|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
52-782 |
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: 1416.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 52 YEKLNKRLEVVRGRLN-RPLTLSEKVLYSHLDDPAN----QDI--VRGTSYLRLRPDRVAMQDATAQMALLQFISSGLKK 124
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIgdVRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 125 VAVPSTVHCDHLIEAQIGGPKDLARAKDLNKEVYDFLASTCAKYGLGFWKPGSGIIHQIILENYAFPGLLMIGTDSHTPN 204
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 205 GGGLGGLCIGVGGADAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISC 284
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 285 TGMATICNMGAEIGATTSLFPFNQRMADYLKSTGRAGIASEAQ--KYQAKILSADKNCEYDELIEINLDTLEPHVNGPFT 362
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKtgQYSFFKLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 363 PDLGHPISKLGENSKKNGYPMDIRVGLIGSCTNSSYEDMGRCASIAKDAMSHGLKSKIPFNVTPGSEQIRATIERDGISE 442
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 443 VFDKFGGTVLANACGPCIGQWDRKD-VKKGDKNTIVTSYNRNFTGRNDANPATHCFVTSPELVTALSIAGRLDFNPLTDE 521
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 522 LTGADGKKFKLKAPFGDELPAKGFDPGQDTYTAPPPS-GENVKVAVDPKSTRLQLLEPFDKWNGQDLTDLTVLIKVKGKC 600
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSpNPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 601 TTDHISAAGPWLKYRGHLDNISNNMFIGATNYENNEMNNIKNQrNGSWGGVPDVARDYKANGIKWVAVGDENYGEGSSRE 680
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDL-DGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 681 HAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYDKIQPTSKISLLNLKSLAP---GKPVDAEIKN-GDKV 756
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKkNGKV 719
|
730 740
....*....|....*....|....*.
gi 17864292 757 ERIKLNHTLNDLQIGWFKAGSALNRM 782
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
68-784 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 903.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 68 RPLTLSEKVLYSHLDDPanqDIVRGTSyLRLRPDRVAMQDATAQMALLQFISSGLKKVAVPSTV-HCDHlieaqiggpkD 146
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 147 LARAKDLNKEVYDFLASTCAKYGLGFWKPGSGIIHQIILENYAFPGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMAD 226
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 227 IPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPF 306
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 307 NQRMADYLKSTGRAGIASEaqkyqakiLSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISKLGEnskkngypMDIR 386
Cdd:PRK07229 227 DERTREFLKAQGREDDWVE--------LLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAG--------IKVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 387 VGLIGSCTNSSYEDMGRCASIAKDamsHGLKSKIPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQwdrk 466
Cdd:PRK07229 291 QVLIGSCTNSSYEDLMRAASILKG---KKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM---- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 467 DVKKGDKNTIVTSYNRNFTGRNdANPATHCFVTSPELVTALSIAGRLDfNPLTDELTGadGKKFKLKAPfgdelpaKGFD 546
Cdd:PRK07229 364 GQAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRTLALEN--GEYPKLEEP-------EGFA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 547 PGQDTYTAPPPSGENVKVAVDPKSTRLQLLEPFDkwngqDLTDLTVLIKVKGKCTTDHISAAGP-WLKYRGHLDNISNNM 625
Cdd:PRK07229 433 VDDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 626 FIGAtnyennemnniknqrngswggVPDVARDYKANGiKWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHET 705
Cdd:PRK07229 508 FEGV---------------------DNTFPERAKEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKA 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17864292 706 NLKKQGLLPLTFANPADYDKIQPTSKISLLNLKSLAPGKPVDAEIKNGDkvERIKLNHTLNDLQIGWFKAGSALNRMKE 784
Cdd:PRK07229 566 NLINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD--EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
102-513 |
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: 842.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 102 RVAMQDATAQMALLQFISSGLKKVAVPSTVHCDHLIEAQIGGPKDLARAKDLNKEVYDFLASTCAKYGLGFWKPGSGIIH 181
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 182 QIILENYAFPGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADI 261
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 262 LTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLKSTGRAGIASEAQKYQAKILSADKNCE 341
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKDDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 342 YDELIEINLDTLEPHVNGPFTPDLGHPISKLGENSKKNGYPMDIRVGLIGSCTNSSYEDMGRCASIAKDAMSHGLKSKIP 421
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 422 FNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDRKDVKKGDKNTIVTSYNRNFTGRNDANPATHCFVTSP 501
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 17864292 502 ELVTALSIAGRL 513
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
57-782 |
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: 738.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 57 KRLEVVRGRLNRpLTLSEKVLYSHLD---DPAN---QDI---------VRGTSYLRLRPDRVAMQDATAQMALLQFISSG 121
Cdd:COG1048 24 PALEEAGGDISR-LPYSLKILLENLLrneDGETvteEDIkalanwlpkARGDDEIPFRPARVLMQDFTGVPAVVDLAAMR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 122 LKKV-----------AVPSTVHCDHLIEAQIGGP-----KDLARAKDLNKEVYDFLASTCAKY-GLGFWKPGSGIIHQII 184
Cdd:COG1048 103 DAVArlggdpkkinpLVPVDLVIDHSVQVDYFGTpdaleKNLELEFERNRERYQFLKWGQQAFdNFRVVPPGTGIVHQVN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 185 LENYAFP-------------GLLMIGTDSHTPNggglgglcigvggA-------------DAVDVMADIPWELKCPKVIG 238
Cdd:COG1048 183 LEYLAFVvwtreedgetvayPDTLVGTDSHTTM-------------InglgvlgwgvggiEAEAAMLGQPVSMLIPEVVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 239 VNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLKSTG 318
Cdd:COG1048 250 VKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 319 RAG--IASEAQKYQAKILSAD---KNCEYDELIEINLDTLEPHVNGPFTPDLGHPISKLGENSKK--------------- 378
Cdd:COG1048 330 RSEeqIELVEAYAKAQGLWRDpdaPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAalaapvgeeldkpvr 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 379 -----NGYPM---DIRVGLIGSCTNSSYEDMGRCASI-AKDAMSHGLKSK--IPFNVTPGSEQIRATIERDGISEVFDKF 447
Cdd:COG1048 410 vevdgEEFELghgAVVIAAITSCTNTSNPSVMIAAGLlAKKAVEKGLKVKpwVKTSLAPGSKVVTDYLERAGLLPYLEAL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 448 GGTVLANACGPCIGQWDR------KDVKKGD-KNTIVTSYNRNFTGRNDaNPATHCFVTSPELVTALSIAGRLDFNPLTD 520
Cdd:COG1048 490 GFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVVAYALAGTVDIDLTTD 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 521 EL-TGADGKKFKLKA--PFGDELPAKGFD--------------------------PGQDTYTAPPPSgenVKVAVDPKST 571
Cdd:COG1048 569 PLgTDKDGKPVYLKDiwPSGEEIPAAVFKavtpemfraryadvfdgderwqalevPAGELYDWDPDS---TYIRRPPFFE 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 572 RLQLL-EPFdkwngQDLTDLTVLIKVKGKCTTDHISAAGP-----------------------WLKYRGHLDNISNNMFI 627
Cdd:COG1048 646 GLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 628 GATnyENNEMNN------IKNQRNGSWGGVPDVARDYKANGIKWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFAR 701
Cdd:COG1048 721 NIR--IKNLLAPgteggyTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFER 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 702 IHETNLKKQGLLPLTFANPADYDK--IQPTSKISLLNLKS-LAPGKPVDAEIKNGD-KVERIKLNHTL-NDLQIGWFKAG 776
Cdd:COG1048 799 IHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADgSTEEFPVLHRIdTPVEVEYYRAG 878
|
....*.
gi 17864292 777 SALNRM 782
Cdd:COG1048 879 GILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
74-511 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 545.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 74 EKVLYSHLDDPANQDIVRgtsylrlRPDRVAMQDATAQMALLQFISSGLKK-----------VAVPSTVHCDHlieAQIG 142
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLY-------IPDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 143 GPKDLARAKDLNKEVYDFLASTCAKYGLGFWKPGSGIIHQIILEN-YAFPGLLMIGTDSHTPNggglgglcigvggA--- 218
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 219 ----------DAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMA 288
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 289 TICNMGAEIGATTSLFPFNQRMADYLKSTGR--AGIASEAQKYQA-KILSADKNCEYDELIEINLDTLEPHVNGPFTPDL 365
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRpeAPKGEAYDKAVAwKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 366 GHPISKLGENS------------------KKNGYPM---DIRVGLIGSCTNSSYEDMGRCASIAKDAMSHGLKSK--IPF 422
Cdd:pfam00330 298 AVPLSELVPDPfadavkrkaaeraleymgLGPGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVApgVKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 423 NVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDRKDvkkgDKNTIVTSYNRNFTGRNdaNPATHCFVTSPE 502
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
gi 17864292 503 LVTALSIAG 511
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
102-513 |
1.50e-138 |
|
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: 414.59 E-value: 1.50e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 102 RVAMQDATAQMALLQFISSGLK-KVAVPSTVHCDHLIEAQIggpkdlarAKDLNKEVYDFLASTCAKYGLGFWKPGSGII 180
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALgKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 181 HQIILENYAFPGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVAD 260
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 261 ILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLKSTGRAGIASEAQKYQAKILsADKNC 340
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELL-ADEGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 341 EYDELIEINLDTLEPHVNGPFTPDLGHPISKLGEnskkngypMDIRVGLIGSCTNSSYEDMGRCASIAKDamsHGLKSKI 420
Cdd:cd01351 232 EYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKG---AKVAPGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 421 PFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDRkdvKKGDKNTIVTSYNRNFTGRNDANPAtHCFVTS 500
Cdd:cd01351 301 RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLAS 376
|
410
....*....|...
gi 17864292 501 PELVTALSIAGRL 513
Cdd:cd01351 377 PELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
71-784 |
4.26e-115 |
|
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: 363.15 E-value: 4.26e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 71 TLSEKVLYSHLddpANQDIVRGTSyLRLRPDRVAMQDATAQMALLQFISSGLKKVAVPSTV-HCDHlieaqiggpkDLAR 149
Cdd:TIGR01342 1 TLAEKIIDDHL---VEGDLEPGEE-IAIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAqYCDH----------NMLQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 150 AKDLNKEVYDFLASTCAKYGLGFWKPGSGIIHQIILENYAFPGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMADIPW 229
Cdd:TIGR01342 67 FDFKNADDHKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 230 ELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQR 309
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 310 MADYLKSTGRAGIASEaqkyqakiLSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISKLGenskknGYPMDIRVgl 389
Cdd:TIGR01342 227 TEAWLAAFDREDDFVD--------LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIA------GIEVDQVM-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 390 IGSCTNSSYEDMGRCASIAKDAMSHglkSKIPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQwdrkDVK 469
Cdd:TIGR01342 291 IGSCTNGAFEDLLPAAKLLEGREVH---KDTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 470 KGDKNTIVTSYNRNFTGRNdANPATHCFVTSPELVTALSIAGRL-DFNPLTDELTgadgkkfKLKAPfGDELPAK---GF 545
Cdd:TIGR01342 364 PASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEIiDPRDLADDEG-------DLEAI-GFEMGEKfpgGY 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 546 DPGqDTYTAPPPSGENVKVAVDPKSTRLQLLEPFdkwnGQDLTDlTVLIKVKGKCTTDHISAAGP-WLKYRGHLDNISNN 624
Cdd:TIGR01342 435 DAA-DIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 625 MFigatNYENNEMnniknqrngswggVPDvARDYKANGIKWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHE 704
Cdd:TIGR01342 509 TL----HRIDDEF-------------AER-AKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHH 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 705 TNLKKQGLLPLTFANPADYDKIQPTSKISLLNLKSLAPGKPVDAEIKNGDKVERIKLNHTLNDLQIGWFKAGSALNRMKE 784
Cdd:TIGR01342 571 ANLFNFGILPLEFDNEEDYAKFELGDDIEIPDDLAAALADGEDEFTINKNDDEEALATLDASEREKEILAAGGKLNLIKN 650
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
595-743 |
1.25e-104 |
|
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: 317.49 E-value: 1.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 595 KVKGKCTTDHISAAGPWLKYRGHLDNISNNMFIGATNYENNEMNNIKNQRNGSWGGVPDVARDYKANGIKWVAVGDENYG 674
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17864292 675 EGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYDKIQPTSKISLLNLKSLAPG 743
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
101-513 |
1.83e-97 |
|
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: 307.84 E-value: 1.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 101 DRVAMQDATAQMALLQFISSGLKKVAVPSTV-HCDHLIEAQigGPKdlarakdlNKEVYDFLASTCAKYGLGFWKPGSGI 179
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVsYVDHNTLQT--DFE--------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 180 IHQIILENYAFPGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVA 259
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 260 DILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLKSTGRAGIASEaqkyqakiLSADKN 339
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVE--------LAADAD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 340 CEYDELIEINLDTLEPHVNGPFTPDLGHPISKLGenskknGYPMDiRVgLIGSCTNSSYEDMGRCASIAKDAMSHglkSK 419
Cdd:cd01585 223 AEYDEEIEIDLSELEPLIARPHSPDNVVPVREVA------GIKVD-QV-AIGSCTNSSYEDLMTVAAILKGRRVH---PH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 420 IPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDrkdvKKGDKNTIVTSYNRNFTGRNdANPATHCFVT 499
Cdd:cd01585 292 VSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLA 366
|
410
....*....|....
gi 17864292 500 SPELVTALSIAGRL 513
Cdd:cd01585 367 SPEVAAAAALTGVI 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
69-513 |
5.01e-75 |
|
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: 249.56 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 69 PLTLSEKVLYSHLDDPanqdiVRGTSYLRLRPDRVAMQDATAQMALLQFISSGLKKVAVPSTVH--CDHLIeaqiggPKD 146
Cdd:COG0065 2 GMTLAEKILARHAGRE-----VEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNV------PTK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 147 LARAKDLNKEVYDFlastCAKYGLGFWKPGS-GIIHQIILEN-YAFPGLLMIGTDSHTPNGGglgglcigvggA------ 218
Cdd:COG0065 71 DPKSAEQVKTLREF----AKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHG-----------Afgafaf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 219 -----DAVDVMA--DIpWeLKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATIC 291
Cdd:COG0065 136 gigttDVAHVLAtgTL-W-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 292 NMGAEIGATTSLFPFNQRMADYLKSTGRAgiaseaqkyQAKILSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISK 371
Cdd:COG0065 214 NMAIEAGAKAGIIAPDETTFEYLKGRPFA---------PWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 372 LGenskknGYPMDirVGLIGSCTNSSYEDMGRCASIAKDamsHGLKSKIPFNVTPGSEQIRATIERDGISEVFDKFGGTV 451
Cdd:COG0065 285 LE------GIKID--QVFIGSCTNGRIEDLRAAAEILKG---RKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17864292 452 LANACGPCIGQwdRKDVKKGDKNTIVTSyNRNFTGRNdANPATHCFVTSPELVTALSIAGRL 513
Cdd:COG0065 354 REPGCGMCLGM--NMGVLAPGERCASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
74-782 |
3.19e-70 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 247.92 E-value: 3.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 74 EKVLYSHLDDPANQDIvRGTSYLRL--RPDRVAMQDATAQMALLQFisSGLKKVA-------------VPSTVHCDHLIE 138
Cdd:PRK12881 56 KKVTEEHLEALANWLP-ERKSDDEIpfVPARVVMQDFTGVPALVDL--AAMRDAAaeaggdpakinplVPVDLVVDHSVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 139 AQIGGPKDlARAKDL------NKEVYDFLA-STCAKYGLGFWKPGSGIIHQIILE--------------NYAFPGLLmIG 197
Cdd:PRK12881 133 VDYFGQKD-ALDLNMkiefqrNAERYQFLKwGMQAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 198 TDSHTP--NGGGLGGLCIGVGGADAVdvMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYH 275
Cdd:PRK12881 211 TDSHTTmiNGIGVLGWGVGGIEAEAV--MLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 276 GKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLKSTGR--AGIASEAQKYQAKILSADKNCE--YDELIEINLD 351
Cdd:PRK12881 289 GEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRteAQIALVEAYAKAQGLWGDPKAEprYTRTLELDLS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 352 TLEPHVNGP---------------FTPDLGHPISKLGENSK---KNGYPM---DIRVGLIGSCTNSSyeD---MGRCASI 407
Cdd:PRK12881 369 TVAPSLAGPkrpqdrialgnvksaFSDLFSKPVAENGFAKKaqtSNGVDLpdgAVAIAAITSCTNTS--NpsvLIAAGLL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 408 AKDAMSHGLKSK--IPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWD------RKDVKKGD-KNTIVT 478
Cdd:PRK12881 447 AKKAVERGLTVKpwVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGpltpeiEQAITKNDlVAAAVL 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 479 SYNRNFTGRNDANpATHCFVTSPELVTALSIAGRLDFNPLTDEL-TGADGKKFKLKA--PFG---DELPAKGFDPGQ--- 549
Cdd:PRK12881 527 SGNRNFEGRIHPN-IKANFLASPPLVVAYALAGTVRRDLMTEPLgKGKDGRPVYLKDiwPSSaeiDALVAFAVDPEDfrk 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 550 --DTYTAPPPSGENVKVAV------DPKSTRLQllEP--FDKWNGQ-----DLTDLTVLIKVKGKCTTDHIS-------- 606
Cdd:PRK12881 606 nyAEVFKGSELWAAIEAPDgplydwDPKSTYIR--RPpfFDFSMGPaasiaTVKGARPLAVLGDSITTDHISpagaikad 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 607 -AAGPWLKYRG---------------HL---------DNISNNMFIGAtnyennEMNNIKNQRNGSWGGVPDVARDYKAN 661
Cdd:PRK12881 684 sPAGKYLKENGvpkadfnsygsrrgnHEvmmrgtfanVRIKNLMIPGK------EGGLTLHQPSGEVLSIYDAAMRYQAA 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 662 GIKWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFA---NPADYdKIQPTSKISLLNLK 738
Cdd:PRK12881 758 GTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKggdSRQSL-GLTGGETFDIEGLP 836
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 17864292 739 S-LAPGKPVDAEIKNGD-KVERIKLN---HTLNDLQIgwFKAGSALNRM 782
Cdd:PRK12881 837 GeIKPRQDVTLVIHRADgSTERVPVLcriDTPIEVDY--YKAGGILPYV 883
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
99-757 |
4.88e-67 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 238.87 E-value: 4.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 99 RPDRVAMQDATAQMAL--LqfisSGLKKVAV-----PSTVH--------CDHLIEAQIGGPKD-LARAKDL----NKEVY 158
Cdd:PRK09277 83 RPARVVMQDFTGVPAVvdL----AAMRDAIAdlggdPAKINplvpvdlvIDHSVQVDYFGTPDaFEKNVELeferNEERY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 159 DFLastcaKYGLGFWK------PGSGIIHQIILE-------------NYAFPGLLmIGTDSHTPnggglgglcigvggad 219
Cdd:PRK09277 159 QFL-----KWGQKAFDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT---------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 220 AVD----------------VMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSIS 283
Cdd:PRK09277 217 MINglgvlgwgvggieaeaAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 284 CTGMATICNMGAEIGATTSLFPFNQRMADYLKSTGRagiaSEAQ-----KYqAKI----LSADKNCEYDELIEINLDTLE 354
Cdd:PRK09277 297 LADRATIANMAPEYGATCGFFPIDEETLDYLRLTGR----DEEQvalveAY-AKAqglwRDPLEEPVYTDVLELDLSTVE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 355 PHVNGP-------FTPDLGHPISKLGENSKKNGYPMDIRVGL-------------IGSCTNSS--YEDMGrCASIAKDAM 412
Cdd:PRK09277 372 PSLAGPkrpqdriPLSDVKEAFAKSAELGVQGFGLDEAEEGEdyelpdgavviaaITSCTNTSnpSVMIA-AGLLAKKAV 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 413 SHGLKSKiPFNVT---PGSEQIRATIERDGISEVFDKFGGTVLANACGPCIG---------QwdrKDVKKGD-KNTIVTS 479
Cdd:PRK09277 451 EKGLKVK-PWVKTslaPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGnsgplppeiE---KAINDNDlVVTAVLS 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 480 YNRNFTGR----NDANpathcFVTSPELVTALSIAGRLDFNPLTDEL-TGADGKKFKLKA--PFGDE---LPAKGFDPGQ 549
Cdd:PRK09277 527 GNRNFEGRihplVKAN-----YLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEidaVVAKAVKPEM 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 550 --DTYtAP----PPSGENVKVAV------DPKSTRLQlLEPFdkWNG--------QDLTDLTVLIKVKGKCTTDHIS--- 606
Cdd:PRK09277 602 frKEY-ADvfegDERWNAIEVPEgplydwDPDSTYIR-NPPY--FEGmlaepgpvRDIKGARVLALLGDSITTDHISpag 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 607 ------AAGPWLK-----------Y-----------RGHLDNIsnnmfigatnyennemnNIKNQ-RNGSWGGV----P- 652
Cdd:PRK09277 678 aikadsPAGKYLLehgvepkdfnsYgsrrgnhevmmRGTFANI-----------------RIRNEmVPGVEGGYtrhfPe 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 653 -------DVARDYKANGIKWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYD- 724
Cdd:PRK09277 741 gevmsiyDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKt 820
|
810 820 830
....*....|....*....|....*....|....*.
gi 17864292 725 -KIQPTSKISLLNLKSLAPGKPVDAEI--KNGDKVE 757
Cdd:PRK09277 821 lGLDGTETFDIEGLEDLKPGATVTVVItrADGEVVE 856
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
69-513 |
1.80e-66 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 226.60 E-value: 1.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 69 PLTLSEKVLYSHLDDPanqdiVRGTSYLRLRPDRVAMQDATAQMALLQFISSGLKKVAVPSTVH--CDHLIEAqiggpKD 146
Cdd:PRK00402 2 GMTLAEKILARHSGRD-----VSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 147 LARAKDLnKEVYDFLAstcaKYGL-GFWKPGSGIIHQIILEN-YAFPGLLMIGTDSHTPNggglgglcigvggADAVDVM 224
Cdd:PRK00402 72 IKSAEQQ-KILREFAK----EQGIpNFFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALGAF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 225 A------DIP--------WeLKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATI 290
Cdd:PRK00402 134 AtgmgstDMAaamatgktW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 291 CNMGAEIGATTSLFPFNQRMADYLKstgragiasEAQKYQAKILSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPIS 370
Cdd:PRK00402 213 ANMAIEAGAKAGIFAPDEKTLEYLK---------ERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 371 KLGenskknGYPMDIRVglIGSCTNSSYEDMGRCASIAKDamsHGLKSKIPFNVTPGSEQIRATIERDGISEVFDKFGGT 450
Cdd:PRK00402 284 EVE------GTKVDQVF--IGSCTNGRLEDLRIAAEILKG---RKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAV 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17864292 451 VLANACGPCIGqwdrkdvkkG------DKNTIVTSYNRNFTGRNdANPATHCFVTSPELVTALSIAGRL 513
Cdd:PRK00402 353 VSTPTCGPCLG---------GhmgvlaPGEVCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTGKI 411
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
102-513 |
5.02e-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: 224.38 E-value: 5.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 102 RVAMQDATAQMALLQFISSGLKKVAVPSTVHC--DHLIEAqiggPKDLARakdlnkEVYDFLASTCAKYGLGFWKPG-SG 178
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT----PDIKAA------EQVKTLRKFAKEFGINFFDVGrQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 179 IIHQIILENYAF-PGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMA--DIpWeLKCPKVIGVNLTGKISGWTSPKDVI 255
Cdd:cd01583 71 ICHVILPEKGLTlPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtgKL-W-FRVPETMRVNVEGKLPPGVTAKDVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 256 LKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLKSTGRAgiaseaqkyQAKILS 335
Cdd:cd01583 149 LYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA---------YWKELK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 336 ADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISKLGenskknGYPMDIRVglIGSCTNSSYEDMGRCASIAKDamsHG 415
Cdd:cd01583 220 SDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVE------GIKIDQVF--IGSCTNGRLEDLRAAAEILKG---RK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 416 LKSKIPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDrkDVKKGDKNTIVTSyNRNFTGR-NDANPAT 494
Cdd:cd01583 289 VADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHM--GVLAPGERCVSTS-NRNFKGRmGSPGARI 365
|
410
....*....|....*....
gi 17864292 495 HcfVTSPELVTALSIAGRL 513
Cdd:cd01583 366 Y--LASPATAAASAITGEI 382
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
101-780 |
3.18e-62 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 225.28 E-value: 3.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 101 DRVAMQDATAQMALlqfissGLKKV--AVPSTVHCDHLIEAQIGGPKDlARAKDL------NKEVYDFLastcaKYGLGF 172
Cdd:PTZ00092 106 DLAAMRDAMKRLGG------DPAKInpLVPVDLVIDHSVQVDFSRSPD-ALELNQeieferNLERFEFL-----KWGSKA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 173 WK------PGSGIIHQIILENYA---FP--GLL----MIGTDSHTP--NGGGLGGLCIGVGGADAVdvMADIPWELKCPK 235
Cdd:PTZ00092 174 FKnllivpPGSGIVHQVNLEYLArvvFNkdGLLypdsVVGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVLPE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 236 VIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLK 315
Cdd:PTZ00092 252 VVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 316 STGRAgiaSEAQKYQAKILSA-------DKNCEYDELIEINLDTLEPHVNGP---------------FTPDLGHPISKLG 373
Cdd:PTZ00092 332 QTGRS---EEKVELIEKYLKAnglfrtyAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGFKG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 374 -----ENSKK------NGYPMDIRVG-----LIGSCTNSSYED-MGRCASIAKDAMSHGLKSK--IPFNVTPGSEQIRAT 434
Cdd:PTZ00092 409 fgipeEKHEKkvkftyKGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPpyIKTSLSPGSKVVTKY 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 435 IERDGISEVFDKFGGTVLANACGPCIGqwDRKDVKKGDKNTI---------VTSYNRNFTGRndANPATHC-FVTSPELV 504
Cdd:PTZ00092 489 LEASGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 505 TALSIAGRLDFN----PLTDELTG-----------------------------------ADGKKF--KLKAPFGDELPak 543
Cdd:PTZ00092 565 VAYALAGRVNIDfetePLGSDKTGkpvflrdiwpsreeiqaleakyvkpemfkevysniTQGNKQwnELQVPKGKLYE-- 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 544 gFDPgQDTYTAPPPSGENVKVAVDPKstrlqllepfdkwngQDLTDLTVLIKVKGKCTTDHISAAG------PWLKY--- 614
Cdd:PTZ00092 643 -WDE-KSTYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlme 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 615 ----------------------RGHLDNIS-NNMFIGATN-----YENNEMNNIKnqrngswggvpDVARDYKANGIKWV 666
Cdd:PTZ00092 706 rgverkdfntygarrgndevmvRGTFANIRlINKLCGKVGpntvhVPTGEKMSIY-----------DAAEKYKQEGVPLI 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 667 AVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFAN--PADYDKIQPTSKISL-LNLKSLAPG 743
Cdd:PTZ00092 775 VLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgeNADSLGLTGKEQFSIdLNSGELKPG 854
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 17864292 744 KPVDAEIKNG---DKVERIKlnhtlNDLQIGWFKAGSALN 780
Cdd:PTZ00092 855 QDVTVKTDTGktfDTILRID-----TEVEVEYFKHGGILQ 889
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
71-513 |
4.92e-60 |
|
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: 208.84 E-value: 4.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 71 TLSEKVLYSHlddpANQDIVRGTSyLRLRPDRVAMQDATAQMALLQFISSGLKKVAVPSTVHC--DHLIeaqiggPKDLA 148
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDL-IEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQV------PADTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 149 RAKDLNKEVYDFLASTCAKYglgFWKPGSGIIHQIILEN-YAFPGLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMADI 227
Cdd:TIGR01343 70 KAAEMQKLAREFVKKQGIKY---FYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 228 PWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFN 307
Cdd:TIGR01343 147 KTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 308 QRMADYLKstgragiasEAQKYQAKILSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISKLgenskkNGYPMDiRV 387
Cdd:TIGR01343 227 EKTIQYLK---------ERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 388 gLIGSCTNSSYEDMGRCASIAKdamSHGLKSKIPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGqwdRKD 467
Cdd:TIGR01343 291 -FIGSCTNGRLEDLRVAAKILK---GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 17864292 468 VKKGDKNTIVTSYNRNFTGRNdANPATHCFVTSPELVTALSIAGRL 513
Cdd:TIGR01343 364 GVLAPGEVCISTSNRNFKGRM-GHPNAEIYLASPATAAASAVKGYI 408
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
99-753 |
2.27e-57 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 211.59 E-value: 2.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 99 RPDRVAMQDATAQMAL--LQFISSGLKKVA---------VPSTVHCDHLIEAQIGGPKDLARAK-----DLNKEVYDFLa 162
Cdd:PLN00070 121 KPARVLLQDFTGVPAVvdLACMRDAMNNLGgdpnkinplVPVDLVIDHSVQVDVARSENAVQANmelefQRNKERFAFL- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 163 stcaKYGLGFWK------PGSGIIHQIILENYA-----FPGLL----MIGTDSHTPNGGGLGGLCIGVGGADAVDVMADI 227
Cdd:PLN00070 200 ----KWGSTAFQnmlvvpPGSGIVHQVNLEYLGrvvfnTDGILypdsVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 228 PWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFN 307
Cdd:PLN00070 276 PMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 308 QRMADYLKSTGRAG-IASEAQKY-QAKILSADKNCE-----YDELIEINLDTLEPHVNGPFTPDLGHPI----------- 369
Cdd:PLN00070 356 HVTLQYLKLTGRSDeTVAMIEAYlRANKMFVDYNEPqqervYSSYLELDLEDVEPCISGPKRPHDRVPLkemkadwhscl 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 370 -SKLG--------ENSKK------NGYPMDIRVG-----LIGSCTNSSYED-MGRCASIAKDAMSHGLKSK--IPFNVTP 426
Cdd:PLN00070 436 dNKVGfkgfavpkEAQSKvakfsfHGQPAELRHGsvviaAITSCTNTSNPSvMLGAGLVAKKACELGLEVKpwIKTSLAP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 427 GSEQIRATIERDGISEVFDKFGGTVLANACGPCI---GQWDRKDVKKGDKNTIVT----SYNRNFTGRndANPATHC-FV 498
Cdd:PLN00070 516 GSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIgnsGELDESVASAITENDIVAaavlSGNRNFEGR--VHPLTRAnYL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 499 TSPELVTALSIAGRLDFNPLTDEL-TGADGKKFKLKA--PFGDE---------LPakgfDPGQDTYTA-----------P 555
Cdd:PLN00070 594 ASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDVFFRDiwPSNEEvaevvqssvLP----DMFKSTYEAitkgnpmwnqlS 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 556 PPSGenVKVAVDPKSTRLQllEP-------FDKWNGQDLTDLTVLIKVKGKCTTDHISAAG------PWLKY---RGhLD 619
Cdd:PLN00070 670 VPSG--TLYSWDPKSTYIH--EPpyfknmtMSPPGPHGVKDAYCLLNFGDSITTDHISPAGsihkdsPAAKYlmeRG-VD 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 620 NISNNMFigATNYENNEM------NNIK--NQR-NGSWG------------GVPDVARDYKANGIKWVAVGDENYGEGSS 678
Cdd:PLN00070 745 RKDFNSY--GSRRGNDEImargtfANIRivNKLlKGEVGpktvhiptgeklSVFDAAMKYKSEGHDTIILAGAEYGSGSS 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 679 REHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYDKIQPTS----KISL-LNLKSLAPGKPVDAEIKNG 753
Cdd:PLN00070 823 RDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGheryTIDLpSNISEIKPGQDVTVTTDNG 902
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
592-720 |
4.77e-52 |
|
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: 177.17 E-value: 4.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 592 VLIKVKGKCTTDHISAAGPWLKYRGHLDNISNNMFIGATNYENNEMNNIKNQRNGSWGGVPDVARDYKANGIKWVAVGDE 671
Cdd:pfam00694 3 VFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIGGK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17864292 672 NYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANP 720
Cdd:pfam00694 83 NFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
102-512 |
4.70e-41 |
|
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: 155.54 E-value: 4.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 102 RVAMQDATAQMALLQFIS--SGLKKV---------AVPSTVHCDHLIEAQIGGPKDlARAKDL------NKEVYDFLast 164
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAmrDAVKRLggdpekinpLIPVDLVIDHSVQVDFYGTAD-ALAKNMkleferNRERYEFL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 165 caKYGLGFWK------PGSGIIHQIILE--------------NYAFPGLLmIGTDSHTPNGGGLGGLCIGVGGADAVDVM 224
Cdd:cd01586 77 --KWGQKAFKnlrvvpPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 225 ADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLF 304
Cdd:cd01586 154 LGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 305 PFNqrmadylkstgragiaseaqkyqakilsadknceyDELIEINLDTLEPHVNGPFTPDLGHPIsklgenskkNGypmD 384
Cdd:cd01586 234 PVD-----------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL---------HG---S 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 385 IRVGLIGSCTNSSYED-MGRCASIAKDAMSHGLKSK--IPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIG 461
Cdd:cd01586 267 VVIAAITSCTNTSNPSvMLAAGLLAKKAVELGLKVKpyVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIG 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17864292 462 ------QWDRKDVKKGD-KNTIVTSYNRNFTGRndANPATHC-FVTSPELVTALSIAGR 512
Cdd:cd01586 347 nsgplpEEVEEAIKENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
115-513 |
3.72e-32 |
|
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: 128.50 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 115 LQFISSGLKKVAVPSTVHC--DHlieaqiggpkDLARAKDLNKEVYDFLASTCAKYGLGFWKPGSGIIHQIILEN-YAFP 191
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH----------DVQNKSEKNLKKYKNIESFAKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 192 GLLMIGTDSHTPNGGGLGGLCIGVGGADAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAI 271
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 272 IEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRmadylkstgragiaseaqkyqakilsadknceydELIeINLD 351
Cdd:cd01582 163 IEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------------------HLI-LDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 352 TLEPHVNGPFTPDLGHPISKLgenSKKNgypMDIRVGLIGSCTNSSYEDMGRCASIAKDAMSHGLKSK----IPFNVTPG 427
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL---EAQN---IKINKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIPvapgVEFYVAAA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 428 SEQIRATIERDGISEVFDKFGGTVLANACGPCI--GQWDRKDVKKGdkntiVTSYNRNFTGRNdANPATHCFVTSPELVT 505
Cdd:cd01582 282 SSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIglGQGLLEPGEVG-----ISATNRNFKGRM-GSTEALAYLASPAVVA 355
|
....*...
gi 17864292 506 ALSIAGRL 513
Cdd:cd01582 356 ASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
161-513 |
2.06e-30 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 125.62 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 161 LASTCAKYGLGFWKPGS---GIIHQIILENYA-FPGLLMIGTDSHTpnggglgglcigvggadAV--------------- 221
Cdd:PRK05478 86 LEKNCKEFGITLFDLGDprqGIVHVVGPEQGLtLPGMTIVCGDSHT-----------------SThgafgalafgigtse 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 222 --DVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICNMGAEIGA 299
Cdd:PRK05478 149 veHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 300 TTSLFPFNQRMADYLKstGRA----GIASEAQKYQAKILSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISK---- 371
Cdd:PRK05478 229 RAGLVAPDETTFEYLK--GRPfapkGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGkvpd 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 372 ----LGENSKKN------------GYPM-DIRVG--LIGSCTNSSYEDMGRCASIAKDamshglkSKIPFNVT----PGS 428
Cdd:PRK05478 307 pedfADPVKRASaeralaymglkpGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVKG-------RKVAPGVRalvvPGS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 429 EQIRATIERDGISEVFDKFG------GtvlanaCGPCIGQWDrkDVKKGDKNTIVTSyNRNFTGRNDANPATHcfVTSPE 502
Cdd:PRK05478 380 GLVKAQAEAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPA 448
|
410
....*....|.
gi 17864292 503 LVTALSIAGRL 513
Cdd:PRK05478 449 MAAAAAITGHF 459
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
595-734 |
3.60e-30 |
|
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: 115.23 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 595 KVKGKCTTDHISAAGP-WLKYRGHLDNISNNMFIGATnyennemnniknqrngswggvPDVARDYKANGiKWVAVGDENY 673
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHRVD---------------------PTFAERAKAAG-PGFIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17864292 674 GEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYDKIQPTSKISL 734
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLEL 119
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
67-521 |
3.93e-29 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 121.94 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 67 NRPLTLSEKVLYSH----LDDpanqdivrGTSYLRLrpDRVAMQDATAQMALlqfisSGLK----KVAVPSTVHC--DHL 136
Cdd:PRK12466 1 MMPRTLYDKLWDSHtvarLDD--------GHVLLYI--DRHLLNEYTSPQAF-----SGLRargrTVRRPDLTLAvvDHV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 137 IEAQIGGpkDLARAKDLNKEVYDFLASTCAKYGL---GFWKPGSGIIHQIILE-NYAFPGLLMIGTDSHTPNGGGLGGLC 212
Cdd:PRK12466 66 VPTRPGR--DRGITDPGGALQVDYLRENCADFGIrlfDVDDPRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 213 IGVGGADAVDVMADIPWELKCPKVIGVNLTGKISGWTSPKDVILKVADILTVKGGTGAIIEYHGKGVDSISCTGMATICN 292
Cdd:PRK12466 144 FGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 293 MGAEIGATTSLFPFNQRMADYLKstGRAGIASEAQKYQA----KILSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHP 368
Cdd:PRK12466 224 MAVEAGARGGLIAPDETTFDYLR--GRPRAPKGALWDAAlaywRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 369 IS-------------KLGENSKKNGYpMDIRVG-----------LIGSCTNSSYEDMGRCASIAK--------DAMshgl 416
Cdd:PRK12466 302 ITgrvpdpaaeadpaRRAAMERALDY-MGLTPGtplagipidrvFIGSCTNGRIEDLRAAAAVLRgrkvapgvRAM---- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 417 kskipfnVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDRKdVKKGDKntIVTSYNRNFTGRNDANPATHc 496
Cdd:PRK12466 377 -------VVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV-LAPGER--CASTTNRNFEGRQGPGARTH- 445
|
490 500
....*....|....*....|....*.
gi 17864292 497 fVTSPELVTALSIAGRL-DFNPLTDE 521
Cdd:PRK12466 446 -LMSPAMVAAAAVAGHItDVRSLLQA 470
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
595-734 |
5.18e-25 |
|
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: 99.46 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 595 KVKGKCTTDHISAAGPWlkyrghldnisnnmfigatnyennemnniknqrngswggvpdvardykangikwVAVGDENYG 674
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 675 EGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYDKIQPTSKISL 734
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDI 86
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
96-725 |
4.87e-17 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 85.83 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 96 LRLRPDRVAMQDAT----AQMAllqfISSGLKKVAVPSTVHCDHLIEAQIGGpkdlarakDLNKEVYDFLASTCAKYGLG 171
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGG--------TINEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 172 FWKPGSGIIHQIILENYAFPGLLMIGTDSHTpnggglgglcigvgGADAVDVMA-------------DIPWELKCPKVIG 238
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgegggelvkqllNDTYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 239 VNLTGKISGWTSPKDVILkvADILTV-KGG--TGAIIEYHGKGVDSISCTGMATICNMGAEIGATTSLFPFNQRMADYLK 315
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVAL--AIIGAVfKNGyvKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 316 STGRAGIASEaqkyqakiLSADKNCEYDELIEINLDTLEPHVNGPFTPDLGHPISKLGEN----------------SKKN 379
Cdd:PRK11413 266 LHGRGQDYCE--------LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNltdilreveieservaHGKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 380 GYPM-------DIRV--GLIGSCTNSSYE------DMGRCASIAKDAMShglkskipFNVTPGSEQIRATIERDG-ISEV 443
Cdd:PRK11413 338 KLSLldkiengRLKVqqGIIAGCSGGNYEnviaaaNALRGQSCGNDTFS--------LSVYPSSQPVFMDLAKKGvVADL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 444 FDkfGGTVLANA-CGPCIGQwdrKDVKKGDKNTIVTSyNRNFTGRNDANPATHCfVTSPELVTALSIA------GRldfn 516
Cdd:PRK11413 410 MG--AGAIIRTAfCGPCFGA---GDTPANNGLSIRHT-TRNFPNREGSKPANGQ-MSAVALMDARSIAataangGY---- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 517 pltdeLTGADGkkfklkAPFGDELPAKGFDPG------QDTYTAPPPS-----GENVKvavdpkstrlqllepfdKWngQ 585
Cdd:PRK11413 479 -----LTSATE------LDCWDNVPEYAFDVTpyknrvYQGFGKGATQqpliyGPNIK-----------------DW--P 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 586 DLTDLT--VLIKVKGK-----CTTDHISAAGPWLKYRghldniSNNM-------------FIGAT--------NYENNEM 637
Cdd:PRK11413 529 EMGALTdnILLKVCSKildpvTTTDELIPSGETSSYR------SNPLglaeftlsrrdpgYVGRSkavaelenQRLAGNV 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 638 NNIKN--QRNGSWGGVPDVArdykangIKWVAVGDENY----GEGSSREHAALEPRHLGGRAIIVKSFA-RIHETNLKKQ 710
Cdd:PRK11413 603 SELTEvfARIKQIAGQEHID-------PLQTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINW 675
|
730
....*....|....*
gi 17864292 711 GLLPLTFANPADYDK 725
Cdd:PRK11413 676 GMLPFQMAEEPTFEV 690
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
601-735 |
2.48e-16 |
|
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: 77.32 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 601 TTDHISAAG------PWLKY-------------------------RGHLDNISN-NMFIGATnyennEMNNIKNQRNGSW 648
Cdd:cd01580 7 TTDHISPAGsiakdsPAGKYlaergvkprdfnsygsrrgndevmmRGTFANIRLrNKLVPGT-----EGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 649 GGVPDVARDYKANGIKWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANP--ADYDKI 726
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161
|
....*....
gi 17864292 727 QPTSKISLL 735
Cdd:cd01580 162 TGEETYDII 170
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
90-513 |
1.64e-13 |
|
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: 73.30 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 90 VRGTSYLRLRPDRVAMQDATAQM--------ALLQFISSGlkkvAVPSTVHCdhlieAQIGGPKDLArakdLNKEVYDFL 161
Cdd:cd01581 15 VRPGTYCEPKMTTVGSQDTTGPMtrdelkelACLGFSADL----VMQSFCHT-----AAYPKPVDVK----THRTLPDFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 162 AStcakYGLGFWKPGSGIIHQIiLENYAFPGLLMIGTDSHT--PNGGGLGGLCIGVGGADAVDVMAdipweLKCPKVIGV 239
Cdd:cd01581 82 SN----RGGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFAAATGVMP-----LDMPESVLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 240 NLTGKISGWTSPKDVILKV------ADILTV--KGG----TGAIIEYHGkgVDSISCTGMATICNMGAEIGATTSLFPFN 307
Cdd:cd01581 152 RFKGKMQPGITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 308 QR-MADYLKS------------------TGRAGIASEAQKYQAKILSADKNCEYDELIEINLDTL-EPHVNGPFTPDlgh 367
Cdd:cd01581 230 KEpVIEYLESnvvlmkimiangyddartLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIkEPILACPNDPD--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 368 PISKLGENSKKNgypmdIRVGLIGSC-TNssyedMGRCASIAKdaMSHGLKSKIP-FNVTPGSEQIRATIERDGISEVFD 445
Cdd:cd01581 307 DVKLLSEVAGKK-----IDEVFIGSCmTN-----IGHFRAAAK--ILRGKEFKPTrLWVAPPTRMDWAILQEEGYYSIFG 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 446 KFGGTVLANACGPCIGQWDRkdVKKGDknTIVTSYNRNFTGR--NDANpathCFVTSPELVTALSIAGRL 513
Cdd:cd01581 375 DAGARTEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
668-727 |
3.34e-11 |
|
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: 60.29 E-value: 3.34e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 668 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYDKIQ 727
Cdd:cd01577 22 VAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEA 81
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
334-513 |
5.59e-11 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 66.35 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 334 LSADKNCEYDELIEINLDTL-EPHVNGPFTPDLGHPISKLGENSkkngypmdIRVGLIGSC-TNssyedMGRCASIAKDA 411
Cdd:PRK09238 647 LEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLSEVAGTK--------IDEVFIGSCmTN-----IGHFRAAGKLL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 412 MSHGLKSKIPFNVTPGSEQIRATIERDGISEVFDKFGGTVLANACGPCIGQWDRkdVKKGDknTIVTSYNRNFTGR--ND 489
Cdd:PRK09238 714 EGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKG 789
|
170 180
....*....|....*....|....
gi 17864292 490 ANpathCFVTSPELVTALSIAGRL 513
Cdd:PRK09238 790 AN----VYLGSAELAAVCALLGRI 809
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
668-727 |
1.62e-10 |
|
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: 60.96 E-value: 1.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 668 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTfANPADYDKIQ 727
Cdd:COG0066 69 VAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALF 127
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
652-734 |
2.83e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 56.74 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 652 PDVARDYKANGIkwvAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPltFANPADYDKIQPTSK 731
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDE 115
|
...
gi 17864292 732 ISL 734
Cdd:PRK14023 116 VEL 118
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
668-762 |
3.70e-09 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 56.37 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 668 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFanPADYDKIQPTSKISllnlkslapgkpVD 747
Cdd:PRK00439 53 VAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLEC--DEAVDKIEDGDEVE------------VD 118
|
90
....*....|....*...
gi 17864292 748 AE---IKNGDKVERIKLN 762
Cdd:PRK00439 119 LEtgvITNLTTGEEYKFK 136
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
666-724 |
6.96e-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: 52.42 E-value: 6.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17864292 666 VAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTFANPADYD 724
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIEAKTEGIKD 108
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
174-521 |
1.22e-07 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 55.31 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 174 KPGSGIIHQIiLENYAFPGLLMIGTDSHT--PNGGGLGGLCIGVGGADAVDVMAdipweLKCPKVIGVNLTGKISGWTSP 251
Cdd:PLN00094 536 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFGAATGVIP-----LDMPESVLVRFTGTMQPGITL 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 252 KDVILKV------ADILTV-KGG-----TGAIIEYhgKGVDSISCTGMATICNMGAEIGATTSLFPFNQR-MADYLKST- 317
Cdd:PLN00094 610 RDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDKEpIIEYLNSNv 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 318 -----------------GRAGIASEAQKYQAKILSADKNCEYDELIEINLDTL-EPHVNGPFTPDLGHPISKLGENSkkn 379
Cdd:PLN00094 688 vmlkwmiaegygdrrtlERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGDK--- 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 380 gypmdIRVGLIGSC-TNssyedMGRCASIAKdaMSHGLKSKIPFN--VTPGSEQIRATIERDGISEVFDKFGGTVLANAC 456
Cdd:PLN00094 765 -----IDEVFIGSCmTN-----IGHFRAAGK--LLNDNLSQLPTRlwVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGC 832
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864292 457 GPCIGQWDRkdvkKGDKNTIVTSYNRNFTGRndANPATHCFVTSPELVTALSIAGRLdfnPLTDE 521
Cdd:PLN00094 833 SLCMGNQAR----VAEKSTVVSTSTRNFPNR--LGKGANVYLASAELAAVAAILGRL---PTVEE 888
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
668-727 |
4.91e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 50.90 E-value: 4.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17864292 668 VGDENYGEGSSREHA--ALEprHLGGRAIIVKSFARIHETNLKKQGLLPLTfANPADYDKIQ 727
Cdd:PRK01641 72 LAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELF 130
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
666-702 |
3.23e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 43.31 E-value: 3.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 17864292 666 VAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARI 702
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
676-770 |
2.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 38.55 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864292 676 GSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGLLPLTfaNPAD----YDKIQPTSKIS--LLNLKSLAPGKPVDAE 749
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIV--QPREvrekLAQLKPTDQVTvdLEQQKIISPVEEFTFE 80
|
90 100
....*....|....*....|.
gi 17864292 750 IkngDKVERIKLNHTLNDLQI 770
Cdd:PRK14812 81 I---DSEWKHKLLNSLDDIGI 98
|
|
| |
