFPGALIIGTDSHT--------PNAGGLgqlaigVGGADAVDVMSdlaweLKAPKIMGVKLTGRM 242
Cdd:PRK09238 462 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGEM 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 243 NGWTSPKDII-------LKlAGITTV--KGG----TGKIVEYfgDGVDTFSATGMGTICNMGAEIGATTSVFPFN----- 304
Cdd:PRK09238 530 QPGITLRDLVhaipyyaIK-QGLLTVekKGKknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKLSkepii 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 305 ----------KSMID--YLDA-TGRDKIAQF-AQLYHKDLLSADEGAEYDEIIEIDLNTL-EPYVNGPFTPDLATPISkm 369
Cdd:PRK09238 607 eylrsnivllKWMIAegYGDArTLERRIAAMeEWLANPELLEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLS-- 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 370 kDVAVKNnwpleVKVGLIGSC-TNssYEDMSRAASVVKDaatHGLKSKSIFTVTPGSEQIRATIARDGQLETFKEFGGTV 448
Cdd:PRK09238 685 -EVAGTK-----IDEVFIGSCmTN--IGHFRAAGKLLEG---KKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARI 753
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50306025 449 LANACGPCIGQWDRqdIKKGDknTIVSSFNRNFTAR--NDGNpdthSFVASPEITTAFAIAGDL 510
Cdd:PRK09238 754 EMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKGAN----VYLGSAELAAVCALLGRI 809
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
663-731 |
6.42e-14 |
|
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: 68.00 E-value: 6.42e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 663 VVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYD-KINPDDTIDI 731
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
652-731 |
7.47e-12 |
|
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: 64.81 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 652 ARAYRDAGIrwvVIGGENFGEGSSREHA--ALEpRFlgGF-AIITKSFARIHETNLKKQGMLPLNfAEPAAYDKI----- 723
Cdd:COG0066 59 QPRYQGADI---LVAGRNFGCGSSREHApwALK-DY--GFrAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaie 131
|
....*....
gi 50306025 724 -NPDDTIDI 731
Cdd:COG0066 132 aNPGDELTV 140
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
171-510 |
4.73e-11 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 66.48 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 171 KPGSGIIHQIvLENYAFPGALIIGTDSHT--------PNAGGLgqlaIGVGGADAVdvmsdlaWELKAPKIMGVKLTGRM 242
Cdd:PLN00094 536 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfpigisfPAGSGL----VAFGAATGV-------IPLDMPESVLVRFTGTM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 243 NGWTSPKDII-------LKLAGITTVKGG-----TGKIVEYFG-------------DGVDTFSATGMGTICNMGAEIGAT 297
Cdd:PLN00094 604 QPGITLRDLVhaipytaIQDGLLTVEKKGkknvfSGRILEIEGlphlkceqafelsDASAERSAAGCTIKLDKEPIIEYL 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 298 TSVFPFNKSMI--DYLDA-TGRDKIAQFAQ-LYHKDLLSADEGAEYDEIIEIDLNTL-EPYVNGPFTPDLATPISKMKDV 372
Cdd:PLN00094 684 NSNVVMLKWMIaeGYGDRrTLERRIARMQQwLADPELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGD 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 373 AVKnnwplEVkvgLIGSC-TNSSYedMSRAASVVKDaatHGLKSKSIFTVTPGSEQIRATIARDGQLETFKEFGGTVLAN 451
Cdd:PLN00094 764 KID-----EV---FIGSCmTNIGH--FRAAGKLLND---NLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMP 830
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50306025 452 ACGPCIGQWDRQdikkGDKNTIVSSFNRNFTARNDGNPDThsFVASPEITTAFAIAGDL 510
Cdd:PLN00094 831 GCSLCMGNQARV----AEKSTVVSTSTRNFPNRLGKGANV--YLASAELAAVAAILGRL 883
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
663-731 |
1.09e-10 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 61.00 E-value: 1.09e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50306025 663 VVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGmLPLnFAEPAAYDKINPDDTIDI 731
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV-LECDEAVDKIEDGDEVEV 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
649-731 |
5.57e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 59.05 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 649 PDTARAYRDAGIrwvVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPlnFAEPAAYDKINPDDT 728
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDE 115
|
...
gi 50306025 729 IDI 731
Cdd:PRK14023 116 VEL 118
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
654-711 |
3.33e-09 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 57.44 E-value: 3.33e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50306025 654 AYRDAGIrwvVIGGENFGEGSSREHA--ALEpRFlgGF-AIITKSFARIHETNLKKQGMLP 711
Cdd:PRK01641 64 RYQGASI---LLAGDNFGCGSSREHApwALA-DY--GFrAVIAPSFADIFYNNCFKNGLLP 118
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
663-731 |
3.23e-08 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131139 [Multi-domain] Cd Length: 156 Bit Score: 53.64 E-value: 3.23e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50306025 663 VVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGmLPLNFAEPAAyDKINPDDTIDI 731
Cdd:TIGR02084 50 IIVAGENFGCGSSREHAPIAIKASGISCVIAKSFARIFYRNAINIG-LPIVESEEAV-DEIEEGDEVEV 116
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
663-745 |
3.81e-08 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 53.19 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50306025 663 VVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNfaepAAYDKINPDD--TIDILGLTTLAPG 740
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE----AKTEGIKDGDevTVDLETGEIRVNG 125
|
....*
gi 50306025 741 KNLIM 745
Cdd:TIGR02087 126 NEEYK 130
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
663-699 |
4.98e-06 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 48.70 E-value: 4.98e-06
10 20 30
....*....|....*....|....*....|....*..
gi 50306025 663 VVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARI 699
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
655-725 |
6.68e-06 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 129275 [Multi-domain] Cd Length: 188 Bit Score: 47.50 E-value: 6.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50306025 655 YRDAGIrwvVIGGENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGMLPLNFAEPAAYDKINP 725
Cdd:TIGR00171 67 YQGASI---LLARENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQ 134
|
|
| |
