|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
45-775 |
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: 1233.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 45 YDLLEKNINIVRKRLN-RPLTLSEKIVYGHLDDPAN----QEIE--RGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPK 117
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 118 VAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPN 197
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 198 GGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 277
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 278 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTDIANLAEEFKDH---LVPDPGCQYDQVIEINLNELKPHINGPFT 354
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSffkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 355 PDLAHPVADVGTVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQ 434
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 435 ILRDVGGIVLANACGPCIGQWDRKD-IKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDF 513
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 514 LTGKDGKKFKLEAPDADELPRSDFDPGQDTYQHPPKDS-SGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKC 592
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPnPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 593 TTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNaVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSRE 672
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYD-LDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 673 HAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNKIHPVDKLTIQGLKDFAP---GKPLKCVIKHPNGTQ 749
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 18079339 750 ETILLNHTFNETQIEWFRAGSALNRM 775
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
61-777 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 899.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 61 RPLTLSEKIVYGHLDDPanqEIERGKTyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTI-HCDHlieaqvggekD 139
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 140 LRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 219
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 220 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 300 NHRMKKYLSKTGRTDIAnlaeefkDHLVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPVADVGtvaekegwPLDIRV 379
Cdd:PRK07229 227 DERTREFLKAQGREDDW-------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVA--------GIKVDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 380 GLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQwdrkD 459
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 460 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLKfNPETdfLTGKDGKKFKLEAPDadelprsDFDP 539
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 540 GQDTYQHPPKDSSGQRVDVSPTSQRLQLLEPFDkwdgkDLEDLQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 618
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 619 IGAINIENGKAnsvrnavtQEFGPvpdtaryykkhgirWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN 698
Cdd:PRK07229 509 EGVDNTFPERA--------KEQGG--------------GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18079339 699 LKKQGLLPLTFADPSDYNKIHPVDKLTIQGLKDFAPGKPLKCVIKHPNgtqETILLNHTFNETQIEWFRAGSALNRMKE 777
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
95-505 |
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: 872.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 95 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIH 174
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 175 QIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGI 254
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 255 LTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTDIANLAEEFK-DHLVPDPGCQ 333
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 334 YDQVIEINLNELKPHINGPFTPDLAHPVADVGTVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQ 413
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 414 FTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSP 493
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 18079339 494 EIVTALAIAGTL 505
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
41-775 |
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: 751.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 41 EYIRYDL--LEKNINIVRKrlnrpLTLSEKIVYGHLD---DPAN------------QEIERGKTYLRLRPDRVAMQDATA 103
Cdd:COG1048 17 PYTYYSLpaLEEAGGDISR-----LPYSLKILLENLLrneDGETvteedikalanwLPKARGDDEIPFRPARVLMQDFTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 104 QMAMLQFISSGLPKV-----------AVPSTIHCDHLIEAQVGG-----EKDLRRAKDINQEVYNFLATAGAKY-GVGFW 166
Cdd:COG1048 92 VPAVVDLAAMRDAVArlggdpkkinpLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 167 RPGSGIIHQIILENYA--------------YPGvLLIGTDSHTPNggglggicigvggA-------------DAVDVMAG 219
Cdd:COG1048 172 PPGTGIVHQVNLEYLAfvvwtreedgetvaYPD-TLVGTDSHTTM-------------InglgvlgwgvggiEAEAAMLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 220 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:COG1048 238 QPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 300 NHRMKKYLSKTGRTDIA-NLAEE-------FKDHLVPDPgcQYDQVIEINLNELKPHINGPFTPDLAHPVADVGTVAEKE 371
Cdd:COG1048 318 DEETLDYLRLTGRSEEQiELVEAyakaqglWRDPDAPEP--YYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 372 GWPL-----------------------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCK--SQFTITPGSEQIRA 425
Cdd:COG1048 396 LAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCTNTSNPSVMIAAGlLAKKAVEKGLKVKpwVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 426 TIERDGYAQILRDVGGIVLANACGPCIGQWDR------KDIKKGE-KNTIVTSYNRNFTGRNDaNPETHAFVTSPEIVTA 498
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVVA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 499 LAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADELP--------RSDFD------------------PGQDTYQHPPK 549
Cdd:COG1048 555 YALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPaavfkavtPEMFRaryadvfdgderwqalevPAGELYDWDPD 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 550 DSSgqrVDVSPTSQRLQLL-EPFdkwdgKDLEDLQILIKVKGKCTTDHISAAGP-----------------------WLK 605
Cdd:COG1048 635 STY---IRRPPFFEGLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 606 FRGHLDNISNNLLIGaINIEN-----GKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRH 680
Cdd:COG1048 707 RRGNHEVMMRGTFAN-IRIKNllapgTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRL 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 681 LGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNK--IHPVDKLTIQGLKD-FAPGKPLKCVIKHPNGTQETILLNHT 757
Cdd:COG1048 786 LGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHR 865
|
890
....*....|....*....
gi 18079339 758 F-NETQIEWFRAGSALNRM 775
Cdd:COG1048 866 IdTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
67-503 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 559.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 67 EKIVYGHLDDPANQEIERgktylrlRPDRVAMQDATAQMAMLQFISSGLPK-----------VAVPSTIHCDHlieAQVG 135
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLY-------IPDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 136 GEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggA--- 211
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 212 ----------DAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMA 281
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 282 TICNMGAEIGATTSVFPYNHRMKKYLSKTGRTDIANLAEEFK----DHLVPDPGCQYDQVIEINLNELKPHINGPFTPDL 357
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKGEAYDKavawKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 358 AHPVAD------------------VGTVAEKEGWPL---DIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKS--QF 414
Cdd:pfam00330 298 AVPLSElvpdpfadavkrkaaeraLEYMGLGPGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPgvKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 415 TITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGRNdaNPETHAFVTSPE 494
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
gi 18079339 495 IVTALAIAG 503
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
95-505 |
2.24e-169 |
|
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: 493.55 E-value: 2.24e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 95 RVAMQDATAQMAMLQFISSGLP-KVAVPSTIHCDHLIEAQVggekdlrrAKDINQEVYNFLATAGAKYGVGFWRPGSGII 173
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALgKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 174 HQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAG 253
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 254 ILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTDIANLAEEFKDHLVPDPGCQ 333
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 334 YDQVIEINLNELKPHINGPFTPDLAHPVADVGTvaekegwpLDIRVGLIGSCTNSSYEDMGRSAAVAKQALahgLKCKSQ 413
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 414 FTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRkdiKKGEKNTIVTSYNRNFTGRNDANPEtHAFVTSP 493
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
gi 18079339 494 EIVTALAIAGTL 505
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
64-777 |
2.13e-124 |
|
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: 387.42 E-value: 2.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 64 TLSEKIVYGHLddpANQEIERGKTyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIEaqvggEKDLRR 142
Cdd:TIGR01342 1 TLAEKIIDDHL---VEGDLEPGEE-IAIEIDQTLSQDATGTMCWLEFEALEMDEVKTElAAQYCDHNML-----QFDFKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 143 AKDinqevYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPW 222
Cdd:TIGR01342 72 ADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 223 ELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHR 302
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 303 MKKYLSKTGRTDianlaeEFKDhLVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPVADVgtvaekEGWPLDIRVglI 382
Cdd:TIGR01342 227 TEAWLAAFDRED------DFVD-LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREI------AGIEVDQVM--I 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 383 GSCTNSSYEDMGRSAAVAKQALAHGlkcKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQwdrkDIKK 462
Cdd:TIGR01342 292 GSCTNGAFEDLLPAAKLLEGREVHK---DTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 463 GEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLkFNPETdfLTGKDGKkfkLEAPDAdELPRS---DFDP 539
Cdd:TIGR01342 365 ASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPRD--LADDEGD---LEAIGF-EMGEKfpgGYDA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 540 GqDTYQHPPKDSSGQRVDVSPTSQRLQLLEPFdkwdGKDLEDlQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 618
Cdd:TIGR01342 437 A-DIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEFTL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 619 igainiengkansvrNAVTQEFGPVPDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN 698
Cdd:TIGR01342 511 ---------------HRIDDEFAERAKAADEKGKAGI---IIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHAN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 699 LKKQGLLPLTFADPSDYNKIHPVDKLTIQG--LKDFAPGKPLKCVIKHpngTQETILLNHTFNETQIEWFRAGSALNRMK 776
Cdd:TIGR01342 573 LFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEFTINKN---DDEEALATLDASEREKEILAAGGKLNLIK 649
|
.
gi 18079339 777 E 777
Cdd:TIGR01342 650 N 650
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
587-735 |
8.05e-109 |
|
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: 328.27 E-value: 8.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 587 KVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYG 666
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18079339 667 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNKIHPVDKLTIQGLKDFAPG 735
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
94-505 |
3.34e-108 |
|
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: 335.57 E-value: 3.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 94 DRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIEAQvggekDLRRAKDinqevYNFLATAGAKYGVGFWRPGSGI 172
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTElSVSYVDHNTLQT-----DFENADD-----HRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 173 IHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVA 252
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 253 GILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTDianlaeEFKDhLVPDPGC 332
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRED------DWVE-LAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 333 QYDQVIEINLNELKPHINGPFTPDLAHPVADVGtvaekegwPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGlkcKS 412
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPDNVVPVREVA--------GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHP---HV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 413 QFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDrkdiKKGEKNTIVTSYNRNFTGRNdANPETHAFVTS 492
Cdd:cd01585 293 SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLAS 367
|
410
....*....|...
gi 18079339 493 PEIVTALAIAGTL 505
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
92-780 |
4.76e-77 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 266.80 E-value: 4.76e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 92 RPDRVAMQDATAQ------MAMLQFISS--GLPKV---AVPSTIHCDHLIEAQVGGEKD-LRRAKDI----NQEVYNFLA 155
Cdd:PRK12881 82 VPARVVMQDFTGVpalvdlAAMRDAAAEagGDPAKinpLVPVDLVVDHSVAVDYFGQKDaLDLNMKIefqrNAERYQFLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 156 -TAGAKYGVGFWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMA 218
Cdd:PRK12881 162 wGMQAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTTmiNGIGVLGWGVGGIEAEAV--ML 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 219 GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 298
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 299 YNHRMKKYLSKTGRTD--IAnLAEEFKDH----LVPDPGCQYDQVIEINLNELKPHINGP---------------FTPDL 357
Cdd:PRK12881 319 VDEQTLDYLRLTGRTEaqIA-LVEAYAKAqglwGDPKAEPRYTRTLELDLSTVAPSLAGPkrpqdrialgnvksaFSDLF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 358 AHPVADVGTVAEKEGWPL------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCKS--QFTITPGSEQIRATIE 428
Cdd:PRK12881 398 SKPVAENGFAKKAQTSNGvdlpdgAVAIAAITSCTNTSNPSVLIAAGlLAKKAVERGLTVKPwvKTSLAPGSKVVTEYLE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 429 RDGYAQILRDVG-GIVlANACGPCIGQWD------RKDIKKGE-KNTIVTSYNRNFTGRNDANPEThAFVTSPEIVTALA 500
Cdd:PRK12881 478 RAGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRIHPNIKA-NFLASPPLVVAYA 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 501 IAGTLKFNPETDFL-TGKDGKKFKLE-----APDADELPRSDFDPgqDTYQH---PPKDSSGQRVDVS-PTSQRLQ---- 566
Cdd:PRK12881 556 LAGTVRRDLMTEPLgKGKDGRPVYLKdiwpsSAEIDALVAFAVDP--EDFRKnyaEVFKGSELWAAIEaPDGPLYDwdpk 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 567 ---LLEP--FDKWDG-----KDLEDLQILIKVKGKCTTDHIS---------AAGPWLKFRGHLDNISN------------ 615
Cdd:PRK12881 634 styIRRPpfFDFSMGpaasiATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNsygsrrgnhevm 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 616 -----------NLLIGAinIENGkanSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGR 684
Cdd:PRK12881 714 mrgtfanvrikNLMIPG--KEGG---LTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVK 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 685 AIITKSFARIHETNLKKQGLLPLTF--ADPSDYNKIHPVDKLTIQGL-KDFAPGKPLKCVIKHPNGTQETILLNHTFnET 761
Cdd:PRK12881 789 AVIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRI-DT 867
|
810 820
....*....|....*....|.
gi 18079339 762 QIE--WFRAGSALNRMkeLQQ 780
Cdd:PRK12881 868 PIEvdYYKAGGILPYV--LRQ 886
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
62-505 |
1.22e-76 |
|
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: 253.80 E-value: 1.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 62 PLTLSEKIvyghLDDPANQEIERGKTYLrLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqvggeKD 139
Cdd:COG0065 2 GMTLAEKI----LARHAGREVEPGEIVL-LYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 140 LRRAKDINQevynfLATAGAKYGVGFWRPGS-GIIHQIILEN-YAYPGVLLIGTDSHTPNGGglggicigvggA------ 211
Cdd:COG0065 72 PKSAEQVKT-----LREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHG-----------Afgafaf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 212 -----DAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICN 285
Cdd:COG0065 136 gigttDVAHVLAtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 286 MGAEIGATTSVFPYNHRMKKYLSKTGRTDIANLAeefkdhlvPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPVADVg 365
Cdd:COG0065 215 MAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLK--------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSEL- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 366 tvaekEGWPLDirVGLIGSCTNSSYEDMGRSAAVAKqalahGLKCKS--QFTITPGSEQIRATIERDGYAQILRDVGGIV 443
Cdd:COG0065 286 -----EGIKID--QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPgvRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18079339 444 LANACGPCIG-QWDRkdIKKGEKnTIVTSyNRNFTGRNdANPETHAFVTSPEIVTALAIAGTL 505
Cdd:COG0065 354 REPGCGMCLGmNMGV--LAPGER-CASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
92-774 |
2.42e-75 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 261.98 E-value: 2.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 92 RPDRVAMQDAT--------AQM--AMLQF------ISsglPKVAVPSTIhcDHLIEAQVGGEKD-LRRAKDI----NQEV 150
Cdd:PRK09277 83 RPARVVMQDFTgvpavvdlAAMrdAIADLggdpakIN---PLVPVDLVI--DHSVQVDYFGTPDaFEKNVELeferNEER 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 151 YNFLatagaKYGVGFWR------PGSGIIHQIILE-------------NYAYPGVLlIGTDSHTPnggglggicigvgga 211
Cdd:PRK09277 158 YQFL-----KWGQKAFDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT--------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 212 dAVD----------------VMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSI 275
Cdd:PRK09277 217 -MINglgvlgwgvggieaeaAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 276 SCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTD--IAnLAEEFKDH----LVPDPGCQYDQVIEINLNELKPHI 349
Cdd:PRK09277 296 SLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEeqVA-LVEAYAKAqglwRDPLEEPVYTDVLELDLSTVEPSL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 350 NGP-------FTPDLAH--------PVADVGTVAEKEGWPLDIRVG-----LIGSCTNSS--YEDMGrsAA-VAKQALAH 406
Cdd:PRK09277 375 AGPkrpqdriPLSDVKEafaksaelGVQGFGLDEAEEGEDYELPDGavviaAITSCTNTSnpSVMIA--AGlLAKKAVEK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 407 GLKCKS--QFTITPGSEQIRATIERDGYAQILRDVG-GIVlANACGPCIG---------QwdrKDIKkgEKNTIVT---S 471
Cdd:PRK09277 453 GLKVKPwvKTSLAPGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAIN--DNDLVVTavlS 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 472 YNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADE---LPRSDFDPGQ--D 542
Cdd:PRK09277 527 GNRNFEGR--IHPLVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEidaVVAKAVKPEMfrK 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 543 TYQHPPK-DSSGQRVDVS--------PTSQRLQlLEPFdkWDG--------KDLEDLQILIKVKGKCTTDHIS------- 598
Cdd:PRK09277 605 EYADVFEgDERWNAIEVPegplydwdPDSTYIR-NPPY--FEGmlaepgpvRDIKGARVLALLGDSITTDHISpagaika 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 599 --AAGPWLK--------F--------------RGHLDNIS--NNLLIGainIENGKAnsvRNAVTQEFGPVPDTARYYKK 652
Cdd:PRK09277 682 dsPAGKYLLehgvepkdFnsygsrrgnhevmmRGTFANIRirNEMVPG---VEGGYT---RHFPEGEVMSIYDAAMKYKE 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 653 HGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYN--KIHPVDKLTIQGLK 730
Cdd:PRK09277 756 EGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLE 835
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 18079339 731 DFAPGKPLKCVIKHPNGTQETI-LLNHTFNETQIEWFRAGSALNR 774
Cdd:PRK09277 836 DLKPGATVTVVITRADGEVVEFpVLCRIDTAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
62-503 |
2.24e-69 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 234.30 E-value: 2.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 62 PLTLSEKIVYGHlddpANQEIERGKtYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqvggeKD 139
Cdd:PRK00402 2 GMTLAEKILARH----SGRDVSPGD-IVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 140 LRRAKdINQEVYNFLATAGAKYgvgFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV---- 214
Cdd:PRK00402 72 IKSAE-QQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALgafa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 215 ------D---VMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATIC 284
Cdd:PRK00402 135 tgmgstDmaaAMAtGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 285 NMGAEIGATTSVFPYNHRMKKYLsktgrtdiANLAEEFKDHLVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPVADV 364
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYL--------KERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 365 gtvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVL 444
Cdd:PRK00402 286 ------EGTKVDQVF--IGSCTNGRLEDLRIAAEILK---GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVS 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 18079339 445 ANACGPCIGqwdrkdIKKGEknTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 503
Cdd:PRK00402 355 TPTCGPCLGghm-gvLAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
95-503 |
1.03e-66 |
|
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: 225.92 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 95 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqvggekDLRRAKDINQEVYNFLATAGAK-YGVGfwrpGSG 171
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT------PDIKAAEQVKTLRKFAKEFGINfFDVG----RQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 172 IIHQIILENY-AYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 249
Cdd:cd01583 71 ICHVILPEKGlTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 250 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRtdianlaEEFKdHLVPD 329
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-------AYWK-ELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 330 PGCQYDQVIEINLNELKPHINGPFTPDLAHPVADVgtvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLK 409
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEV------EGIKIDQVF--IGSCTNGRLEDLRAAAEILK---GRKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 410 CKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIG-QWDRkdIKKGEknTIVTSYNRNFTGR-NDANPETH 487
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRmGSPGARIY 366
|
410
....*....|....*.
gi 18079339 488 afVTSPEIVTALAIAG 503
Cdd:cd01583 367 --LASPATAAASAITG 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
94-709 |
9.95e-62 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 223.74 E-value: 9.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 94 DRVAMQDAtaqMAML----QFISsglPKVAVPSTIhcDHLIEAQVGGEKD-LRRAKDI----NQEVYNFLatagaKYGVG 164
Cdd:PTZ00092 106 DLAAMRDA---MKRLggdpAKIN---PLVPVDLVI--DHSVQVDFSRSPDaLELNQEIeferNLERFEFL-----KWGSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 165 FWR------PGSGIIHQIILE----------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMAGIPWELKC 226
Cdd:PTZ00092 173 AFKnllivpPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 227 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKY 306
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 307 LSKTGRTDIA-NLAEEF--KDHLVPDPGCQ--YDQVIEINLNELKPHINGP---------------FTPDLAHPVA---- 362
Cdd:PTZ00092 330 LKQTGRSEEKvELIEKYlkANGLFRTYAEQieYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGfkgf 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 363 -----DVGTVAEKE--GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATI 427
Cdd:PTZ00092 410 gipeeKHEKKVKFTykGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPyiKTSLSPGSKVVTKYL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 428 ERDGYAQILRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVT 497
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVV 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 498 ALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADEL--------------------------------PRSDF---DP 539
Cdd:PTZ00092 566 AYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIqaleakyvkpemfkevysnitqgnkqwnelqvPKGKLyewDE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 540 gQDTYQHPPKDSSGQRVDVSPTsqrlqllepfdkwdgKDLEDLQILIKVKGKCTTDHISAAG------PWLKF------- 606
Cdd:PTZ00092 646 -KSTYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlmergve 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 607 ------------------RGHLDNIS-NNLLIGA-----INIENGKANSVRNAvtqefgpvpdtARYYKKHGIRWVVIGD 662
Cdd:PTZ00092 710 rkdfntygarrgndevmvRGTFANIRlINKLCGKvgpntVHVPTGEKMSIYDA-----------AEKYKQEGVPLIVLAG 778
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 18079339 663 ENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTF 709
Cdd:PTZ00092 779 KEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQF 825
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
582-712 |
1.45e-61 |
|
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: 202.98 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 582 LQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIG 661
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18079339 662 DENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP 712
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
67-714 |
1.68e-59 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 217.75 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 67 EKIVYGHLDDPANQEIErgktylrLRPDRVAMQDAT--------AQM--AMLQFIS-SGLPKVAVPSTIHCDHLIEAQVG 135
Cdd:PLN00070 103 EKIIDWENTSPKQVEIP-------FKPARVLLQDFTgvpavvdlACMrdAMNNLGGdPNKINPLVPVDLVIDHSVQVDVA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 136 GEKDLRRAK-----DINQEVYNFLatagaKYGVGFWR------PGSGIIHQIILENYA----------YPGVLlIGTDSH 194
Cdd:PLN00070 176 RSENAVQANmelefQRNKERFAFL-----KWGSTAFQnmlvvpPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDSH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 195 TPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDS 274
Cdd:PLN00070 250 TTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 275 ISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTD----------IANlaEEFKDHLVPDPGCQYDQVIEINLNE 344
Cdd:PLN00070 330 LSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDetvamieaylRAN--KMFVDYNEPQQERVYSSYLELDLED 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 345 LKPHINGPFTPD---------------LAHPVADVGTVAEKE-----------GWPLDIRVG-----LIGSCTNSSYED- 392
Cdd:PLN00070 408 VEPCISGPKRPHdrvplkemkadwhscLDNKVGFKGFAVPKEaqskvakfsfhGQPAELRHGsvviaAITSCTNTSNPSv 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 393 MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI-- 468
Cdd:PLN00070 488 MLGAGLVAKKACELGLEVKPwiKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG--NSGELDESVASAIte 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 469 -------VTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKK--FKLEAPDADE------ 531
Cdd:PLN00070 566 ndivaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEvaevvq 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 532 ---LPrsdfDPGQDTYQHPPKDS---------SGQRVDVSPTSQRLQllEP-------FDKWDGKDLEDLQILIKVKGKC 592
Cdd:PLN00070 644 ssvLP----DMFKSTYEAITKGNpmwnqlsvpSGTLYSWDPKSTYIH--EPpyfknmtMSPPGPHGVKDAYCLLNFGDSI 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 593 TTDHISAAG------PWLKF-------------------------RGHLDNIS--NNLLIG-----AINIENGKANSVRn 634
Cdd:PLN00070 718 TTDHISPAGsihkdsPAAKYlmergvdrkdfnsygsrrgndeimaRGTFANIRivNKLLKGevgpkTVHIPTGEKLSVF- 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 635 avtqefgpvpDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSD 714
Cdd:PLN00070 797 ----------DAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGED 866
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
94-503 |
3.97e-58 |
|
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: 203.45 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 94 DRVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqvggekDLRRAKDINQEVYNFLATAGAKYgvgFWRPGSG 171
Cdd:TIGR01343 26 DLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTIKAAEMQKLAREFVKKQGIKY---FYDVGEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 172 IIHQIILEN-YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 249
Cdd:TIGR01343 97 ICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAtGKTW-FKVPETIRVNITGKLNPGVTAKDVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 250 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRTDianlAEEFKDhlvpD 329
Cdd:TIGR01343 176 EVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP----FRVYKS----D 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 330 PGCQYDQVIEINLNELKPHINGPFTPDLAHPVADVgtvaekEGWPLDiRVgLIGSCTNSSYEDMGRSAAVAKqalAHGLK 409
Cdd:TIGR01343 248 EDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV-FIGSCTNGRLEDLRVAAKILK---GRKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 410 CKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGqwdRKDIKKGEKNTIVTSYNRNFTGRNdANPETHAF 489
Cdd:TIGR01343 317 PDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQGVLAPGEVCISTSNRNFKGRM-GHPNAEIY 392
|
410
....*....|....
gi 18079339 490 VTSPEIVTALAIAG 503
Cdd:TIGR01343 393 LASPATAAASAVKG 406
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
95-504 |
4.92e-46 |
|
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: 169.79 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 95 RVAMQDATAQMAMLQFIS--------SGLP-KV--AVPSTIHCDHLIEAQVGG-----EKDLRRAKDINQEVYNFLATAG 158
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAmrdavkrlGGDPeKInpLIPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 159 AKYG-VGFWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWE 223
Cdd:cd01586 81 KAFKnLRVVPPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 224 LKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNhrm 303
Cdd:cd01586 160 MLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 304 kkylsktgrtdianlaeefkdhlvpdpgcqyDQVIEINLNELKPHINGPFTPDLAHPVadvgtvaekEGwplDIRVGLIG 383
Cdd:cd01586 237 -------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL---------HG---SVVIAAIT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 384 SCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIG------Q 454
Cdd:cd01586 274 SCTNTSNPSvMLAAGLLAKKAVELGLKVKPyvKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 18079339 455 WDRKDIKKGE-KNTIVTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGT 504
Cdd:cd01586 354 EVEEAIKENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
108-505 |
1.99e-36 |
|
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: 141.21 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 108 LQFISSGLPKVAVPSTIHC--DHliEAQVGGEKDLRRAKDINqevyNFlataGAKYGVGFWRPGSGIIHQIILEN-YAYP 184
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH--DVQNKSEKNLKKYKNIE----SF----AKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 185 GVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGA 263
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 264 IVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRmkkylsktgrtdianlaeefkdHLVpdpgcqydqvieINLN 343
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------HLI------------LDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 344 ELKPHINGPFTPDLAHPVADVgtvaekEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQA--------LAHGLKcksqFT 415
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL------EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGVE----FY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 416 ITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGqWDRKDIKKGEKNtiVTSYNRNFTGRNdANPETHAFVTSPEI 495
Cdd:cd01582 278 VAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLASPAV 353
|
410
....*....|
gi 18079339 496 VTALAIAGTL 505
Cdd:cd01582 354 VAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
227-505 |
3.25e-31 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 127.93 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 227 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGA---------TTsvF 297
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT--F 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 298 PYnhrMKkylsktGRtDIANLAEEFK------DHLVPDPGCQYDQVIEINLNELKPH------------INGPF-TPDLA 358
Cdd:PRK05478 241 EY---LK------GR-PFAPKGEDWDkavaywKTLKSDEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKVpDPEDF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 359 HPVADVGTVAE-------KEGWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRAT 426
Cdd:PRK05478 311 ADPVKRASAERalaymglKPGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVK-----GRKVAPGVRalVVPGSGLVKAQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 427 IERDGYAQILRDVG------GivlanaCGPCIGQWDrkDIKKGEKNTIVTSyNRNFTGRNDANPETHafVTSPEIVTALA 500
Cdd:PRK05478 386 AEAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPAMAAAAA 454
|
....*
gi 18079339 501 IAGTL 505
Cdd:PRK05478 455 ITGHF 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
587-728 |
6.62e-30 |
|
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: 113.33 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 587 KVKGKCTTDHISAAGPWlkfrghldnisnnlligainiengkansvrnavtqefgpvpdtaryykkhgirwVVIGDENYG 666
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18079339 667 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNKIHPVDKLTIQG 728
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
60-505 |
2.42e-28 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 119.24 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 60 NRPLTLSEKIVYGH----LDDpanqeierGKTYLRLrpDRVAMQDATAQMAMLQFISSGLPkVAVPSTIHC--DHLIEAQ 133
Cdd:PRK12466 1 MMPRTLYDKLWDSHtvarLDD--------GHVLLYI--DRHLLNEYTSPQAFSGLRARGRT-VRRPDLTLAvvDHVVPTR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 134 VGGEKDLRRAKDINQEVYnfLATAGAKYGVGFWR---PGSGIIHQIILE-NYAYPGVLLIGTDSHTPNGGGLGGICIGVG 209
Cdd:PRK12466 70 PGRDRGITDPGGALQVDY--LRENCADFGIRLFDvddPRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 210 GADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAE 289
Cdd:PRK12466 148 TSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 290 IGATTSVFPYNHRMKKYLSKTGRTDIANLAEEFKDH---LVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPV----- 361
Cdd:PRK12466 228 AGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYwrtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPItgrvp 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 362 --ADVGTVAEKE-------------GWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSE 421
Cdd:PRK12466 308 dpAAEADPARRAameraldymgltpGTPLaGIPIDrvFIGSCTNGRIEDLRAAAAVLR-----GRKVAPGVRamVVPGSG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 422 QIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKdIKKGEKntIVTSYNRNFTGRNDANPETHafVTSPEIVTALAI 501
Cdd:PRK12466 383 AVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV-LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAV 457
|
....
gi 18079339 502 AGTL 505
Cdd:PRK12466 458 AGHI 461
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
587-728 |
2.68e-28 |
|
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: 109.83 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 587 KVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLIGainiengkansvrnaVTQEFGPvpdtaryYKKHGIRWVVIGDENY 665
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHR---------------VDPTFAE-------RAKAAGPGFIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18079339 666 GEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNKIHPVDKLTIQG 728
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL 121
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
89-731 |
3.23e-24 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 108.56 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 89 LRLRPDRVAMQDAT----AQMAmlqfISSGLPKVAVPSTIHCDHLIEAQVGGEkdlrrakdINQEVYNFLATAGAKYGVG 164
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 165 FWRPGSGIIHQIILENYAYPGVLLIGTDSHTpnggglggicigvgGADAVDVMA---GIP----------WELKCPKVIG 231
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgeGGGelvkqllndtYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 232 VKLTGSLSGWTSPKDVILKVAGILTVKGGT-GAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKT 310
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 311 GRtdianlAEEFKDhLVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPVA-------DVGTVAEKEGWPLD------- 376
Cdd:PRK11413 268 GR------GQDYCE-LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDelnqnltDILREVEIESERVAhgkakls 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 377 ---------IRV--GLIGSCTNSSYEDMgrsaavakQALAHGLKCKS----QFTIT--PGSEQIRATIERDGYAQILRDV 439
Cdd:PRK11413 341 lldkiengrLKVqqGIIAGCSGGNYENV--------IAAANALRGQScgndTFSLSvyPSSQPVFMDLAKKGVVADLMGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 440 GGIVLANACGPCIGQWDrkdikkgekntivTSYN---------RNFTGRNDANPeTHAFVTSPEIVTALAIAGTLKFNpe 510
Cdd:PRK11413 413 GAIIRTAFCGPCFGAGD-------------TPANnglsirhttRNFPNREGSKP-ANGQMSAVALMDARSIAATAANG-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 511 tDFLTGKDgkkfklEAPDADELPRSDFDPgqDTYQHPPKDSSGQRVdvspTSQRLQLLEPFDKWdgKDLEDL--QILIKV 588
Cdd:PRK11413 477 -GYLTSAT------ELDCWDNVPEYAFDV--TPYKNRVYQGFGKGA----TQQPLIYGPNIKDW--PEMGALtdNILLKV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 589 KGK-----CTTDHISAAGPWLKFRghldniSNNLLIGAIN--------IENGKA-----NSVRNAVTQEFGPVPDTAR-Y 649
Cdd:PRK11413 542 CSKildpvTTTDELIPSGETSSYR------SNPLGLAEFTlsrrdpgyVGRSKAvaeleNQRLAGNVSELTEVFARIKqI 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 650 YKKHGIRW--VVIGDENY----GEGSSREHAALEPRHLGGRAIITKSFA-RIHETNLKKQGLLPLTFADPSDynkIHPVD 722
Cdd:PRK11413 616 AGQEHIDPlqTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEEPT---FEVGD 692
|
....*....
gi 18079339 723 KLTIQGLKD 731
Cdd:PRK11413 693 YIYIPGIRA 701
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
593-712 |
1.49e-18 |
|
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: 83.86 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 593 TTDHISAAGPWLK-------------------------------FRGHLDNISN-NLLIGainieNGKANSVRNAVTQEF 640
Cdd:cd01580 7 TTDHISPAGSIAKdspagkylaergvkprdfnsygsrrgndevmMRGTFANIRLrNKLVP-----GTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18079339 641 GPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP 712
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPG 153
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
658-726 |
1.33e-13 |
|
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: 66.84 E-value: 1.33e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP-SDYNKIHPVDKLTI 726
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEdVEEVEAKPGDEVEV 89
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
65-505 |
1.39e-12 |
|
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: 70.61 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 65 LSEKIVyGHldDPANQEIERGkTYLRLRPDRVAMQDATAQM--------AMLQFISSGlpkvAVPSTIHcdhliEAQVGG 136
Cdd:cd01581 1 LAQKIV-GR--ACGVKGVRPG-TYCEPKMTTVGSQDTTGPMtrdelkelACLGFSADL----VMQSFCH-----TAAYPK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 137 EKDLRRAKDINQEVYNFlatagakyGVGFWRPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAV 214
Cdd:cd01581 68 PVDVKTHRTLPDFISNR--------GGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFAAAT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 215 DVMAgipweLKCPKVIGVKLTGSLSGWTSPKDVILKV------AGILTV--KGG----TGAIVEYHGpgVDSISCTGMAT 282
Cdd:cd01581 139 GVMP-----LDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 283 ICNMGAEIGATTSVFPYNH------------RMKKYLSKtGRTDIANLAEEFKDH---------LVPDPGCQYDQVIEIN 341
Cdd:cd01581 212 LTDASAERSAAACTVRLDKepvieylesnvvLMKIMIAN-GYDDARTLLRRIIAMeewlanpplLEPDADAEYAAVIEID 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 342 LNELK-PHINGPFTPDlahpvaDVGTVAEKEGWPLDIrvGLIGSC-TNssyedMGRSAAVAKQALAHGLKcKSQFTITPG 419
Cdd:cd01581 291 LDDIKePILACPNDPD------DVKLLSEVAGKKIDE--VFIGSCmTN-----IGHFRAAAKILRGKEFK-PTRLWVAPP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 420 SEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--NDANpethAFVTSPEIVT 497
Cdd:cd01581 357 TRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAA 428
|
....*...
gi 18079339 498 ALAIAGTL 505
Cdd:cd01581 429 VCALLGRI 436
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
658-751 |
2.57e-11 |
|
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: 63.27 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTfADPSDYNKI------HPVDKLTIqglkD 731
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDELTV----D 141
|
90 100
....*....|....*....|
gi 18079339 732 FApgkplKCVIKHPNGTQET 751
Cdd:COG0066 142 LE-----AGTVTNGTGETYP 156
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
152-505 |
7.45e-11 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 65.71 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 152 NFLATAGakyGVGFwRPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKV 229
Cdd:PLN00094 525 DFIRNRG---GVSL-RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFGAATGVIP-----LDMPES 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 230 IGVKLTGSLSGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYHGpgVDSISCTGMATICNMGAEIGAT---- 293
Cdd:PLN00094 595 VLVRFTGTMQPGITLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAgcti 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 294 ----TSVFPY---NHRMKKYLSKTGRTD-------IANLAEEFKD-HLV-PDPGCQYDQVIEINLNELK-PHINGPFTPD 356
Cdd:PLN00094 673 kldkEPIIEYlnsNVVMLKWMIAEGYGDrrtlerrIARMQQWLADpELLeADPDAEYAAVIEIDMDEIKePILCAPNDPD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 357 lahpvaDVGTVAEKEGWPLDiRVgLIGSC-TNssyedMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQI 435
Cdd:PLN00094 753 ------DARLLSEVTGDKID-EV-FIGSCmTN-----IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYST 819
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18079339 436 LRDVGGIVLANACGPCIGQWDRkdikKGEKNTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 505
Cdd:PLN00094 820 FGTVGARTEMPGCSLCMGNQAR----VAEKSTVVSTSTRNFPNRlgKGAN----VYLASAELAAVAAILGRL 883
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
658-726 |
3.95e-09 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 56.37 E-value: 3.95e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18079339 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDynKIHPVDKLTI 726
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVD--KIEDGDEVEV 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
644-714 |
1.11e-08 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 55.19 E-value: 1.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18079339 644 PDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSD 714
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVD 108
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
326-505 |
4.00e-08 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 57.11 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 326 LVPDPGCQYDQVIEINLNELK-PHINGPFTPDLAHPVADVGtvAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQA 403
Cdd:PRK09238 647 LEADADAEYAAVIEIDLAEIKePILACPNDPDDVRLLSEVA--GTK------IDEVFIGSCmTN-----IGHFRAAGKLL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18079339 404 LAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--ND 481
Cdd:PRK09238 714 EGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKG 789
|
170 180
....*....|....*....|....
gi 18079339 482 ANpethAFVTSPEIVTALAIAGTL 505
Cdd:PRK09238 790 AN----VYLGSAELAAVCALLGRI 809
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
658-707 |
5.58e-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: 52.81 E-value: 5.58e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 18079339 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 707
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
658-726 |
5.19e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 50.90 E-value: 5.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18079339 658 VVIGDENYGEGSSREHA--ALEprHLGGRAIITKSFARIHETNLKKQGLLPLTfADPSDYNKI------HPVDKLTI 726
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELfklveaNPGAELTV 143
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
658-694 |
2.15e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.78 E-value: 2.15e-05
10 20 30
....*....|....*....|....*....|....*..
gi 18079339 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARI 694
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| |
