|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
41-772 |
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: 1285.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 41 YKQNVETLDIVRKRLN-RPFTYAEKILYGHLDDPHG----QDIQ--RGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQ 113
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 114 VAKPVTVHCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPN 193
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 194 AGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSA 273
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 274 TGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAK--LYHKDLLSADKDAEYDEVVEIDLNTLEPYINGPFT 351
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKtgQYSFFKLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 352 PDLATPVSKMKEVAVANNWPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTIFTVTPGSEQIRATIERDGQLE 431
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 432 TFKEFGGIVLANACGPCIGQWDRRD-IKKGDKNTIVSSYNRNFTSRNDGNPQTHAFVASPELVTAFAIAGDLRFNPLTDK 510
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 511 LKDKDGNEFMLKPPHGDGLPQRGYDAGENTYQAPPAD-RSTVEVKVSPTSDRLQLLKPFKPWDGKDAKDMPILIKAVGKT 589
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSpNPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 590 TTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNVyTGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSSRE 669
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDL-DGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 670 HAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDILGLAELAP---GKPVTMRVHPKNGKP 746
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 6323335 747 WDAVLTHTFNDEQIEWFKYGSALNKI 772
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
57-778 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 952.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 57 RPFTYAEKILYGHLDDPhgqDIQRGVSyLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTV-HCDHliqaqvggekD 135
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 136 LKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAG 215
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 216 RPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 295
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 296 NKSMIEYLEATGRGkiADFAKLYhkdllsADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVAnnwpldvr 375
Cdd:PRK07229 227 DERTREFLKAQGRE--DDWVELL------ADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVD-------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 376 VGLIGSCTNSSYEDMSRSASIVKDaaaHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQwdrr 455
Cdd:PRK07229 291 QVLIGSCTNSSYEDLMRAASILKG---KKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM---- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 456 DIKKGDKNTIVSSYNRNFTSRNdGNPQTHAFVASPELVTAFAIAGDLRfNPLTdkLKDKDGNEFMLKPPHgdglpqrGYD 535
Cdd:PRK07229 364 GQAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 536 AGENTYQAPPADRSTVEVKVSPTSDRLQLLKPFkpwdgKDAKDMPILIKAVGKTTTDHISMAGP-WLKYRGHLENISNNY 614
Cdd:PRK07229 433 VDDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPL-----PDLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 615 MIGAINAENKKAncvknvytgeykgvpdtardyRDQGiKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHET 694
Cdd:PRK07229 508 FEGVDNTFPERA---------------------KEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKA 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 695 NLKKQGLLPLNFKNPADYDKINPDDRIDILGLAELAPGKPVTMRVHPKNgkpWDAVLTHTFNDEQIEWFKYGSALNKIKA 774
Cdd:PRK07229 566 NLINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
....
gi 6323335 775 DEKK 778
Cdd:PRK07229 643 KLAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
91-502 |
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: 860.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 91 RVACQDATAQMAILQFMSAGLPQVAKPVTVHCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIH 170
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 171 QIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGI 250
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 251 TTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAKLYHKDLLSADKDAE 330
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKDDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 331 YDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVANNWPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTI 410
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 411 FTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDRRDIKKGDKNTIVSSYNRNFTSRNDGNPQTHAFVASP 490
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 6323335 491 ELVTAFAIAGDL 502
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
60-778 |
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: 805.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 60 TYAEKILYGHLD---DPHG---QDIQ---------RGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAK-------- 116
Cdd:COG1048 37 PYSLKILLENLLrneDGETvteEDIKalanwlpkaRGDDEIPFRPARVLMQDFTGVPAVVDLAAMRDAVARLggdpkkin 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 117 ---PVTVHCDHLIQAQVGG-----EKDLKRAIDLNKEVYDFLASATAKY-NMGFWKPGSGIIHQIVLENYAFP------- 180
Cdd:COG1048 117 plvPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVVPPGTGIVHQVNLEYLAFVvwtreed 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 181 GALI------IGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVK 254
Cdd:COG1048 197 GETVaypdtlVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 255 GGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGK-----IADFAK---LYHKDllsAD 326
Cdd:COG1048 277 GVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEeqielVEAYAKaqgLWRDP---DA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 327 KDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVANNWPL-----------------------DVRVGLIGSCT 383
Cdd:COG1048 354 PEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCT 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 384 NSSYEDMSRSASIV-KDAAAHGLKSKT--IFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDR------ 454
Cdd:COG1048 434 NTSNPSVMIAAGLLaKKAVEKGLKVKPwvKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeis 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 455 RDIKKGD-KNTIVSSYNRNFTSRNdGNPQTHAFVASPELVTAFAIAGDLRFNPLTDKL-KDKDGNEFMLKP--PHGDGLP 530
Cdd:COG1048 514 EAIEENDlVVAAVLSGNRNFEGRI-HPDVKANFLASPPLVVAYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIP 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 531 ------------QRGYD---AGENTYQAPPA--------DRSTVEVKVSPTSDRLQLL-KPFkpwdgKDAKDMPILIKAV 586
Cdd:COG1048 593 aavfkavtpemfRARYAdvfDGDERWQALEVpagelydwDPDSTYIRRPPFFEGLQLEpEPF-----KDIKGARVLAKLG 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 587 GKTTTDHISMAGP-----------------------WLKYRGHLENISNNYMIGA--IN--AENKKANCVKNVYTGEYKG 639
Cdd:COG1048 668 DSITTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFANIriKNllAPGTEGGYTKHQPTGEVMS 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 640 VPDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDK--INP 717
Cdd:COG1048 748 IYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTG 827
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323335 718 DDRIDILGLAE-LAPGKPVTMRVHPKNGKPWDAVLTHTF-NDEQIEWFKYGSALNKIKADEKK 778
Cdd:COG1048 828 DETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHRIdTPVEVEYYRAGGILQYVLRQLLA 890
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
63-500 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 603.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 63 EKILYGHLDDPHGQDIqrgvSYLklrPDRVACQDATAQMAILQFMSAGLP------QVAK-----PVTVHCDHliqAQVG 131
Cdd:pfam00330 1 EKIWDAHLVEELDGSL----LYI---PDRVLMHDVTSPQAFVDLRAAGRAvrrpggTPATidhlvPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 132 GEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAV 210
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 211 DVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATT 290
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 291 SVFPFNKSMIEYLEATGRG---KIADFAKLYHKDLLSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVA 367
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRPeapKGEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 368 ------------------NNWPL---DVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTI--FTVTPGSEQIRATI 424
Cdd:pfam00330 311 davkrkaaeraleymglgPGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPGvkASVVPGSEVVRAYA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323335 425 ERDGQLETFKEFGGIVLANACGPCIGQWDRrdIKKGDknTIVSSYNRNFTSRNdgNPQTHAFVASPELVTAFAIAG 500
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNSDR--LPPGE--RCVSSSNRNFEGRQ--GPGGRTHLASPALVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
91-502 |
1.08e-145 |
|
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: 432.69 E-value: 1.08e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 91 RVACQDATAQMAILQF-MSAGLPQVAKPVTVHCDHLIQAQVGGEKdlkraidlNKEVYDFLASATAKYNMGFWKPGSGII 169
Cdd:cd01351 1 RVMLQDATGPMAMKAFeILAALGKVADPSQIACVHDHAVQLEKPV--------NNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 170 HQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAG 249
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 250 ITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAKLYhKDLLSADKDA 329
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAF-PEELLADEGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 330 EYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEvavannwpLDVRVGLIGSCTNSSYEDMSRSASIVKDaaaHGLKSKT 409
Cdd:cd01351 232 EYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKG---AKVAPGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 410 IFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDRrdiKKGDKNTIVSSYNRNFTSRNdGNPQTHAFVAS 489
Cdd:cd01351 301 RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRL-GTYERHVYLAS 376
|
410
....*....|...
gi 6323335 490 PELVTAFAIAGDL 502
Cdd:cd01351 377 PELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
60-778 |
3.44e-142 |
|
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: 433.26 E-value: 3.44e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 60 TYAEKILYGHLDDphgQDIQRGvSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTV-HCDHLIQaqvggEKDLKR 138
Cdd:TIGR01342 1 TLAEKIIDDHLVE---GDLEPG-EEIAIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAqYCDHNML-----QFDFKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 139 AIDlnkevYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPW 218
Cdd:TIGR01342 72 ADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 219 ELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKS 298
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 299 MIEYLEATGRGKiaDFAKLyhkdllSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVskmKEVAvannwPLDVRVGL 378
Cdd:TIGR01342 227 TEAWLAAFDRED--DFVDL------LADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPV---REIA-----GIEVDQVM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 379 IGSCTNSSYEDMSRSASIVKDAAAHglkSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQwdrrDIK 458
Cdd:TIGR01342 291 IGSCTNGAFEDLLPAAKLLEGREVH---KDTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 459 KGDKNTIVSSYNRNFTSRNdGNPQTHAFVASPELVTAFAIAGDLrFNPltDKLKDKDGNEFMLKPPHGDGLPQrGYDAGE 538
Cdd:TIGR01342 364 PASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDP--RDLADDEGDLEAIGFEMGEKFPG-GYDAAD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 539 nTYQAPPADRSTVEVKVSPTSDRLQLLKPFkpwdGKDAKDmPILIKAVGKTTTDHISMAGP-WLKYRGHLENISnNYMIG 617
Cdd:TIGR01342 439 -IDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAIS-EFTLH 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 618 AINAEnkkancvknvytgeykgVPDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLK 697
Cdd:TIGR01342 512 RIDDE-----------------FAERAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHANLF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 698 KQGLLPLNFKNPADYDKINPDDRIDILG--LAELAPGKPV-TMRVHPKngkpWDAVLTHTFNDEQIEWFKYGSALNKIKA 774
Cdd:TIGR01342 575 NFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEfTINKNDD----EEALATLDASEREKEILAAGGKLNLIKN 650
|
....
gi 6323335 775 DEKK 778
Cdd:TIGR01342 651 KHRE 654
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-502 |
1.62e-121 |
|
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: 369.86 E-value: 1.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 90 DRVACQDATAQMAILQFMSAGLPQVAKPVTV-HCDH-LIQAqvggekDLKRAIDlnkevYDFLASATAKYNMGFWKPGSG 167
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVsYVDHnTLQT------DFENADD-----HRFLQTVAARYGIYFSRPGNG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 168 IIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKL 247
Cdd:cd01585 70 ICHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 248 AGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGkiADFAKlyhkdlLSADK 327
Cdd:cd01585 150 LRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRE--DDWVE------LAADA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 328 DAEYDEVVEIDLNTLEPYINGPFTPDLATPVskmKEVAvannwPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHglkS 407
Cdd:cd01585 222 DAEYDEEIEIDLSELEPLIARPHSPDNVVPV---REVA-----GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVH---P 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 408 KTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDrrdiKKGDKNTIVSSYNRNFTSRNdGNPQTHAFV 487
Cdd:cd01585 291 HVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYL 365
|
410
....*....|....*
gi 6323335 488 ASPELVTAFAIAGDL 502
Cdd:cd01585 366 ASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
584-732 |
3.10e-103 |
|
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: 313.64 E-value: 3.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 584 KAVGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNVYTGEYKGVPDTARDYRDQGIKWVVIGDENFG 663
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323335 664 EGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDILGLAELAPG 732
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
88-744 |
4.26e-95 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 316.10 E-value: 4.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 88 RPDRVACQDATAQMAI--LQFMSAGL------PQVAK---PVTVHCDHLIQAQVGGEKD-----LKRAIDLNKEVYDFLA 151
Cdd:PRK12881 82 VPARVVMQDFTGVPALvdLAAMRDAAaeaggdPAKINplvPVDLVVDHSVAVDYFGQKDaldlnMKIEFQRNAERYQFLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 152 SAT-AKYNMGFWKPGSGIIHQIVLE--------------NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMAGR 216
Cdd:PRK12881 162 WGMqAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTLV-GTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 217 PWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFN 296
Cdd:PRK12881 241 PVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 297 KSMIEYLEATGRGK--IADFAKlYHKDL-LSADKDAE--YDEVVEIDLNTLEPYINGPFTP-------DLATPVSKMKEV 364
Cdd:PRK12881 321 EQTLDYLRLTGRTEaqIALVEA-YAKAQgLWGDPKAEprYTRTLELDLSTVAPSLAGPKRPqdrialgNVKSAFSDLFSK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 365 AVANNWPL--------------DVRVGLIGSCTNSSYEDMSRSASIV-KDAAAHGLKS----KTifTVTPGSEQIRATIE 425
Cdd:PRK12881 400 PVAENGFAkkaqtsngvdlpdgAVAIAAITSCTNTSNPSVLIAAGLLaKKAVERGLTVkpwvKT--SLAPGSKVVTEYLE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 426 RDGQLETFKEFG-GIVlANACGPCIGQWD------RRDIKKGD-KNTIVSSYNRNFTSRNDGNPQThAFVASPELVTAFA 497
Cdd:PRK12881 478 RAGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRIHPNIKA-NFLASPPLVVAYA 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 498 IAGDLRFNPLTDKL-KDKDGNEFMLKP--PHG---DGLPQRGYDA---GENTYQAPPADRSTVEVKVsPTSDRLqllkpf 568
Cdd:PRK12881 556 LAGTVRRDLMTEPLgKGKDGRPVYLKDiwPSSaeiDALVAFAVDPedfRKNYAEVFKGSELWAAIEA-PDGPLY------ 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 569 kPWDGK---------------------DAKDMPILIKAVGKTTTDHIS---------MAGPWLKYRGHLENISNNY---- 614
Cdd:PRK12881 629 -DWDPKstyirrppffdfsmgpaasiaTVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNSYgsrr 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 615 -----MIGAINAeNKKancVKN-------------VYTGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPR 676
Cdd:PRK12881 708 gnhevMMRGTFA-NVR---IKNlmipgkeggltlhQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTR 783
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323335 677 FLGGFAIITKSFARIHETNLKKQGLLPLNFK---NPADYdKINPDDRIDILGL-AELAPGKPVTMRVHPKNG 744
Cdd:PRK12881 784 LLGVKAVIAESFERIHRSNLVGMGVLPLQFKggdSRQSL-GLTGGETFDIEGLpGEIKPRQDVTLVIHRADG 854
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
88-745 |
5.12e-93 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 310.52 E-value: 5.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 88 RPDRVACQDATAQMAI--LqfmsAGL---------------PQVakPVTVHCDHLIQAQVGGEKD-LKRAIDL----NKE 145
Cdd:PRK09277 83 RPARVVMQDFTGVPAVvdL----AAMrdaiadlggdpakinPLV--PVDLVIDHSVQVDYFGTPDaFEKNVELeferNEE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 146 VYDFLASA-TAKYNMGFWKPGSGIIHQIVLE-------------NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVD 211
Cdd:PRK09277 157 RYQFLKWGqKAFDNFRVVPPGTGICHQVNLEylapvvwtredgeLVAYPDTLV-GTDSHTTMINGLGVLGWGVGGIEAEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 212 VMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKlagITTV---KGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGA 288
Cdd:PRK09277 236 AMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLT---VTEMlrkKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 289 TTSVFPFNKSMIEYLEATGRGK--IA---DFAK---LYHkdllSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSK 360
Cdd:PRK09277 313 TCGFFPIDEETLDYLRLTGRDEeqVAlveAYAKaqgLWR----DPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSD 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 361 MKEvAVANNWPLDVRVGL---------------------IGSCTNSSYEDMSRSASIV-KDAAAHGLKS----KTIFtvT 414
Cdd:PRK09277 389 VKE-AFAKSAELGVQGFGldeaeegedyelpdgavviaaITSCTNTSNPSVMIAAGLLaKKAVEKGLKVkpwvKTSL--A 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 415 PGSEQIRATIERDGQLETFKEFG-GIVlANACGPCIG---------QwdrRDIKKGD-KNTIVSSYNRNFtsrnDG--NP 481
Cdd:PRK09277 466 PGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAINDNDlVVTAVLSGNRNF----EGriHP 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 482 QTHA-FVASPELVTAFAIAGDLRFNPLTDKL-KDKDGNEFMLKpphgDGLP------------------QRGYdagENTY 541
Cdd:PRK09277 538 LVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLK----DIWPsdeeidavvakavkpemfRKEY---ADVF 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 542 QAPPADRStVEVKVSPT------SDRLQlLKPFkpWDG--------KDAKDMPILIKAVGKTTTDHISMAGP-------- 599
Cdd:PRK09277 611 EGDERWNA-IEVPEGPLydwdpdSTYIR-NPPY--FEGmlaepgpvRDIKGARVLALLGDSITTDHISPAGAikadspag 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 600 -WLKYRGHLENISNNY---------MIGA----INAENKKANCVKNVYT-----GEYKGVPDTARDYRDQGIKWVVIGDE 660
Cdd:PRK09277 687 kYLLEHGVEPKDFNSYgsrrgnhevMMRGtfanIRIRNEMVPGVEGGYTrhfpeGEVMSIYDAAMKYKEEGTPLVVIAGK 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 661 NFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYD--KINPDDRIDILGLAELAPGKPVTMR 738
Cdd:PRK09277 767 EYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGATVTVV 846
|
....*..
gi 6323335 739 VHPKNGK 745
Cdd:PRK09277 847 ITRADGE 853
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
58-500 |
5.27e-92 |
|
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: 294.25 E-value: 5.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 58 PFTYAEKILYGHLddphGQDIQRGvSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKP--VTVHCDHLIQAqvggeKD 135
Cdd:COG0065 2 GMTLAEKILARHA----GREVEPG-EIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPdrIVAVFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 136 LKRAidlnkEVYDFLASATAKYNMGFWKPGS-GIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVM 213
Cdd:COG0065 72 PKSA-----EQVKTLREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 214 A-GRPWeLKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSV 292
Cdd:COG0065 147 AtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 293 FPFNKSMIEYLEatGRGKiADFAKLYhkdllsADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVannwpl 372
Cdd:COG0065 226 IAPDETTFEYLK--GRPF-APWRTLK------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKI------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 373 DvrVGLIGSCTNSSYEDMSRSASIVKDaaaHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIG-Q 451
Cdd:COG0065 291 D--QVFIGSCTNGRIEDLRAAAEILKG---RKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmN 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 6323335 452 WDRrdIKKGDknTIVSSYNRNFTSRNdGNPQTHAFVASPELVTAFAIAG 500
Cdd:COG0065 366 MGV--LAPGE--RCASTSNRNFEGRM-GSPGSRTYLASPATAAASAIAG 409
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
60-500 |
9.78e-86 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 277.83 E-value: 9.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 60 TYAEKILYGHLDDPH--GQDIQRGVsylklrpDRVACQDATAQMAILQFMSAGLPQVAKP--VTVHCDHLIQAqvggeKD 135
Cdd:PRK00402 4 TLAEKILARHSGRDVspGDIVEAKV-------DLVMAHDITGPLAIKEFEKIGGDKVFDPskIVIVFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 136 LKRAiDLNKEVYDFLASATAKYnmgFWKPGSGIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMA 214
Cdd:PRK00402 72 IKSA-EQQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 215 -GRPWeLKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVF 293
Cdd:PRK00402 148 tGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 294 PFNKSMIEYLEATGRgkiADFAKLYhkdllsADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVannwplD 373
Cdd:PRK00402 227 APDEKTLEYLKERAG---RDYKPWK------SDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKV------D 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 374 VRVglIGSCTNSSYEDMSRSASIVKDaaaHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGqwd 453
Cdd:PRK00402 292 QVF--IGSCTNGRLEDLRIAAEILKG---RKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLG--- 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 6323335 454 rrdikkG------DKNTIVSSYNRNFTSRNdGNPQTHAFVASPELVTAFAIAG 500
Cdd:PRK00402 364 ------GhmgvlaPGEVCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
91-500 |
1.69e-84 |
|
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: 273.30 E-value: 1.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 91 RVACQDATAQMAILQFMSAGLPQVAKPVTVHC--DHLIQAqvggeKDLKRAIDLNKEVYDFLASATAKYNMGfwkpGSGI 168
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT-----PDIKAAEQVKTLRKFAKEFGINFFDVG----RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 169 IHQIVLENYAF-PGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMA-GRPWeLKAPKILGVKLTGKMNGWTSPKDIILK 246
Cdd:cd01583 72 CHVILPEKGLTlPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVILY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 247 LAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEatGRGKiADFAKLYhkdllsAD 326
Cdd:cd01583 151 IIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLK--GRGK-AYWKELK------SD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 327 KDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVavannwPLDVRVglIGSCTNSSYEDMSRSASIVKDaaaHGLK 406
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI------KIDQVF--IGSCTNGRLEDLRAAAEILKG---RKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 407 SKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGqwdRRDIKKGDKNTIVSSYNRNFTSRNdGNPQTHAF 486
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLG---GHMGVLAPGERCVSTSNRNFKGRM-GSPGARIY 366
|
410
....*....|....
gi 6323335 487 VASPELVTAFAIAG 500
Cdd:cd01583 367 LASPATAAASAITG 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
89-770 |
8.32e-82 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 279.97 E-value: 8.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 89 PDRVACQDATAQMAILQF--------MSAGLPQVAKP---VTVHCDHLIQAQVGG-----EKDLKRAIDLNKEVYDFLA- 151
Cdd:PTZ00092 90 PARVLLQDFTGVPAVVDLaamrdamkRLGGDPAKINPlvpVDLVIDHSVQVDFSRspdalELNQEIEFERNLERFEFLKw 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 152 SATAKYNMGFWKPGSGIIHQIVLE----------NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELK 221
Cdd:PTZ00092 170 GSKAFKNLLIVPPGSGIVHQVNLEylarvvfnkdGLLYPDSVV-GTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 222 APKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIE 301
Cdd:PTZ00092 249 LPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 302 YLEATGRG--KIADFAKLYHKDLL--SADKDAEYDEVVEIDLNTLEPYINGP---------------FTPDLATPVS--- 359
Cdd:PTZ00092 329 YLKQTGRSeeKVELIEKYLKANGLfrTYAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGfkg 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 360 ----------KMKEVAVANNWPLD---VRVGLIGSCTNSSYED-MSRSASIVKDAAAHGLKS----KTifTVTPGSEQIR 421
Cdd:PTZ00092 409 fgipeekhekKVKFTYKGKEYTLThgsVVIAAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVppyiKT--SLSPGSKVVT 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 422 ATIERDGQLETFKEFGGIVLANACGPCIGQWDRRD------IKkgDKNTIVS---SYNRNFTSRNdgNPQTHA-FVASPE 491
Cdd:PTZ00092 487 KYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDpevseaIT--NNDLVAAavlSGNRNFEGRV--HPLTRAnYLASPP 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 492 LVTAFAIAGDLRFNPLTDKL-KDKDGNEFMLKpphgDGLPQRGY-DAGENTYQAPPADRSTVEvKVSPTSDRLQLLK--- 566
Cdd:PTZ00092 563 LVVAYALAGRVNIDFETEPLgSDKTGKPVFLR----DIWPSREEiQALEAKYVKPEMFKEVYS-NITQGNKQWNELQvpk 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 567 -PFKPWDGKDA--------KDMPILIKAVGK-------------TTTDHISMAG------PWLKY--------------- 603
Cdd:PTZ00092 638 gKLYEWDEKSTyihnppffQTMELEPPPIKSienaycllnlgdsITTDHISPAGniaknsPAAKYlmergverkdfntyg 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 604 ----------RGHLENIS-NNYMIGAInaenkkanCVKNVY--TGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSSREH 670
Cdd:PTZ00092 718 arrgndevmvRGTFANIRlINKLCGKV--------GPNTVHvpTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDW 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 671 AALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDR----IDiLGLAELAPGKPVTMRVhpKNGKP 746
Cdd:PTZ00092 790 AAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKeqfsID-LNSGELKPGQDVTVKT--DTGKT 866
|
810 820
....*....|....*....|....*
gi 6323335 747 WDAVLthTFNDE-QIEWFKYGSALN 770
Cdd:PTZ00092 867 FDTIL--RIDTEvEVEYFKHGGILQ 889
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
60-500 |
6.18e-72 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 241.20 E-value: 6.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 60 TYAEKILYGHlddpHGQDIQRGVSyLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTVHC--DHLIQAqvggeKDLK 137
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDL-IEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA-----DTIK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 138 RAiDLNKEVYDFLASATAKYnmgFWKPGSGIIHQIVLEN-YAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMA-G 215
Cdd:TIGR01343 71 AA-EMQKLAREFVKKQGIKY---FYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAtG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 216 RPWeLKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 295
Cdd:TIGR01343 147 KTW-FKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 296 NKSMIEYLEATGRGKiadfAKLYhkdllSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVANNWpldvr 375
Cdd:TIGR01343 226 DEKTIQYLKERRKEP----FRVY-----KSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVF----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 376 vglIGSCTNSSYEDMSRSASIVKdaaAHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGqwdRR 455
Cdd:TIGR01343 292 ---IGSCTNGRLEDLRVAAKILK---GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SH 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 6323335 456 DIKKGDKNTIVSSYNRNFTSRNdGNPQTHAFVASPELVTAFAIAG 500
Cdd:TIGR01343 363 QGVLAPGEVCISTSNRNFKGRM-GHPNAEIYLASPATAAASAVKG 406
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
88-769 |
1.42e-67 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 240.86 E-value: 1.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 88 RPDRVACQDATAQMAI--LQFMSAGLPQVAK---------PVTVHCDHLIQAQVGG-----EKDLKRAIDLNKEVYDFLA 151
Cdd:PLN00070 121 KPARVLLQDFTGVPAVvdLACMRDAMNNLGGdpnkinplvPVDLVIDHSVQVDVARsenavQANMELEFQRNKERFAFLK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 152 -SATAKYNMGFWKPGSGIIHQIVLENYA----------FPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWEL 220
Cdd:PLN00070 201 wGSTAFQNMLVVPPGSGIVHQVNLEYLGrvvfntdgilYPDSVV-GTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 221 KAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMI 300
Cdd:PLN00070 280 VLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 301 EYLEATGR-GKIADFAKLYHK------DLLSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEvavanNWP-- 371
Cdd:PLN00070 360 QYLKLTGRsDETVAMIEAYLRankmfvDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKA-----DWHsc 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 372 LDVRVGL----------------------------------IGSCTNSSYEDMSRSASIV-KDAAAHGLKSKT-IFT-VT 414
Cdd:PLN00070 435 LDNKVGFkgfavpkeaqskvakfsfhgqpaelrhgsvviaaITSCTNTSNPSVMLGAGLVaKKACELGLEVKPwIKTsLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 415 PGSEQIRATIERDGQLETFKEFGGIVLANACGPCI---GQWDRRDIKKGDKNTIVS----SYNRNFTSRNdgNPQTHA-F 486
Cdd:PLN00070 515 PGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIgnsGELDESVASAITENDIVAaavlSGNRNFEGRV--HPLTRAnY 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 487 VASPELVTAFAIAGDLRFNPLTDKL-KDKDGNEFMLKpphgDGLPQRGYDAGENTYQA-PPADRSTVEV--KVSPTSDRL 562
Cdd:PLN00070 593 LASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDVFFR----DIWPSNEEVAEVVQSSVlPDMFKSTYEAitKGNPMWNQL 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 563 QL-LKPFKPWDGKDA--------KDMPI-------------LIKAVGKTTTDHISMAG------PWLKY----------- 603
Cdd:PLN00070 669 SVpSGTLYSWDPKSTyiheppyfKNMTMsppgphgvkdaycLLNFGDSITTDHISPAGsihkdsPAAKYlmergvdrkdf 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 604 --------------RGHLENIS--NNYMIGAINAENkkancvKNVYTGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSS 667
Cdd:PLN00070 749 nsygsrrgndeimaRGTFANIRivNKLLKGEVGPKT------VHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSS 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 668 REHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDK--INPDDRIDI---LGLAELAPGKPVTmrVHPK 742
Cdd:PLN00070 823 RDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTlgLTGHERYTIdlpSNISEIKPGQDVT--VTTD 900
|
810 820
....*....|....*....|....*...
gi 6323335 743 NGKPWDAVLthTFNDE-QIEWFKYGSAL 769
Cdd:PLN00070 901 NGKSFTCTL--RFDTEvELAYFDHGGIL 926
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
579-709 |
1.24e-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: 203.37 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 579 MPILIKAVGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNVYTGEYKGVPDTARDYRDQGIKWVVIG 658
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6323335 659 DENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNP 709
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
112-500 |
1.08e-57 |
|
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: 202.15 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 112 PQVakPVTVHCDHLIQAQVGG-----EKDLKRAIDLNKEVYDFL-ASATAKYNMGFWKPGSGIIHQIVLE---------- 175
Cdd:cd01586 35 PLI--PVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFLkWGQKAFKNLRVVPPGTGIIHQVNLEylarvvftse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 176 ----NYAFPGALIiGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGIT 251
Cdd:cd01586 113 edgdGVAYPDSVV-GTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 252 TVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNksmieyleatgrgkiadfaklyhkdllsadkdaey 331
Cdd:cd01586 192 RKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD----------------------------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 332 DEVVEIDLNTLEPYINGPFTPDLATPVSKmkevavannwplDVRVGLIGSCTNSSYEDMSRSASIV-KDAAAHGLKS--- 407
Cdd:cd01586 237 TQVVELDLSTVEPSVSGPKRPQDRVPLHG------------SVVIAAITSCTNTSNPSVMLAAGLLaKKAVELGLKVkpy 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 408 -KTifTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIG------QWDRRDIKKGD-KNTIVSSYNRNFTSRNdg 479
Cdd:cd01586 305 vKT--SLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpEEVEEAIKENDlVVAAVLSGNRNFEGRI-- 380
|
410 420
....*....|....*....|..
gi 6323335 480 NPQTHA-FVASPELVTAFAIAG 500
Cdd:cd01586 381 HPLVRAnYLASPPLVVAYALAG 402
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
103-502 |
1.10e-41 |
|
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: 156.24 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 103 ILQFMSAGLPQVAKPVTVHC--DHLIQAQvgGEKDLKRaidlnkevYDFLASATAKYNMGFWKPGSGIIHQIVLEN-YAF 179
Cdd:cd01582 12 ALKFMSIGATKIHNPDQIVMtlDHDVQNK--SEKNLKK--------YKNIESFAKKHGIDFYPAGRGIGHQIMIEEgYAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 180 PGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMA-GRPWeLKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTG 258
Cdd:cd01582 82 PGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 259 KIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPfnksmieyleatgrgkiADFAKLYhkdllsadkdaeydevveID 338
Cdd:cd01582 161 HAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFP-----------------TDAKHLI------------------LD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 339 LNTLEPYINGPFTPDLATPVSKMKEVAVAnnwpldVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTI----FTVT 414
Cdd:cd01582 206 LSTLSPYVSGPNSVKVSTPLKELEAQNIK------INKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIPVApgveFYVA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 415 PGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGqwdrrdIKKG---DKNTIVSSYNRNFTSRNdGNPQTHAFVASPE 491
Cdd:cd01582 280 AASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG------LGQGllePGEVGISATNRNFKGRM-GSTEALAYLASPA 352
|
410
....*....|.
gi 6323335 492 LVTAFAIAGDL 502
Cdd:cd01582 353 VVAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
150-500 |
1.05e-40 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 156.05 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 150 LASATAKYNMGFWKPGS---GIIHQIVLENYA-FPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKI 225
Cdd:PRK05478 86 LEKNCKEFGITLFDLGDprqGIVHVVGPEQGLtLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 226 LGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGA---------TTsvfpfn 296
Cdd:PRK05478 166 MKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 297 ksmIEYLEatGR-----GKIADFAKLYHKDLLSaDKDAEYDEVVEIDLNTLEPY------------INGPFtPDLA---- 355
Cdd:PRK05478 240 ---FEYLK--GRpfapkGEDWDKAVAYWKTLKS-DEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKV-PDPEdfad 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 356 ----------------TPVSKMKEVAVannwplDVrVgLIGSCTNSSYEDMSRSASIVKDaaaHGLKSKTIFTVTPGSEQ 419
Cdd:PRK05478 313 pvkrasaeralaymglKPGTPITDIKI------DK-V-FIGSCTNSRIEDLRAAAAVVKG---RKVAPGVRALVVPGSGL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 420 IRATIERDGQLETFKEFG------GivlanaCGPCIGQWDRRdIKKGDKntIVSSYNRNFTSRNDGNPQTHafVASPELV 493
Cdd:PRK05478 382 VKAQAEAEGLDKIFIEAGfewrepG------CSMCLAMNPDK-LPPGER--CASTSNRNFEGRQGKGGRTH--LVSPAMA 450
|
....*..
gi 6323335 494 TAFAIAG 500
Cdd:PRK05478 451 AAAAITG 457
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
164-502 |
1.93e-39 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 152.37 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 164 PGSGIIHQIVLE-NYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKD 242
Cdd:PRK12466 105 PRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 243 IILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGR---GKIADFAKLYH 319
Cdd:PRK12466 185 LILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRapkGALWDAALAYW 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 320 KDLLSaDKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVS-------------KMKEVAVANNW-------PL-DVRVG- 377
Cdd:PRK12466 265 RTLRS-DADAVFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpaaeadpaRRAAMERALDYmgltpgtPLaGIPIDr 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 378 -LIGSCTNSSYEDMSRSASIVKD--AAAH--GLksktiftVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQW 452
Cdd:PRK12466 344 vFIGSCTNGRIEDLRAAAAVLRGrkVAPGvrAM-------VVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMN 416
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 6323335 453 DRRdIKKGDKntIVSSYNRNFTSRNDGNPQTHafVASPELVTAFAIAGDL 502
Cdd:PRK12466 417 DDV-LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAGHI 461
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
85-714 |
1.94e-34 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 140.91 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 85 LKLRPDRVACQDATAqMAILQFMSA-GLPQVAKPVTVHCDHLIQAQVGGEkdlkraidLNKEVYDFLASATAKYNMGFWK 163
Cdd:PRK11413 54 LKIKFDSLASHDITF-VGIIQTAKAsGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGIFVP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 164 PGSGIIHQIVLENYAFPGALIIGTDSHTpNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDI 243
Cdd:PRK11413 125 PHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 244 ILKLAGiTTVKGG--TGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKiaDFAKLYHKD 321
Cdd:PRK11413 204 ALAIIG-AVFKNGyvKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQ--DYCELNPQP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 322 LlsadkdAEYDEVVEIDLNTLEPYINGPFTP--------------DLATPVSKMKEVAVANNWPLD-----------VRV 376
Cdd:PRK11413 281 M------AYYDGCISVDLSAIKPMIALPFHPsnvyeidelnqnltDILREVEIESERVAHGKAKLSlldkiengrlkVQQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 377 GLIGSCTNSSYEDMSrsasivkdAAAHGLKSKTI------FTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIG 450
Cdd:PRK11413 355 GIIAGCSGGNYENVI--------AAANALRGQSCgndtfsLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 451 QWDrrdiKKGDKNTIVSSYNRNFTSRNDGNPQTHAfVASPELVTAFAIAGDL----RFNPLTDklKDKDGNefmlKPP-H 525
Cdd:PRK11413 427 AGD----TPANNGLSIRHTTRNFPNREGSKPANGQ-MSAVALMDARSIAATAanggYLTSATE--LDCWDN----VPEyA 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 526 GDGLPqrgYDAgeNTYQAPPADRSTVEVKVSPTsdrlqllkpFKPWdgkdaKDMP-----ILIKAVGK-----TTTDHIS 595
Cdd:PRK11413 496 FDVTP---YKN--RVYQGFGKGATQQPLIYGPN---------IKDW-----PEMGaltdnILLKVCSKildpvTTTDELI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 596 MAGPWLKYRGH-------------LENISNNYMIGAINAENKKANC--VKNVYT--GEYKGVPDTarDYRDQGIKWVVIG 658
Cdd:PRK11413 557 PSGETSSYRSNplglaeftlsrrdPGYVGRSKAVAELENQRLAGNVseLTEVFAriKQIAGQEHI--DPLQTEIGSMVYA 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323335 659 DENfGEGSSREHAALEPRFLGGFAIITKSFA-RIHETNLKKQGLLPLNFKNPADYDK 714
Cdd:PRK11413 635 VKP-GDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEEPTFEV 690
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
590-723 |
1.24e-27 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 107.91 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 590 TTDHISMAGP-WLKYRGHLENISNnymigainaenkkancvknvYTgeYKGVPDTARDYRDQGIKWVVIGDENFGEGSSR 668
Cdd:cd01579 7 TTDHIMPAGAkVLPLRSNIPAISE--------------------FV--FHRVDPTFAERAKAAGPGFIVGGENYGQGSSR 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6323335 669 EHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDI 723
Cdd:cd01579 65 EHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLEL 119
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
654-725 |
2.19e-27 |
|
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: 106.01 E-value: 2.19e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323335 654 WVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDILG 725
Cdd:cd00404 17 GVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
137-500 |
5.83e-20 |
|
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: 93.33 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 137 KRAIDLNKEVYDFLASatakYNMGFWKPGSGIIHQiVLENYAFPGALIIGTDSHT--------PNAGGLGQLAIGVGgad 208
Cdd:cd01581 68 PVDVKTHRTLPDFISN----RGGVALRPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGLVAFAAATG--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 209 avdVMAgrpweLKAPKILGVKLTGKMNGWTSPKDII-------LKLAGITTVKGG-----TGKIVEYfgDGVDTFSATGM 276
Cdd:cd01581 140 ---VMP-----LDMPESVLVRFKGKMQPGITLRDLVnaipyyaIQQGLLTVEKKGkknvfNGRILEI--EGLPDLKVEQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 277 GTICNMGAEIGATTSVFPFNK-SMIEYLEA------------------TGRGKIADFAKLYHKDLLSADKDAEYDEVVEI 337
Cdd:cd01581 210 FELTDASAERSAAACTVRLDKePVIEYLESnvvlmkimiangyddartLLRRIIAMEEWLANPPLLEPDADAEYAAVIEI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 338 DLNTL-EPYINGPFTPDlatPVSKMKEVAVANnwpldVRVGLIGSC-TNSSyeDMSRSASIVKDAAahglKSKTIFTVTP 415
Cdd:cd01581 290 DLDDIkEPILACPNDPD---DVKLLSEVAGKK-----IDEVFIGSCmTNIG--HFRAAAKILRGKE----FKPTRLWVAP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 416 GSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDRrdIKKGDknTIVSSYNRNFTSRNDGNPQThaFVASPELVTA 495
Cdd:cd01581 356 PTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRVGKGAEV--YLGSAELAAV 429
|
....*
gi 6323335 496 FAIAG 500
Cdd:cd01581 430 CALLG 434
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
588-725 |
1.91e-19 |
|
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: 86.18 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 588 KTTTDHISMAGP---------WLKYRGHLENISNNY---------MIGAINAE----NKKANCVKNVYT-----GEYKGV 640
Cdd:cd01580 5 SVTTDHISPAGSiakdspagkYLAERGVKPRDFNSYgsrrgndevMMRGTFANirlrNKLVPGTEGGTThhpptGEVMSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 641 PDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNP--ADYDKINPD 718
Cdd:cd01580 85 YDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGLTGE 164
|
....*..
gi 6323335 719 DRIDILG 725
Cdd:cd01580 165 ETYDIIG 171
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
163-502 |
1.71e-18 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 90.62 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 163 KPGSGIIHQiVLENYAFPGALIIGTDSHT--------PNAGGLgqlaigVGGADAVDVMAgrpweLKAPKILGVKLTGKM 234
Cdd:PRK09238 462 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGEM 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 235 NGWTSPKDII-------LKlAGITTV--KGG----TGKIVEYfgDGVDTFSATGMGTICNMGAEIGATTSVFPFNK-SMI 300
Cdd:PRK09238 530 QPGITLRDLVhaipyyaIK-QGLLTVekKGKknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKLSKePII 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 301 EYLE-----------------ATGRGKIADF-AKLYHKDLLSADKDAEYDEVVEIDLNTL-EPYINGPFTPDLATPVSkm 361
Cdd:PRK09238 607 EYLRsnivllkwmiaegygdaRTLERRIAAMeEWLANPELLEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLS-- 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 362 kEVAvanNWPLDvrVGLIGSC-TNssYEDMSRSASIVKDaaaHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIV 440
Cdd:PRK09238 685 -EVA---GTKID--EVFIGSCmTN--IGHFRAAGKLLEG---KKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARI 753
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323335 441 LANACGPCIGQWDRrdIKKGDknTIVSSYNRNFTSR--NDGNpqthAFVASPELVTAFAIAGDL 502
Cdd:PRK09238 754 EMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKGAN----VYLGSAELAAVCALLGRI 809
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
163-502 |
2.00e-12 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 71.11 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 163 KPGSGIIHQIvLENYAFPGALIIGTDSHT--------PNAGGLgqlaIGVGGADAVdvmagrpWELKAPKILGVKLTGKM 234
Cdd:PLN00094 536 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfpigisfPAGSGL----VAFGAATGV-------IPLDMPESVLVRFTGTM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 235 NGWTSPKDII-------LKLAGITTVKGG-----TGKIVEYfgDGVDTFSATGMGTICNMGAEIGATTSVFPFNK-SMIE 301
Cdd:PLN00094 604 QPGITLRDLVhaipytaIQDGLLTVEKKGkknvfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDKePIIE 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 302 YLE----------ATGRG-------KIADFAK-LYHKDLLSADKDAEYDEVVEIDLNTL-EPYINGPFTPDLATPVS--- 359
Cdd:PLN00094 682 YLNsnvvmlkwmiAEGYGdrrtlerRIARMQQwLADPELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSevt 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 360 --KMKEVavannwpldvrvgLIGSC-TNSSYedMSRSASIVKDaaaHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEF 436
Cdd:PLN00094 762 gdKIDEV-------------FIGSCmTNIGH--FRAAGKLLND---NLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTV 823
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323335 437 GGIVLANACGPCIGQWDRrdikKGDKNTIVSSYNRNFTSR-NDGnpqTHAFVASPELVTAFAIAGDL 502
Cdd:PLN00094 824 GARTEMPGCSLCMGNQAR----VAEKSTVVSTSTRNFPNRlGKG---ANVYLASAELAAVAAILGRL 883
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
655-723 |
7.27e-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: 59.14 E-value: 7.27e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 655 VVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYD-KINPDDRIDI 723
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
655-736 |
4.41e-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: 59.80 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 655 VVIGDENFGEGSSREHA--ALEpRFlgGF-AIITKSFARIHETNLKKQGLLPLnfknpadydKINPDDRIDILGLAELAP 731
Cdd:COG0066 67 ILVAGRNFGCGSSREHApwALK-DY--GFrAVIAPSFADIFYRNAINNGLLPI---------ELPEEAVDALFAAIEANP 134
|
....*
gi 6323335 732 GKPVT 736
Cdd:COG0066 135 GDELT 139
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
655-723 |
3.13e-09 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 56.76 E-value: 3.13e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323335 655 VVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGlLPLnFKNPADYDKINPDDRIDI 723
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV-LECDEAVDKIEDGDEVEV 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
641-723 |
4.72e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 56.35 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 641 PDTARDYRDQGIkwvVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPlnFKNPADYDKINPDDR 720
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDE 115
|
...
gi 6323335 721 IDI 723
Cdd:PRK14023 116 VEL 118
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
655-736 |
6.30e-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: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 655 VVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFK----NPADYDKINPDDRIDILGLAELA 730
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIEAKtegiKDGDEVTVDLETGEIRVNGNEEY 129
|
....*.
gi 6323335 731 PGKPVT 736
Cdd:TIGR02087 130 KGEPLP 135
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
655-736 |
6.44e-08 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 53.59 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323335 655 VVIGDENFGEGSSREHA--ALEpRFlgGF-AIITKSFARIHETNLKKQGLLPLnfknpadydKINPDDRIDILGLAELAP 731
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA-DY--GFrAVIAPSFADIFYNNCFKNGLLPI---------VLPEEDVDELFKLVEANP 137
|
....*
gi 6323335 732 GKPVT 736
Cdd:PRK01641 138 GAELT 142
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
642-711 |
8.37e-07 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131139 [Multi-domain] Cd Length: 156 Bit Score: 49.41 E-value: 8.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323335 642 DTARDYRDQGIKW-VVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPAD 711
Cdd:TIGR02084 36 DLDKDFVKKVKEGdIIVAGENFGCGSSREHAPIAIKASGISCVIAKSFARIFYRNAINIGLPIVESEEAVD 106
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
655-691 |
6.36e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 45.23 E-value: 6.36e-05
10 20 30
....*....|....*....|....*....|....*..
gi 6323335 655 VVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARI 691
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
655-704 |
3.94e-04 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 129275 [Multi-domain] Cd Length: 188 Bit Score: 42.11 E-value: 3.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6323335 655 VVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPL 704
Cdd:TIGR00171 72 ILLARENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPI 121
|
|
| |
