|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
41-771 |
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: 1250.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 41 YKQNLEYVDIVRQRLG-RPLTYAEKILYGHLEDPHG----QEIE--RGVSYLKLNPDRVACQDATAQMAILQFMSAGLPE 113
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 114 VAKPVTVHCDHLIQAQVGGEKDLARACDLNKEVYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALLIGTDSHTPN 193
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 194 AGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSA 273
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 274 TGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRHQVAEFAQ--LYKKDLLSADEGAEYDEVIEIDLNKLEPYVNGPFT 351
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKtgQYSFFKLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 352 PDLATPISKLKEVAVEKNWPLEVKVGLIGSCTNSSYEDMSRSASIIKDAAAHGLKAKSLFTVTPGSEQIRATIARDGQLD 431
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 432 TFTEFGGIVLANACGPCIGQWDRRD-IKKGEKNTIVSSYNRNFTSRNDGNPETHSFVASPELVTAFAIAGDLRFNPMTDK 510
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 511 LKGKDGKEFLLQPPTGEGLPSGGYDPGENTYQAPPKDRNQ-VEVKVSPTSDRLQLLSAFKPWDGKDPQNMPILIKSLGKT 589
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPNPnVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 590 TTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNHyTGEYSGVPETARAYRDQGIKWVVIGGENFGEGSSRE 669
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDL-DGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 670 HAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYDKINPEDTVDIIGLSEFAP---GKPLTLRIHSSSG-T 745
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGkV 719
|
730 740
....*....|....*....|....*.
gi 45187842 746 WETPLDHTFNKEQIEWFKAGSALNKL 771
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
57-776 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 920.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 57 RPLTYAEKILYGHLEDPhgqEIERGVSyLKLNPDRVACQDATAQMAILQFMSAGLPEVAKPVTV-HCDH-LIQAqvgGEK 134
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDHnLLQA---DFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 135 dlaracdlNKEVYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMS 214
Cdd:PRK07229 74 --------NADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 215 NLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFP 294
Cdd:PRK07229 146 GGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 295 FNKSMVEYLNATNRHQVAefaqlykkDLLSADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEVAVEknwplev 374
Cdd:PRK07229 226 SDERTREFLKAQGREDDW--------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVD------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 375 kVGLIGSCTNSSYEDMSRSASIIKDaaaHGLKAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQwdr 454
Cdd:PRK07229 291 -QVLIGSCTNSSYEDLMRAASILKG---KKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 455 rDIKKGEKNTIVSSYNRNFTSRNdGNPETHSFVASPELVTAFAIAGDLRfNPMTDKLKGkdGKEFLLQPPTgeglpsgGY 534
Cdd:PRK07229 364 -GQAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRTLALEN--GEYPKLEEPE-------GF 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 535 DPGENTYQAPPKDRNQVEVKVSPTSDRLQLLSAFkpwdgKDPQNMPILIKSLGKTTTDHISMAGP-WLKYRGHLENISNN 613
Cdd:PRK07229 432 AVDDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPL-----PDLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEF 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 614 YMIGAINAENKKAncvknhytgeysgvpetarayRDQGiKWVVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHE 693
Cdd:PRK07229 507 VFEGVDNTFPERA---------------------KEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHK 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 694 TNLKKQGLLPLTFHEPAAYDKINPEDTVDIIGLSEFAPGKPLTLRIHssSGTWETPLDHTFNKEQIEWFKAGSALNKLAA 773
Cdd:PRK07229 565 ANLINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNV--TKDEEIEVRHTLSERQIEILLAGGALNLIKK 642
|
...
gi 45187842 774 AKK 776
Cdd:PRK07229 643 KLA 645
|
|
| 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: 836.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 91 RVACQDATAQMAILQFMSAGLPEVAKPVTVHCDHLIQAQVGGEKDLARACDLNKEVYDFLATATAKYNMGFWKPGSGIIH 170
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 171 QIVLENYAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGI 250
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 251 TTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRHQVAEFAQLYKKDLLSADEGAE 330
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKDDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 331 YDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEVAVEKNWPLEVKVGLIGSCTNSSYEDMSRSASIIKDAAAHGLKAKSL 410
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 411 FTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQWDRRDIKKGEKNTIVSSYNRNFTSRNDGNPETHSFVASP 490
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 45187842 491 ELVTAFAIAGDL 502
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
59-774 |
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: 765.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 59 LTYAEKILYGHL---EDP------HGQEI------ERGVSYLKLNPDRVACQDATAQMAILQFMSAGLPEVAK------- 116
Cdd:COG1048 36 LPYSLKILLENLlrnEDGetvteeDIKALanwlpkARGDDEIPFRPARVLMQDFTGVPAVVDLAAMRDAVARLggdpkki 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 117 ----PVTVHCDHLIQAQVGG-----EKDLARACDLNKEVYDFLATATAKY-NMGFWKPGSGIIHQIVLENYAFP------ 180
Cdd:COG1048 116 nplvPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVVPPGTGIVHQVNLEYLAFVvwtree 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 181 -GAL------LIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTV 253
Cdd:COG1048 196 dGETvaypdtLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 254 KGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNR--HQVAEFAQLYKKDLLSADEGA-- 329
Cdd:COG1048 276 KGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRseEQIELVEAYAKAQGLWRDPDApe 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 330 -EYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKE---------VAVEKNWPLEVKV--------------GLIGSCTNS 385
Cdd:COG1048 356 pYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEafraalaapVGEELDKPVRVEVdgeefelghgavviAAITSCTNT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 386 SYEDMSRSASII-KDAAAHGL--KAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQWDR------RD 456
Cdd:COG1048 436 SNPSVMIAAGLLaKKAVEKGLkvKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEA 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 457 IKKGE-KNTIVSSYNRNFTSRNdGNPETHSFVASPELVTAFAIAGDLRFNPMTDKL-KGKDGKEFLLQP--PTGEGLP-- 530
Cdd:COG1048 516 IEENDlVVAAVLSGNRNFEGRI-HPDVKANFLASPPLVVAYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPaa 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 531 ------SGGY----------DPGENTYQAP-----PKDRNQVEVKVSPTSDRLQLLsafkPWDGKDPQNMPILIKSLGKT 589
Cdd:COG1048 595 vfkavtPEMFraryadvfdgDERWQALEVPagelyDWDPDSTYIRRPPFFEGLQLE----PEPFKDIKGARVLAKLGDSI 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 590 TTDHISMAGP-----------------------WLKYRGHLENISNNYMIGA--IN--AENKKANCVKNHYTGEYSGVPE 642
Cdd:COG1048 671 TTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFANIriKNllAPGTEGGYTKHQPTGEVMSIYD 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 643 TARAYRDQGIKWVVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYDK--INPEDT 720
Cdd:COG1048 751 AAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDET 830
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45187842 721 VDIIGLSE-FAPGKPLTLRIHSSSG-TWETPLDHTF-NKEQIEWFKAGSALN----KLAAA 774
Cdd:COG1048 831 FDIEGLDEgLAPGKTVTVTATRADGsTEEFPVLHRIdTPVEVEYYRAGGILQyvlrQLLAA 891
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
63-500 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 580.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 63 EKILYGHLEDphgqEIERGVSYLklnPDRVACQDATAQMAILQFMSAGLP------EVAK-----PVTVHCDHliqAQVG 131
Cdd:pfam00330 1 EKIWDAHLVE----ELDGSLLYI---PDRVLMHDVTSPQAFVDLRAAGRAvrrpggTPATidhlvPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 132 GEKDLARACDLNKEVYDFLATATAKYNMGFWKPGSGIIHQIVLEN-YAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAV 210
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 211 DVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATT 290
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 291 SVFPFNKSMVEYLNATNR---HQVAEFAQLYKKDLLSADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISK------- 360
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRpeaPKGEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpfa 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 361 --LKEVAVEK---------NWPL---EVKVGLIGSCTNSSYEDMSRSASIIKDAAAHGLKAKSL--FTVTPGSEQIRATI 424
Cdd:pfam00330 311 daVKRKAAERaleymglgpGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPGvkASVVPGSEVVRAYA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45187842 425 ARDGQLDTFTEFGGIVLANACGPCIGQWDRRDikkgEKNTIVSSYNRNFTSRNdgNPETHSFVASPELVTAFAIAG 500
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPALVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
91-502 |
2.24e-139 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 416.51 E-value: 2.24e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 91 RVACQDATAQMAILQF-MSAGLPEVAKPVTVHCDHLIQAQVGGEKdlaracdlNKEVYDFLATATAKYNMGFWKPGSGII 169
Cdd:cd01351 1 RVMLQDATGPMAMKAFeILAALGKVADPSQIACVHDHAVQLEKPV--------NNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 170 HQIVLENYAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAG 249
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 250 ITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRHQVAEFAQLYKKDLLsADEGA 329
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELL-ADEGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 330 EYDEVIEIDLNKLEPYVNGPFTPDLATPISklkEVAVEKnwpleVKVGLIGSCTNSSYEDMSRSASIIKDaaaHGLKAKS 409
Cdd:cd01351 232 EYDQVIEIDLSELEPDISGPNRPDDAVSVS---EVEGTK-----IDQVLIGSCTNNRYSDMLAAAKLLKG---AKVAPGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 410 LFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQWDRrdiKKGEKNTIVSSYNRNFTSRNdGNPETHSFVAS 489
Cdd:cd01351 301 RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRL-GTYERHVYLAS 376
|
410
....*....|...
gi 45187842 490 PELVTAFAIAGDL 502
Cdd:cd01351 377 PELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
60-769 |
1.21e-133 |
|
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: 411.30 E-value: 1.21e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 60 TYAEKILYGHLEDPH---GQEIergvsylKLNPDRVACQDATAQMAILQFMSAGLPEVAKPVTV-HCDHLIQaqvggEKD 135
Cdd:TIGR01342 1 TLAEKIIDDHLVEGDlepGEEI-------AIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAqYCDHNML-----QFD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 136 LARACDlnkevYDFLATATAKYNMGFWKPGSGIIHQIVLENYAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMSN 215
Cdd:TIGR01342 69 FKNADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 216 LAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 295
Cdd:TIGR01342 144 EAFYLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 296 NKSMVEYLNATNRHQvaEFAQLykkdllSADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEVAVEKNwplevk 375
Cdd:TIGR01342 224 DDITEAWLAAFDRED--DFVDL------LADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIAGIEVDQV------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 376 vgLIGSCTNSSYEDMSRSASIIKDAAAHglkAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQwdrr 455
Cdd:TIGR01342 290 --MIGSCTNGAFEDLLPAAKLLEGREVH---KDTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI---- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 456 DIKKGEKNTIVSSYNRNFTSRNdGNPETHSFVASPELVTAFAIAGDLrFNPMtdKLKGKDGKEFLLQPPTGEGLPsGGYD 535
Cdd:TIGR01342 361 GFAPASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPR--DLADDEGDLEAIGFEMGEKFP-GGYD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 536 PGEnTYQAPPKDRNQVEVKVSPTsdrlqllsaFKPWDGKDPQNMPI----LIKSLGKTTTDHISMAGP-WLKYRGHLENI 610
Cdd:TIGR01342 436 AAD-IDIIPKEEREDDDIIKGPN---------IKPLPEFDPLGADIegetALIMEDNITTDHIIPAGAdILKFRSNIEAI 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 611 SnNYMIGAINAEnkkancvknhytgeysgVPETARAYRDQGIKWVVIGGENFGEGSSREHAALEPRYLGGFAIITRSFAR 690
Cdd:TIGR01342 506 S-EFTLHRIDDE-----------------FAERAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFAR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 691 IHETNLKKQGLLPLTFHEPAAYDKINPEDTVDIIG--LSEFAPGKP-LTLRIHSSsgtWETPLDHTFNKEQIEWFKAGSA 767
Cdd:TIGR01342 568 IHHANLFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDeFTINKNDD---EEALATLDASEREKEILAAGGK 644
|
..
gi 45187842 768 LN 769
Cdd:TIGR01342 645 LN 646
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-502 |
5.79e-116 |
|
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: 355.60 E-value: 5.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 90 DRVACQDATAQMAILQFMSAGLPEVAKPVTV-HCDHLIqAQVGGEkdlaracdlNKEVYDFLATATAKYNMGFWKPGSGI 168
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVsYVDHNT-LQTDFE---------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 169 IHQIVLENYAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLA 248
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 249 GITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRHQvaEFAQlykkdlLSADEG 328
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRED--DWVE------LAADAD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 329 AEYDEVIEIDLNKLEPYVNGPFTPDLATPIsklKEVAveknwPLEVKVGLIGSCTNSSYEDMSRSASIIKDAAAHglkAK 408
Cdd:cd01585 223 AEYDEEIEIDLSELEPLIARPHSPDNVVPV---REVA-----GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVH---PH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 409 SLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQWDrrdiKKGEKNTIVSSYNRNFTSRNdGNPETHSFVA 488
Cdd:cd01585 292 VSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLA 366
|
410
....*....|....
gi 45187842 489 SPELVTAFAIAGDL 502
Cdd:cd01585 367 SPEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
584-732 |
1.10e-97 |
|
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: 299.38 E-value: 1.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 584 KSLGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNHYTGEYSGVPETARAYRDQGIKWVVIGGENFG 663
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45187842 664 EGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYDKINPEDTVDIIGLSEFAPG 732
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
89-768 |
3.46e-90 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 302.62 E-value: 3.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 89 PDRVACQDATAQMAI--LQFMSAGLPEVAK---------PVTVHCDHLIQAQVGGEKD-----LARACDLNKEVYDFLAT 152
Cdd:PRK12881 83 PARVVMQDFTGVPALvdLAAMRDAAAEAGGdpakinplvPVDLVVDHSVAVDYFGQKDaldlnMKIEFQRNAERYQFLKW 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 153 AT-AKYNMGFWKPGSGIIHQIVLE--------------NYAFPGALlIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLA 217
Cdd:PRK12881 163 GMqAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 218 WELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNK 297
Cdd:PRK12881 242 VYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 298 SMVEYLNATNR--HQVAEFAQLYKKDLLSADEGAE--YDEVIEIDLNKLEPYVNGPFTP-------DLATPISKLKEVAV 366
Cdd:PRK12881 322 QTLDYLRLTGRteAQIALVEAYAKAQGLWGDPKAEprYTRTLELDLSTVAPSLAGPKRPqdrialgNVKSAFSDLFSKPV 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 367 EKNWPLE--------------VKVGLIGSCTNSSYEDMSRSASII-KDAAAHGLKAK-----SLftvTPGSEQIRATIAR 426
Cdd:PRK12881 402 AENGFAKkaqtsngvdlpdgaVAIAAITSCTNTSNPSVLIAAGLLaKKAVERGLTVKpwvktSL---APGSKVVTEYLER 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 427 DGQLDTFTEFG-GIVlANACGPCI---GQWDRRDIKKGEKNTIVS----SYNRNFTSRNDGNPEThSFVASPELVTAFAI 498
Cdd:PRK12881 479 AGLLPYLEKLGfGIV-GYGCTTCIgnsGPLTPEIEQAITKNDLVAaavlSGNRNFEGRIHPNIKA-NFLASPPLVVAYAL 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 499 AGDLRFNPMTDKL-KGKDGKEFLLQP--PTGE---GLPSGGYDP---GENTYQAPPKDRNQVEVKVsPTSDRLqllsafk 569
Cdd:PRK12881 557 AGTVRRDLMTEPLgKGKDGRPVYLKDiwPSSAeidALVAFAVDPedfRKNYAEVFKGSELWAAIEA-PDGPLY------- 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 570 PWD---------------GKDPQNM-------PILIksLGKT-TTDHIS---------MAGPWLKYRGHLENISNNY--- 614
Cdd:PRK12881 629 DWDpkstyirrppffdfsMGPAASIatvkgarPLAV--LGDSiTTDHISpagaikadsPAGKYLKENGVPKADFNSYgsr 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 615 ------MIGAINAeNKKancVKNHY-------------TGEYSGVPETARAYRDQGIKWVVIGGENFGEGSSREHAALEP 675
Cdd:PRK12881 707 rgnhevMMRGTFA-NVR---IKNLMipgkeggltlhqpSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGT 782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 676 RYLGGFAIITRSFARIHETNLKKQGLLPLTFHE---PAAYdKINPEDTVDIIGLS-EFAPGKPLTLRIHSSSGTW----- 746
Cdd:PRK12881 783 RLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGgdsRQSL-GLTGGETFDIEGLPgEIKPRQDVTLVIHRADGSTervpv 861
|
810 820
....*....|....*....|....*.
gi 45187842 747 ----ETPLDhtfnkeqIEWFKAGSAL 768
Cdd:PRK12881 862 lcriDTPIE-------VDYYKAGGIL 880
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
58-500 |
1.46e-88 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 285.39 E-value: 1.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 58 PLTYAEKILYGHLedphGQEIERGvSYLKLNPDRVACQDATAQMAILQFMSAGLPEVAKP--VTVHCDHLIQAqvggeKD 135
Cdd:COG0065 2 GMTLAEKILARHA----GREVEPG-EIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPdrIVAVFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 136 LARAcdlnkEVYDFLATATAKYNMGFWKPGS-GIIHQIVLEN-YAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVM 213
Cdd:COG0065 72 PKSA-----EQVKTLREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 214 snlA----WeLKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGAT 289
Cdd:COG0065 147 ---AtgtlW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 290 TSVFPFNKSMVEYLNAtnrHQVAEFAQLYkkdllsADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEVAVEkn 369
Cdd:COG0065 223 AGIIAPDETTFEYLKG---RPFAPWRTLK------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKID-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 370 wplevkVGLIGSCTNSSYEDMSRSASIIKdaaahGLKAKSLFT--VTPGSEQIRATIARDGQLDTFTEFGGIVLANACGP 447
Cdd:COG0065 292 ------QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPGVRaiVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGM 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 45187842 448 CIG-QWDRrdIKKGEknTIVSSYNRNFTSRNdGNPETHSFVASPELVTAFAIAG 500
Cdd:COG0065 361 CLGmNMGV--LAPGE--RCASTSNRNFEGRM-GSPGSRTYLASPATAAASAIAG 409
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
58-500 |
1.07e-84 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 275.13 E-value: 1.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 58 PLTYAEKILYGHLedphGQEIERGvSYLKLNPDRVACQDATAQMAILQFMSAGLPEVAKP--VTVHCDHLIQAqvggeKD 135
Cdd:PRK00402 2 GMTLAEKILARHS----GRDVSPG-DIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPskIVIVFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 136 LARACDLnKEVYDFLATATAKYnmgFWKPGSGIIHQIVLEN-YAFPGALLIGTDSHTPNAGGLGQLAIGVGGAD-AVDVM 213
Cdd:PRK00402 72 IKSAEQQ-KILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCTYGALGAFATGMGSTDmAAAMA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 214 SNLAWeLKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVF 293
Cdd:PRK00402 148 TGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 294 PFNKSMVEYLnatNRHQVAEFAQLYkkdllsADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEVAVEknwple 373
Cdd:PRK00402 227 APDEKTLEYL---KERAGRDYKPWK------SDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVD------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 374 vkVGLIGSCTNSSYEDMSRSASIIKDaaaHGLKAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQWD 453
Cdd:PRK00402 292 --QVFIGSCTNGRLEDLRIAAEILKG---RKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHM 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 45187842 454 RRdIKKGEknTIVSSYNRNFTSRNdGNPETHSFVASPELVTAFAIAG 500
Cdd:PRK00402 367 GV-LAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
89-745 |
1.43e-84 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 287.40 E-value: 1.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 89 PDRVACQDATAQMAI--LqfmsAGL---------------PEVakPVTVHCDHLIQAQVGGEKD-LARACDL----NKEV 146
Cdd:PRK09277 84 PARVVMQDFTGVPAVvdL----AAMrdaiadlggdpakinPLV--PVDLVIDHSVQVDYFGTPDaFEKNVELeferNEER 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 147 YDFLA-TATAKYNMGFWKPGSGIIHQIVLE-------------NYAFPGALlIGTDSHTPNAGGLGQLAIGVGGADAVDV 212
Cdd:PRK09277 158 YQFLKwGQKAFDNFRVVPPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 213 MSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKlagITTV---KGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGAT 289
Cdd:PRK09277 237 MLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLT---VTEMlrkKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGAT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 290 TSVFPFNKSMVEYLNATNR--HQVAEFAQLYKKDLL--SADEGAEYDEVIEIDLNKLEPYVNGP-------FTPDLATPI 358
Cdd:PRK09277 314 CGFFPIDEETLDYLRLTGRdeEQVALVEAYAKAQGLwrDPLEEPVYTDVLELDLSTVEPSLAGPkrpqdriPLSDVKEAF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 359 SKLKEVAVEKNWPLEVKVGL-------------IGSCTNSSYEDMSRSASII-KDAAAHGLKAK-----SLftvTPGSEQ 419
Cdd:PRK09277 394 AKSAELGVQGFGLDEAEEGEdyelpdgavviaaITSCTNTSNPSVMIAAGLLaKKAVEKGLKVKpwvktSL---APGSKV 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 420 IRATIARDGQLDTFTEFG-GIVlANACGPCIG---------QwdrRDIKKGE-KNTIVSSYNRNFtsrnDG--NPETH-S 485
Cdd:PRK09277 471 VTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAINDNDlVVTAVLSGNRNF----EGriHPLVKaN 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 486 FVASPELVTAFAIAGDLRFNPMTDKL-KGKDGKEFLLQ--------------------------------PPTGEGLPSg 532
Cdd:PRK09277 543 YLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKdiwpsdeeidavvakavkpemfrkeyadvfegDERWNAIEV- 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 533 gydPGENTYQAPPKD---RNqvevkvSPTSDRLQLlsafKPWDGKDPQNMPILIKsLG-KTTTDHISMAGP--------- 599
Cdd:PRK09277 622 ---PEGPLYDWDPDStyiRN------PPYFEGMLA----EPGPVRDIKGARVLAL-LGdSITTDHISPAGAikadspagk 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 600 WLKYRGHLENISNNY---------MIGA----INAENKKANCVKNHYT-----GEYSGVPETARAYRDQGIKWVVIGGEN 661
Cdd:PRK09277 688 YLLEHGVEPKDFNSYgsrrgnhevMMRGtfanIRIRNEMVPGVEGGYTrhfpeGEVMSIYDAAMKYKEEGTPLVVIAGKE 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 662 FGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYD--KINPEDTVDIIGLSEFAPGKPLTLRI 739
Cdd:PRK09277 768 YGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGATVTVVI 847
|
....*.
gi 45187842 740 HSSSGT 745
Cdd:PRK09277 848 TRADGE 853
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
91-500 |
1.90e-79 |
|
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: 259.81 E-value: 1.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 91 RVACQDATAQMAILQFMSAGLPEVAKPVTVHC--DHLIQAQvggEKDLARACD-LNKEVYDFLATAtakYNMGfwkpGSG 167
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPTP---DIKAAEQVKtLRKFAKEFGINF---FDVG----RQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 168 IIHQIVLENYAF-PGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVM-SNLAWeLKAPKILGVKLTGRMSGWTSPKDIIL 245
Cdd:cd01583 71 ICHVILPEKGLTlPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLaTGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 246 KLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRhqvAEFAQLYkkdllsA 325
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK---AYWKELK------S 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 326 DEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKevaveknwPLEVKVGLIGSCTNSSYEDMSRSASIIKDaaaHGL 405
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVE--------GIKIDQVFIGSCTNGRLEDLRAAAEILKG---RKV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 406 KAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIG-QWDRrdIKKGEknTIVSSYNRNFTSRNdGNPETH 484
Cdd:cd01583 290 ADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRM-GSPGAR 364
|
410
....*....|....*.
gi 45187842 485 SFVASPELVTAFAIAG 500
Cdd:cd01583 365 IYLASPATAAASAITG 380
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
60-500 |
7.43e-74 |
|
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: 246.20 E-value: 7.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 60 TYAEKILYGHledpHGQEIERGVSyLKLNPDRVACQDATAQMAILQFMSAGLPEVAKPVTVHC--DHLIQAqvggekDLA 137
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDL-IEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 138 RACDLNKEVYDFLATATAKYnmgFWKPGSGIIHQIVLEN-YAFPGALLIGTDSHTPNAGGLGQLAIGVGGAD-AVDVMSN 215
Cdd:TIGR01343 70 KAAEMQKLAREFVKKQGIKY---FYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDmAYAIATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 216 LAWeLKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPF 295
Cdd:TIGR01343 147 KTW-FKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 296 NKSMVEYLnatnrhqvaefAQLYKKD--LLSADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEvaveknwpLE 373
Cdd:TIGR01343 226 DEKTIQYL-----------KERRKEPfrVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEG--------TE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 374 VKVGLIGSCTNSSYEDMSRSASIIKdaaAHGLKAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGqwd 453
Cdd:TIGR01343 287 IDQVFIGSCTNGRLEDLRVAAKILK---GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG--- 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 45187842 454 RRDIKKGEKNTIVSSYNRNFTSRNdGNPETHSFVASPELVTAFAIAG 500
Cdd:TIGR01343 361 SHQGVLAPGEVCISTSNRNFKGRM-GHPNAEIYLASPATAAASAVKG 406
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
89-708 |
1.71e-71 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 251.47 E-value: 1.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 89 PDRVACQDATAQMAILQF--------MSAGLPEVAKP---VTVHCDHLIQAQVGGEKDlARACDL------NKEVYDFLA 151
Cdd:PTZ00092 90 PARVLLQDFTGVPAVVDLaamrdamkRLGGDPAKINPlvpVDLVIDHSVQVDFSRSPD-ALELNQeieferNLERFEFLK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 152 -TATAKYNMGFWKPGSGIIHQIVLE----------NYAFPGALlIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWEL 220
Cdd:PTZ00092 169 wGSKAFKNLLIVPPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISM 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 221 KAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMV 300
Cdd:PTZ00092 248 VLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 301 EYLNATNR--HQVAEFAQLYKKDLLSADEGA--EYDEVIEIDLNKLEPYVNGP---------------FTPDLATPISK- 360
Cdd:PTZ00092 328 DYLKQTGRseEKVELIEKYLKANGLFRTYAEqiEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGFk 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 361 ---LKEVAVEKNWPLEVK------------VGLIGSCTNSSYEDMSRSASII-KDAAAHGLKAKSLF--TVTPGSEQIRA 422
Cdd:PTZ00092 408 gfgIPEEKHEKKVKFTYKgkeytlthgsvvIAAITSCTNTSNPSVMLAAGLLaKKAVEKGLKVPPYIktSLSPGSKVVTK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 423 TIARDGQLDTFTEFGGIVLANACGPCIGQWDRRD------IKkgEKNTIVS---SYNRNFTSRNdgNPETHS-FVASPEL 492
Cdd:PTZ00092 488 YLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDpevseaIT--NNDLVAAavlSGNRNFEGRV--HPLTRAnYLASPPL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 493 VTAFAIAGDLRFNPMTDKL-KGKDGKEFLLQP--PTGEGLPSggydpGENTYqAPPKDRNQVEVKVSPTSDRLQLLSAFK 569
Cdd:PTZ00092 564 VVAYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIQA-----LEAKY-VKPEMFKEVYSNITQGNKQWNELQVPK 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 570 ----PWDGK-----DP---QNM---PILIKS---------LG-KTTTDHISMAG------PWLKY--------------- 603
Cdd:PTZ00092 638 gklyEWDEKstyihNPpffQTMelePPPIKSienaycllnLGdSITTDHISPAGniaknsPAAKYlmergverkdfntyg 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 604 ----------RGHLENIS-NNYMIGainaeNKKANCVkNHYTGEYSGVPETARAYRDQGIKWVVIGGENFGEGSSREHAA 672
Cdd:PTZ00092 718 arrgndevmvRGTFANIRlINKLCG-----KVGPNTV-HVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAA 791
|
730 740 750
....*....|....*....|....*....|....*.
gi 45187842 673 LEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHE 708
Cdd:PTZ00092 792 KGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLN 827
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
117-706 |
9.58e-58 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 212.74 E-value: 9.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 117 PVTVHCDHLIQAQVGGEKDLARA-----CDLNKEVYDFLA-TATAKYNMGFWKPGSGIIHQIVLENYA----------FP 180
Cdd:PLN00070 161 PVDLVIDHSVQVDVARSENAVQAnmeleFQRNKERFAFLKwGSTAFQNMLVVPPGSGIVHQVNLEYLGrvvfntdgilYP 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 181 GALlIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKI 260
Cdd:PLN00070 241 DSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKF 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 261 VEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNR--HQVAEFAQLYKKDLLSAD-----EGAEYDE 333
Cdd:PLN00070 320 VEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRsdETVAMIEAYLRANKMFVDynepqQERVYSS 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 334 VIEIDLNKLEPYVNGPFTPDLATPISKLKE--------------VAVEKN------------WPLEVKVG-----LIGSC 382
Cdd:PLN00070 400 YLELDLEDVEPCISGPKRPHDRVPLKEMKAdwhscldnkvgfkgFAVPKEaqskvakfsfhgQPAELRHGsvviaAITSC 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 383 TNSSYED-MSRSASIIKDAAAHGLKAKSLF--TVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCI---GQWDRRD 456
Cdd:PLN00070 480 TNTSNPSvMLGAGLVAKKACELGLEVKPWIktSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIgnsGELDESV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 457 IKKGEKNTIVS----SYNRNFTSRNdgNPETHS-FVASPELVTAFAIAGDLRFNPMTDKL-KGKDGKEFLLQP--PTGEG 528
Cdd:PLN00070 560 ASAITENDIVAaavlSGNRNFEGRV--HPLTRAnYLASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDVFFRDiwPSNEE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 529 ---------LPsggyDPGENTYQAPPKDR---NQVEVkvsPTSDRLqllsafkPWDGK-----DP---QNMPI------- 581
Cdd:PLN00070 638 vaevvqssvLP----DMFKSTYEAITKGNpmwNQLSV---PSGTLY-------SWDPKstyihEPpyfKNMTMsppgphg 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 582 ------LIKSLGKTTTDHISMAG------PWLKY-------------------------RGHLENIS--NNYMIGAINAE 622
Cdd:PLN00070 704 vkdaycLLNFGDSITTDHISPAGsihkdsPAAKYlmergvdrkdfnsygsrrgndeimaRGTFANIRivNKLLKGEVGPK 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 623 NKkancvknHY-TGEYSGVPETARAYRDQGIKWVVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGL 701
Cdd:PLN00070 784 TV-------HIpTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGI 856
|
....*
gi 45187842 702 LPLTF 706
Cdd:PLN00070 857 IPLCF 861
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
579-709 |
5.01e-57 |
|
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: 190.65 E-value: 5.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 579 MPILIKSLGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNHYTGEYSGVPETARAYRDQGIKWVVIG 658
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 45187842 659 GENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEP 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 ... |
91-500 |
3.58e-50 |
|
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: 181.35 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 91 RVACQDATAQMAILQFmsAGLPEVAK-------------PVTVHCDHLIQAQVGG-----EKDLARACDLNKEVYDFLAT 152
Cdd:cd01586 1 RVILQDFTGVPAVVDL--AAMRDAVKrlggdpekinpliPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFLKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 153 ATAKY-NMGFWKPGSGIIHQIVLE--------------NYAFPGALlIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLA 217
Cdd:cd01586 79 GQKAFkNLRVVPPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 218 WELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNk 297
Cdd:cd01586 158 ISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 298 smveylnatnrhqvaefaqlykkdllsadegaeyDEVIEIDLNKLEPYVNGPFTPDLATPISKlkevaveknwplEVKVG 377
Cdd:cd01586 237 ----------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPLHG------------SVVIA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 378 LIGSCTNSSYED-MSRSASIIKDAAAHGLKAKSLF--TVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIG---- 450
Cdd:cd01586 271 AITSCTNTSNPSvMLAAGLLAKKAVELGLKVKPYVktSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgp 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 45187842 451 --QWDRRDIKKGE-KNTIVSSYNRNFTSRNdgNPETHS-FVASPELVTAFAIAG 500
Cdd:cd01586 351 lpEEVEEAIKENDlVVAAVLSGNRNFEGRI--HPLVRAnYLASPPLVVAYALAG 402
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
103-502 |
3.01e-38 |
|
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: 146.22 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 103 ILQFMSAGLPEVAKPVTVHC--DHLIQAQvgGEKDLARacdlnkevYDFLATATAKYNMGFWKPGSGIIHQIVLEN-YAF 179
Cdd:cd01582 12 ALKFMSIGATKIHNPDQIVMtlDHDVQNK--SEKNLKK--------YKNIESFAKKHGIDFYPAGRGIGHQIMIEEgYAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 180 PGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGK 259
Cdd:cd01582 82 PGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 260 IVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNksmveylnatnrhqvaefaqlyKKDLLsadegaeydevieIDL 339
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD----------------------AKHLI-------------LDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 340 NKLEPYVNGPFTPDLATPISKL--KEVAVEKNWplevkvglIGSCTNSSYEDMSRSASIIKDAA--------AHGLKaks 409
Cdd:cd01582 207 STLSPYVSGPNSVKVSTPLKELeaQNIKINKAY--------LVSCTNSRASDIAAAADVVKGKKekngkipvAPGVE--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 410 lFTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGqWDRRDIKKGEKNtiVSSYNRNFTSRNdGNPETHSFVAS 489
Cdd:cd01582 276 -FYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLAS 350
|
410
....*....|...
gi 45187842 490 PELVTAFAIAGDL 502
Cdd:cd01582 351 PAVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
164-502 |
1.92e-37 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 146.59 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 164 PGSGIIHQIVLE-NYAFPGALLIGTDSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKD 242
Cdd:PRK12466 105 PRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 243 IILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRH-QVAEF--AQLYK 319
Cdd:PRK12466 185 LILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRApKGALWdaALAYW 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 320 KDLLSaDEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPIS-----------KLKEVAVEK---------NWPLE---VKV 376
Cdd:PRK12466 265 RTLRS-DADAVFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpaaeadPARRAAMERaldymgltpGTPLAgipIDR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 377 GLIGSCTNSSYEDMSRSASIIKD-AAAHGLKAkslfTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIGQWDRR 455
Cdd:PRK12466 344 VFIGSCTNGRIEDLRAAAAVLRGrKVAPGVRA----MVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 45187842 456 dIKKGEKntIVSSYNRNFTSRNDGNPETHsfVASPELVTAFAIAGDL 502
Cdd:PRK12466 420 -LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAGHI 461
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
150-500 |
8.93e-37 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 144.49 E-value: 8.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 150 LATATAKYNMGFWKPGS---GIIHQIVLENyafpGALLIGT-----DSHTPNAGGLGQLAIGVGGADAVDVMSNLAWELK 221
Cdd:PRK05478 86 LEKNCKEFGITLFDLGDprqGIVHVVGPEQ----GLTLPGMtivcgDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 222 APKILGVKLTGRMSGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGA---------TTsv 292
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 293 fpfnksmVEYLNatNRH---QVAEF--AQLYKKDLLSaDEGAEYDEVIEIDLNKLEPYV------------NGPFtPDLA 355
Cdd:PRK05478 240 -------FEYLK--GRPfapKGEDWdkAVAYWKTLKS-DEDAVFDKVVTLDAADIEPQVtwgtnpgqvisiDGKV-PDPE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 356 TPISKLKEVAVEK---------NWPLE-VKVG--LIGSCTNSSYEDMSRSASIIKD-AAAHGLKAkslfTVTPGSEQIRA 422
Cdd:PRK05478 309 DFADPVKRASAERalaymglkpGTPITdIKIDkvFIGSCTNSRIEDLRAAAAVVKGrKVAPGVRA----LVVPGSGLVKA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 423 TIARDGQLDTFTEFG------GivlanaCGPCIGQWDRRdIKKGEKntIVSSYNRNFTSRNDGNPETHsfVASPELVTAF 496
Cdd:PRK05478 385 QAEAEGLDKIFIEAGfewrepG------CSMCLAMNPDK-LPPGER--CASTSNRNFEGRQGKGGRTH--LVSPAMAAAA 453
|
....
gi 45187842 497 AIAG 500
Cdd:PRK05478 454 AITG 457
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
85-739 |
5.20e-31 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 130.13 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 85 LKLNPDRVACQDATAqMAILQFMSA-GLPEVAKPVTVHCDHLIQAQVGGEkdlaracdLNKEVYDFLATATAKYNMGFWK 163
Cdd:PRK11413 54 LKIKFDSLASHDITF-VGIIQTAKAsGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGIFVP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 164 PGSGIIHQIVLENYAFPGALLIGTDSHTpNAGGLGQLAIGVGGADAVDVMSNLAWELKAPKILGVKLTGRMSGWTSPKDI 243
Cdd:PRK11413 125 PHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 244 ILKLAGiTTVKGG--TGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMVEYLNATNRhqvaefAQLYKKd 321
Cdd:PRK11413 204 ALAIIG-AVFKNGyvKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGR------GQDYCE- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 322 lLSADEGAEYDEVIEIDLNKLEPYVNGPFTPDLATPISKLKEVA------VEK-------------------NWPLEVKV 376
Cdd:PRK11413 276 -LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLtdilreVEIeservahgkaklslldkieNGRLKVQQ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 377 GLIGSCTNSSYEDMSrsasiikdAAAHGLKAKSL------FTVTPGSEQIRATIARDGQLDTFTEFGGIVLANACGPCIG 450
Cdd:PRK11413 355 GIIAGCSGGNYENVI--------AAANALRGQSCgndtfsLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 451 QWDrrdiKKGEKNTIVSSYNRNFTSRnDGNPETHSFVASPELVTAFAIAGdlrfnpmTDKLKGkdgkefLLQPPTG---- 526
Cdd:PRK11413 427 AGD----TPANNGLSIRHTTRNFPNR-EGSKPANGQMSAVALMDARSIAA-------TAANGG------YLTSATEldcw 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 527 EGLPSGGYDPG--EN-TYQAPPKDRNQVEVKVSPTsdrlqllsaFKPWdgkdPQnMP-----ILIKSLGK-----TTTDH 593
Cdd:PRK11413 489 DNVPEYAFDVTpyKNrVYQGFGKGATQQPLIYGPN---------IKDW----PE-MGaltdnILLKVCSKildpvTTTDE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 594 ISMAGPWLKYRghleniSNNYMIGAINAENKKANCV----------KNHYTGEYSGVPE------TARAYRDQGIKWVVI 657
Cdd:PRK11413 555 LIPSGETSSYR------SNPLGLAEFTLSRRDPGYVgrskavaeleNQRLAGNVSELTEvfarikQIAGQEHIDPLQTEI 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 658 GGENF----GEGSSREHAALEPRYLGGFAIITRSFA-RIHETNLKKQGLLPLTFHEPAAYDK-------------INPED 719
Cdd:PRK11413 629 GSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEEPTFEVgdyiyipgiraalDNPGT 708
|
730 740
....*....|....*....|
gi 45187842 720 TVDIIGLSEFAPGKPLTLRI 739
Cdd:PRK11413 709 TFKGYVIHEDAPVTEITLYM 728
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
590-723 |
3.36e-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: 106.75 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 590 TTDHISMAGP-WLKYRGHLENISNnYMIGAINAEnkkancvknhytgeysgVPETARAyRDQGIkwvVIGGENFGEGSSR 668
Cdd:cd01579 7 TTDHIMPAGAkVLPLRSNIPAISE-FVFHRVDPT-----------------FAERAKA-AGPGF---IVGGENYGQGSSR 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 45187842 669 EHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYDKINPEDTVDI 723
Cdd:cd01579 65 EHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLEL 119
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
654-725 |
1.31e-24 |
|
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: 98.31 E-value: 1.31e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45187842 654 WVVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYDKINPEDTVDIIG 725
Cdd:cd00404 17 GVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
588-725 |
6.85e-20 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 87.72 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 588 KTTTDHISMAGP---------WLKYRGHLENISNNY---------MIGAINAE----NKKANCVKNHYT-----GEYSGV 640
Cdd:cd01580 5 SVTTDHISPAGSiakdspagkYLAERGVKPRDFNSYgsrrgndevMMRGTFANirlrNKLVPGTEGGTThhpptGEVMSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 641 PETARAYRDQGIKWVVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFH--EPAAYDKINPE 718
Cdd:cd01580 85 YDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPpgENADSLGLTGE 164
|
....*..
gi 45187842 719 DTVDIIG 725
Cdd:cd01580 165 ETYDIIG 171
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
163-500 |
1.84e-16 |
|
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: 82.55 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 163 KPGSGIIHQiVLENYAFPGALLIGTDSHT--------PNAGGLGQLAIGVGgadavdVMSnlaweLKAPKILGVKLTGRM 234
Cdd:cd01581 90 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGLVAFAAATG------VMP-----LDMPESVLVRFKGKM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 235 SGWTSPKDII-------LKLAGITTVKGG-----TGKIVEYfgDGVDTFSATGMGTICNMGAEIGATTSVFPFNK-SMVE 301
Cdd:cd01581 158 QPGITLRDLVnaipyyaIQQGLLTVEKKGkknvfNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVRLDKePVIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 302 YLNA------------------TNRHQVAEFAQLYKKDLLSADEGAEYDEVIEIDLNKL-EPYVNGPFTPDLATPISklk 362
Cdd:cd01581 236 YLESnvvlmkimiangyddartLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIkEPILACPNDPDDVKLLS--- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 363 EVAVEKnwpleVKVGLIGSC-TNSSyeDMSRSASIIKDAAahglKAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVL 441
Cdd:cd01581 313 EVAGKK-----IDEVFIGSCmTNIG--HFRAAAKILRGKE----FKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTE 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 45187842 442 ANACGPCIGQWDRrdIKKGEknTIVSSYNRNFTSRNDGNpeTHSFVASPELVTAFAIAG 500
Cdd:cd01581 382 MPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRVGKG--AEVYLGSAELAAVCALLG 434
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
163-502 |
1.15e-15 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 81.38 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 163 KPGSGIIHQiVLENYAFPGALLIGTDSHT--------PNAGGLgqlaigVGGADAVDVMSnlaweLKAPKILGVKLTGRM 234
Cdd:PRK09238 462 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGEM 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 235 SGWTSPKDII-------LKlAGITTV--KGG----TGKIVEYfgDGVDTFSATGMGTICNMGAEIGATTSVFPFNK-SMV 300
Cdd:PRK09238 530 QPGITLRDLVhaipyyaIK-QGLLTVekKGKknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKLSKePII 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 301 EYLN-----------------ATNRHQVAEF-AQLYKKDLLSADEGAEYDEVIEIDLNKL-EPYVNGPFTPDLATPISkl 361
Cdd:PRK09238 607 EYLRsnivllkwmiaegygdaRTLERRIAAMeEWLANPELLEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLS-- 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 362 kEVAVEKnwpleVKVGLIGSC-TNssYEDMsRSASIIKDAAAHGLKAKslFTVTPGSEQIRATIARDGQLDTFTEFGGIV 440
Cdd:PRK09238 685 -EVAGTK-----IDEVFIGSCmTN--IGHF-RAAGKLLEGKKGQLPTR--LWVAPPTKMDADQLTEEGYYSIFGKAGARI 753
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45187842 441 LANACGPCIGQWDRrdIKKGEknTIVSSYNRNFTSR--NDGNpethSFVASPELVTAFAIAGDL 502
Cdd:PRK09238 754 EMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKGAN----VYLGSAELAAVCALLGRI 809
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
655-723 |
1.40e-13 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 66.84 E-value: 1.40e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 655 VVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYD-KINPEDTVDI 723
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
163-502 |
9.77e-13 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 71.88 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 163 KPGSGIIHQIvLENYAFPGALLIGTDSHT--------PNAGGLgqlaIGVGGADAVdvmsnlaWELKAPKILGVKLTGRM 234
Cdd:PLN00094 536 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfpigisfPAGSGL----VAFGAATGV-------IPLDMPESVLVRFTGTM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 235 SGWTSPKDII-------LKLAGITTVKGG-----TGKIVEYfgDGVDTFSATGMGTICNMGAEIGATTSVFPFNK-SMVE 301
Cdd:PLN00094 604 QPGITLRDLVhaipytaIQDGLLTVEKKGkknvfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDKePIIE 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 302 YLNA-----------------TNRHQVAEFAQ-LYKKDLLSADEGAEYDEVIEIDLNKL-EPYVNGPFTPDLATPISklk 362
Cdd:PLN00094 682 YLNSnvvmlkwmiaegygdrrTLERRIARMQQwLADPELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLS--- 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 363 EVAVEKnwpleVKVGLIGSC-TNSSYedMSRSASIIKDaaaHGLKAKSLFTVTPGSEQIRATIARDGQLDTFTEFGGIVL 441
Cdd:PLN00094 759 EVTGDK-----IDEVFIGSCmTNIGH--FRAAGKLLND---NLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTE 828
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45187842 442 ANACGPCIGQWDRrdikKGEKNTIVSSYNRNFTSR-NDGnpeTHSFVASPELVTAFAIAGDL 502
Cdd:PLN00094 829 MPGCSLCMGNQAR----VAEKSTVVSTSTRNFPNRlGKG---ANVYLASAELAAVAAILGRL 883
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
655-736 |
8.15e-12 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 64.81 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 655 VVIGGENFGEGSSREHA--ALEpRYlgGF-AIITRSFARIHETNLKKQGLLPLTFhepaaydkinPEDTVD-IIGLSEFA 730
Cdd:COG0066 67 ILVAGRNFGCGSSREHApwALK-DY--GFrAVIAPSFADIFYRNAINNGLLPIEL----------PEEAVDaLFAAIEAN 133
|
....*.
gi 45187842 731 PGKPLT 736
Cdd:COG0066 134 PGDELT 139
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
655-723 |
8.19e-11 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 61.00 E-value: 8.19e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45187842 655 VVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFhePAAYDKINPEDTVDI 723
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLEC--DEAVDKIEDGDEVEV 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
641-723 |
6.20e-10 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 58.66 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 641 PETARAYRDQGIkwvVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPltFHEPAAYDKINPEDT 720
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDE 115
|
...
gi 45187842 721 VDI 723
Cdd:PRK14023 116 VEL 118
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
655-736 |
9.06e-10 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 58.99 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 655 VVIGGENFGEGSSREHA--ALEpRYlgGF-AIITRSFARIHETNLKKQGLLPLTFhepaaydkinPEDTVD-IIGLSEFA 730
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA-DY--GFrAVIAPSFADIFYNNCFKNGLLPIVL----------PEEDVDeLFKLVEAN 136
|
....*.
gi 45187842 731 PGKPLT 736
Cdd:PRK01641 137 PGAELT 142
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
655-736 |
2.86e-09 |
|
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: 56.66 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45187842 655 VVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYD----KINPEDTVDIIGLSEFA 730
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIEAKTEGIKDgdevTVDLETGEIRVNGNEEY 129
|
....*.
gi 45187842 731 PGKPLT 736
Cdd:TIGR02087 130 KGEPLP 135
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
655-723 |
2.75e-08 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131139 [Multi-domain] Cd Length: 156 Bit Score: 53.64 E-value: 2.75e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45187842 655 VVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEpaAYDKINPEDTVDI 723
Cdd:TIGR02084 50 IIVAGENFGCGSSREHAPIAIKASGISCVIAKSFARIFYRNAINIGLPIVESEE--AVDEIEEGDEVEV 116
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
655-691 |
6.31e-06 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 48.32 E-value: 6.31e-06
10 20 30
....*....|....*....|....*....|....*..
gi 45187842 655 VVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARI 691
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
655-717 |
7.34e-05 |
|
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: 44.42 E-value: 7.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45187842 655 VVIGGENFGEGSSREHAALEPRYLGGFAIITRSFARIHETNLKKQGLLPLTFHEPAAYDKINP 717
Cdd:TIGR00171 72 ILLARENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQ 134
|
|
| |
