|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
42-771 |
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: 1440.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 42 YKKMSENLDIVRRRL-SRPLTYAEKVLYSHLDDPHG----QDIE--RGVSYLKLRPDRVACQDATAQMAILQFMSAGMPS 114
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLnSRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 115 VATPTTVHCDHLIEAQVGGEKDLARANEINKEVYDFLATATAKYNIGFWKPGSGIIHQIVLENYAFPGGLMIGTDSHTPN 194
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 195 AGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSC 274
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 275 TGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRQHIGEFAR--SYAKE-LREDEGAEYDQLIEINLSELEPHINGPFT 351
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKtgQYSFFkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 352 PDLATPISKFKEAVDANGWPEELKVGLIGSCTNSSYEDMSRAASIARDALNHGVKSKSLFTVTPGSEQIRATIERDGQLQ 431
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 432 TLEEFGGVILANACGPCIGQWDRKD-VKKGEPNSIISSYNRNFTGRNDANPATHAFVASPDLVVAMCVAGTLKFNPLTDT 510
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 511 VKDKDGKEFKLAPPSGDGLPSKGYDAGRNTYQAPPQD-RASINVAVSPTSDRLQLLAGFEAWDGKDANGIPILIKCQGKT 589
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSpNPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 590 TTDHISMAGPWLKYRGHLDNISNNMLIGAVNAENGEANKVKNKfTGEYGAVPATARDYKARGVKWVVIGDWNYGEGSSRE 669
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDL-DGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 670 HAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKIQPEDTVDLL-CTELEV---GKPMTLRVHPKNGST 745
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLnLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 3661614 746 FDVKLNHTFNESQIEWFKDGSALNTM 771
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
58-776 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 926.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 58 RPLTYAEKVLYSHLDDPhgqDIERGVSyLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTV-HCDHlieaqvggekD 136
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 137 LARANEINKEVYDFLATATAKYNIGFWKPGSGIIHQIVLENYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAG 216
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 217 LPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPF 296
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 297 NDRMYDYLKATKRQHIgefarsyAKELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISKFKEavdangwpEELKV 376
Cdd:PRK07229 227 DERTREFLKAQGREDD-------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAG--------IKVDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 377 GLIGSCTNSSYEDMSRAASIARDalnHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGQwdrkD 456
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILKG---KKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 457 VKKGEPNSIISSYNRNFTGRNdANPATHAFVASPDLVVAMCVAGTLKfNPLTDTvkDKDGKEFKLAPPsgdglpsKGYDA 536
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRTLA--LENGEYPKLEEP-------EGFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 537 GRNTYQAPPQDRASINVAVSPTSDRLQLLAGFEawdgkDANGIPILIKCQGKTTTDHISMAGP-WLKYRGHLDNISNNML 615
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 616 IGAVNAENGEAnkvknkftgeygavpatardyKARGvKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETN 695
Cdd:PRK07229 509 EGVDNTFPERA---------------------KEQG-GGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 696 LKKQGMLPLTFADPADYDKIQPEDTVDL--LCTELEvGKPMTLRVHPKNgstFDVKLNHTFNESQIEWFKDGSALNTMAR 773
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIedLREFLP-GGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
...
gi 3661614 774 KAA 776
Cdd:PRK07229 643 KLA 645
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
92-502 |
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: 841.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 92 RVACQDATAQMAILQFMSAGMPSVATPTTVHCDHLIEAQVGGEKDLARANEINKEVYDFLATATAKYNIGFWKPGSGIIH 171
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 172 QIVLENYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGL 251
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 252 LTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRQHIGEFARSYA-KELREDEGAE 330
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 331 YDQLIEINLSELEPHINGPFTPDLATPISKFKEAVDANGWPEELKVGLIGSCTNSSYEDMSRAASIARDALNHGVKSKSL 410
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 411 FTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGQWDRKDVKKGEPNSIISSYNRNFTGRNDANPATHAFVASP 490
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 3661614 491 DLVVAMCVAGTL 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: 804.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 60 LTYAEKVLYSHLD---DPHG---QDIE---------RGVSYLKLRPDRVACQDATAQMAILQFMSA--------GMPSV- 115
Cdd:COG1048 36 LPYSLKILLENLLrneDGETvteEDIKalanwlpkaRGDDEIPFRPARVLMQDFTGVPAVVDLAAMrdavarlgGDPKKi 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 116 --ATPTTVHCDHLIEAQVGG-----EKDLARANEINKEVYDFLATATAKY-NIGFWKPGSGIIHQIVLENYAFP------ 181
Cdd:COG1048 116 npLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVVPPGTGIVHQVNLEYLAFVvwtree 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 182 -------GGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTV 254
Cdd:COG1048 196 dgetvayPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 255 KGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKR--QHIgEFARSYAKE---LREDEGA 329
Cdd:COG1048 276 KGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRseEQI-ELVEAYAKAqglWRDPDAP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 330 E--YDQLIEINLSELEPHINGPFTPDLATPISKFKEA------------------VDANGWPEELK-----VGLIGSCTN 384
Cdd:COG1048 355 EpyYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAfraalaapvgeeldkpvrVEVDGEEFELGhgavvIAAITSCTN 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 385 SSYEDMSRAASI-ARDALNHG--VKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGQWDR------K 455
Cdd:COG1048 435 TSNPSVMIAAGLlAKKAVEKGlkVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisE 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 456 DVKKGE-PNSIISSYNRNFTGRNDaNPATHAFVASPDLVVAMCVAGTLKFNPLTDTV-KDKDGKEFKLAP--PSGDGLPS 531
Cdd:COG1048 515 AIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVVAYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 532 KG------------Y------DAGRNTYQAP-----PQDRASINVAVSPTSDRLQLLAGfeawDGKDANGIPILIKCQGK 588
Cdd:COG1048 594 AVfkavtpemfrarYadvfdgDERWQALEVPagelyDWDPDSTYIRRPPFFEGLQLEPE----PFKDIKGARVLAKLGDS 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 589 TTTDHISMAGP-----------------------WLKYRGHLDNISNNMLIGAV--N--AENGEANKVKNKFTGEYGAVP 641
Cdd:COG1048 670 ITTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFANIRikNllAPGTEGGYTKHQPTGEVMSIY 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 642 ATARDYKARGVKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDK--IQPED 719
Cdd:COG1048 750 DAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDE 829
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3661614 720 TVDL--LCTELEVGKPMTLRVHPKNGSTFDVKLNHTF-NESQIEWFKDGSALNTMARKAASN 778
Cdd:COG1048 830 TFDIegLDEGLAPGKTVTVTATRADGSTEEFPVLHRIdTPVEVEYYRAGGILQYVLRQLLAA 891
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
64-500 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 601.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 64 EKVLYSHLDDPHGQDIergvSYLklrPDRVACQDATAQMAILQFMSAGMP-----------SVATPTTVHCDHlieAQVG 132
Cdd:pfam00330 1 EKIWDAHLVEELDGSL----LYI---PDRVLMHDVTSPQAFVDLRAAGRAvrrpggtpatiDHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 133 GEKDLARANEINKEVYDFLATATAKYNIGFWKPGSGIIHQIVLEN-YAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAV 211
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 212 DVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATT 291
Cdd:pfam00330 151 HVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 292 SMFPFNDRMYDYLKATKRQH--IGE-FARSYA-KELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISK-----FK 362
Cdd:pfam00330 231 GLFPPDETTFEYLRATGRPEapKGEaYDKAVAwKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 363 EAVDA-------------NGWPE---ELKVGLIGSCTNSSYEDMSRAASIARDALNHGVKSKSL--FTVTPGSEQIRATI 424
Cdd:pfam00330 311 DAVKRkaaeraleymglgPGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPGvkASVVPGSEVVRAYA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3661614 425 ERDGQLQTLEEFGGVILANACGPCIGQWDRkdVKKGEpnSIISSYNRNFTGRNdaNPATHAFVASPDLVVAMCVAG 500
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNSDR--LPPGE--RCVSSSNRNFEGRQ--GPGGRTHLASPALVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
92-502 |
2.66e-140 |
|
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: 418.82 E-value: 2.66e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 92 RVACQDATAQMAILQFMSAGMPS-VATPTTVHCDHLIEAQVggekdlarANEINKEVYDFLATATAKYNIGFWKPGSGII 170
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGkVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 171 HQIVLENYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAG 250
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 251 LLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRQHIGEFARSYAKELREDEGAE 330
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 331 YDQLIEINLSELEPHINGPFTPDLATPISKFKEavdangwpEELKVGLIGSCTNSSYEDMSRAASIARDALnhgVKSKSL 410
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 411 FTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGQWDRkdvKKGEPNSIISSYNRNFTGRNDANPAtHAFVASP 490
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
gi 3661614 491 DLVVAMCVAGTL 502
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
61-723 |
1.01e-129 |
|
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: 400.90 E-value: 1.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 61 TYAEKVLYSHLDDphgQDIERGvSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTV-HCDHlieaqvggekDLAR 139
Cdd:TIGR01342 1 TLAEKIIDDHLVE---GDLEPG-EEIAIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAqYCDH----------NMLQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 140 ANEINKEVYDFLATATAKYNIGFWKPGSGIIHQIVLENYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPW 219
Cdd:TIGR01342 67 FDFKNADDHKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 220 ELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDR 299
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 300 MYDYLKATKRQHigEFArsyakELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISKFKEavdangwpEELKVGLI 379
Cdd:TIGR01342 227 TEAWLAAFDRED--DFV-----DLLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIAG--------IEVDQVMI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 380 GSCTNSSYEDMSRAASIARdalNHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGqwdrkdVKK 459
Cdd:TIGR01342 292 GSCTNGAFEDLLPAAKLLE---GREVHKDTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIG------IGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 460 GEPNSIIS--SYNRNFTGRNdANPATHAFVASPDLVVAMCVAGTLkFNP--LTDTVKDKDGKEFKLappsGDGLPSkGYD 535
Cdd:TIGR01342 363 APASDGVSlrSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPrdLADDEGDLEAIGFEM----GEKFPG-GYD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 536 AGrNTYQAPPQDRASINVAVSPTsdrLQLLAGFEAWdGKDANGiPILIKCQGKTTTDHISMAGP-WLKYRGHLDNISNNM 614
Cdd:TIGR01342 436 AA-DIDIIPKEEREDDDIIKGPN---IKPLPEFDPL-GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEFT 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 615 LigavnaengeaNKVKNKFTgeygavpATARDYKARGVKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHET 694
Cdd:TIGR01342 510 L-----------HRIDDEFA-------ERAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHA 571
|
650 660
....*....|....*....|....*....
gi 3661614 695 NLKKQGMLPLTFADPADYDKIQPEDTVDL 723
Cdd:TIGR01342 572 NLFNFGILPLEFDNEEDYAKFELGDDIEI 600
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
91-502 |
9.94e-115 |
|
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: 352.52 E-value: 9.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 91 DRVACQDATAQMAILQFMSAGMPSVATPTTV-HCDHLIeAQVGGEkdlaraneiNKEVYDFLATATAKYNIGFWKPGSGI 169
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVsYVDHNT-LQTDFE---------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 170 IHQIVLENYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVA 249
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 250 GLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRQhiGEFArsyakELREDEGA 329
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRE--DDWV-----ELAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 330 EYDQLIEINLSELEPHINGPFTPDLATPISKFkeavdangwpEELKVG--LIGSCTNSSYEDMSRAASIARDALnhgVKS 407
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPDNVVPVREV----------AGIKVDqvAIGSCTNSSYEDLMTVAAILKGRR---VHP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 408 KSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGqwdrkdVKKGEPNSIIS--SYNRNFTGRNdANPATHA 485
Cdd:cd01585 291 HVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIG------MGQAPPTGGVSvrTFNRNFEGRS-GTKDDLV 363
|
410
....*....|....*..
gi 3661614 486 FVASPDLVVAMCVAGTL 502
Cdd:cd01585 364 YLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
584-727 |
3.73e-101 |
|
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: 308.24 E-value: 3.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 584 KCQGKTTTDHISMAGPWLKYRGHLDNISNNMLIGAVNAENGEANKVKNKFTGEYGAVPATARDYKARGVKWVVIGDWNYG 663
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3661614 664 EGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKIQPEDTVDLLCTE 727
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLT 144
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
59-502 |
5.06e-87 |
|
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: 281.15 E-value: 5.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 59 PLTYAEKVLYSHLddphGQDIERGvSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATP--TTVHCDHLIEAqvggekd 136
Cdd:COG0065 2 GMTLAEKILARHA----GREVEPG-EIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPdrIVAVFDHNVPT------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 137 larANEINKEVYDFLATATAKYNIGFWKPGS-GIIHQIVLEN-YAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVM 214
Cdd:COG0065 70 ---KDPKSAEQVKTLREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 215 A-GLPWeLKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSM 293
Cdd:COG0065 147 AtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 294 FPFNDRMYDYLKatkrqhigefARSYA--KELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISKFKE-AVDangw 370
Cdd:COG0065 226 IAPDETTFEYLK----------GRPFApwRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGiKID---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 371 peelkVGLIGSCTNSSYEDMSRAASIARdalNHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIG 450
Cdd:COG0065 292 -----QVFIGSCTNGRIEDLRAAAEILK---GRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLG 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 3661614 451 -QWDRkdVKKGEpnSIISSYNRNFTGRNdANPATHAFVASPdLVVAMC-VAGTL 502
Cdd:COG0065 364 mNMGV--LAPGE--RCASTSNRNFEGRM-GSPGSRTYLASP-ATAAASaIAGRI 411
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
89-777 |
1.18e-85 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 290.30 E-value: 1.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 89 RPDRVACQDATAQMAILQFmsAGMPSVA-------------TPTTVHCDHLIEAQVGGEKDLARAN---EI--NKEVYDF 150
Cdd:PRK12881 82 VPARVVMQDFTGVPALVDL--AAMRDAAaeaggdpakinplVPVDLVVDHSVAVDYFGQKDALDLNmkiEFqrNAERYQF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 151 LATAT-AKYNIGFWKPGSGIIHQIVLE--------------NYAFPGgLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMA 215
Cdd:PRK12881 160 LKWGMqAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVML 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 216 GLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFP 295
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 296 FNDRMYDYLKATKR--QHIgEFARSYAKE--LREDEGAE--YDQLIEINLSELEPHINGPFTP-------DLATPISKFK 362
Cdd:PRK12881 319 VDEQTLDYLRLTGRteAQI-ALVEAYAKAqgLWGDPKAEprYTRTLELDLSTVAPSLAGPKRPqdrialgNVKSAFSDLF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 363 EAVDANGWPEE---------LKVG-----LIGSCTNSSyeD---MSRAASIARDALNHGVKSK-----SLftvTPGSEQI 420
Cdd:PRK12881 398 SKPVAENGFAKkaqtsngvdLPDGavaiaAITSCTNTS--NpsvLIAAGLLAKKAVERGLTVKpwvktSL---APGSKVV 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 421 RATIERDGQLQTLEEFGGVILANACGPCIGQWD------RKDVKKGE--PNSIISSyNRNFTGRNDANpATHAFVASPDL 492
Cdd:PRK12881 473 TEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGpltpeiEQAITKNDlvAAAVLSG-NRNFEGRIHPN-IKANFLASPPL 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 493 VVAMCVAGTLKFNPLTDTV-KDKDGKEFKLAP--PSG---DGLPSKGYDA---GRNTYQAPPQDR--ASINVAVSPT--- 558
Cdd:PRK12881 551 VVAYALAGTVRRDLMTEPLgKGKDGRPVYLKDiwPSSaeiDALVAFAVDPedfRKNYAEVFKGSElwAAIEAPDGPLydw 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 559 ---SDRLQLLAGFEAWDGkDANGIP------ILIKCQGKTTTDHIS---------MAGPWLKYRGHLDNISNN------- 613
Cdd:PRK12881 631 dpkSTYIRRPPFFDFSMG-PAASIAtvkgarPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNSygsrrgn 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 614 ---MLIGAVnaengeANK-VKNKF-------------TGEYGAVPATARDYKARGVKWVVIGDWNYGEGSSREHAALEPR 676
Cdd:PRK12881 710 hevMMRGTF------ANVrIKNLMipgkeggltlhqpSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTR 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 677 HLGGLAIITRSFARIHETNLKKQGMLPLTF--ADPADYDKIQPEDTVDL--LCTELEVGKPMTLRVHPKNGSTFDVKLN- 751
Cdd:PRK12881 784 LLGVKAVIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIegLPGEIKPRQDVTLVIHRADGSTERVPVLc 863
|
810 820
....*....|....*....|....*...
gi 3661614 752 --HTFNEsqIEWFKDGSALNTMARKAAS 777
Cdd:PRK12881 864 riDTPIE--VDYYKAGGILPYVLRQLLA 889
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
89-774 |
5.35e-85 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 288.56 E-value: 5.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 89 RPDRVACQDATAQMAI--LqfmsAGM---------------PSVatPTTVHCDHLIEAQVGGEKDLARAN-----EINKE 146
Cdd:PRK09277 83 RPARVVMQDFTGVPAVvdL----AAMrdaiadlggdpakinPLV--PVDLVIDHSVQVDYFGTPDAFEKNvelefERNEE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 147 VYDFLA-TATAKYNIGFWKPGSGIIHQIVLE-------------NYAFPGGLmIGTDSHTPNAGGLAMAAIGVGGADAVD 212
Cdd:PRK09277 157 RYQFLKwGQKAFDNFRVVPPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTTMINGLGVLGWGVGGIEAEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 213 VMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTS 292
Cdd:PRK09277 236 AMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 293 MFPFNDRMYDYLKATKR--QHIgEFARSYAKE----LREDEGAEYDQLIEINLSELEPHINGP-------FTPDLATPIS 359
Cdd:PRK09277 316 FFPIDEETLDYLRLTGRdeEQV-ALVEAYAKAqglwRDPLEEPVYTDVLELDLSTVEPSLAGPkrpqdriPLSDVKEAFA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 360 KFKEAVDANGWPEELKVGL-------------IGSCTNSSY-EDMSRAASIARDALNHGVKSK-----SLftvTPGSEQI 420
Cdd:PRK09277 395 KSAELGVQGFGLDEAEEGEdyelpdgavviaaITSCTNTSNpSVMIAAGLLAKKAVEKGLKVKpwvktSL---APGSKVV 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 421 RATIERDGQLQTLEEFGGVILANACGPCIGqwdrkdvkkgepNS----------IIS---------SYNRNFTGRndANP 481
Cdd:PRK09277 472 TDYLEKAGLLPYLEALGFNLVGYGCTTCIG------------NSgplppeiekaINDndlvvtavlSGNRNFEGR--IHP 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 482 -ATHAFVASPDLVVAMCVAGTLKFNPLTDTV-KDKDGKEFKLAppsgDGLPS------------------KGYDagrNTY 541
Cdd:PRK09277 538 lVKANYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLK----DIWPSdeeidavvakavkpemfrKEYA---DVF 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 542 QAPPQDRAsINVAVSPTSD---------RLQLLAGFEAWDG--KDANGIPILIKCQGKTTTDHISMAGP---------WL 601
Cdd:PRK09277 611 EGDERWNA-IEVPEGPLYDwdpdstyirNPPYFEGMLAEPGpvRDIKGARVLALLGDSITTDHISPAGAikadspagkYL 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 602 K-----------Y-----------RGHLDNIS--NNMLIGavnAENGEAnkvKNKFTGEYGAVPATARDYKARGVKWVVI 657
Cdd:PRK09277 690 LehgvepkdfnsYgsrrgnhevmmRGTFANIRirNEMVPG---VEGGYT---RHFPEGEVMSIYDAAMKYKEEGTPLVVI 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 658 GDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYD--KIQPEDTVDLLCTE-LEVGKPM 734
Cdd:PRK09277 764 AGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLEdLKPGATV 843
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 3661614 735 TLRVHPKNGS--TFDVKLN-HTFNEsqIEWFKDGSALNTMARK 774
Cdd:PRK09277 844 TVVITRADGEvvEFPVLCRiDTAVE--VDYYRNGGILQYVLRD 884
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
92-500 |
7.33e-80 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 260.97 E-value: 7.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 92 RVACQDATAQMAILQFMSAGMPSVATPTTVHC--DHLIEAqvggeKDLARANEINKEVYDFlatatAKYNIGFWKPG-SG 168
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT-----PDIKAAEQVKTLRKFA-----KEFGINFFDVGrQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 169 IIHQIVLENYAF-PGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMA-GLPWeLKAPKVIGVKLTGEMSGWTTPKDIIL 246
Cdd:cd01583 71 ICHVILPEKGLTlPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 247 KVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKatkrqhigEFARSYAKELRED 326
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLK--------GRGKAYWKELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 327 EGAEYDQLIEINLSELEPHINGPFTPDLATPISKFKeavdangwPEELKVGLIGSCTNSSYEDMSRAASIARDalnHGVK 406
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVE--------GIKIDQVFIGSCTNGRLEDLRAAAEILKG---RKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 407 SKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGqwdRKDVKKGEPNSIISSYNRNFTGRNdANPATHAF 486
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLG---GHMGVLAPGERCVSTSNRNFKGRM-GSPGARIY 366
|
410
....*....|....
gi 3661614 487 VASPDLVVAMCVAG 500
Cdd:cd01583 367 LASPATAAASAITG 380
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
59-500 |
2.41e-78 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 258.18 E-value: 2.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 59 PLTYAEKVLYSHLDDPH--GQDIERGVsylklrpDRVACQDATAQMAILQFMSAGMPSVATPTTVH--CDHLIEAqvgge 134
Cdd:PRK00402 2 GMTLAEKILARHSGRDVspGDIVEAKV-------DLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 135 KDLARAnEINKEVYDFlataTAKYNI-GFWKPGSGIIHQIVLEN-YAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVD 212
Cdd:PRK00402 70 KDIKSA-EQQKILREF----AKEQGIpNFFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 213 VMA-GLPWeLKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATT 291
Cdd:PRK00402 145 AMAtGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 292 SMFPFNDRMYDYLKatkrqhigEFARSYAKELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISKF-KEAVDangw 370
Cdd:PRK00402 224 GIFAPDEKTLEYLK--------ERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVeGTKVD---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 371 peelkVGLIGSCTNSSYEDMSRAASIARDalnHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIG 450
Cdd:PRK00402 292 -----QVFIGSCTNGRLEDLRIAAEILKG---RKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLG 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 3661614 451 qwdrkdvkKGEpnSIISSYNRNFTGRNdANPATHAFVASPDLVVAMCVAG 500
Cdd:PRK00402 364 ghmg-vlaPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
90-774 |
6.18e-75 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 261.10 E-value: 6.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 90 PDRVACQDATAQMAILQF--------MSAGMPSV---ATPTTVHCDHLIEAQVGGEKDLARANEI-----NKEVYDFLA- 152
Cdd:PTZ00092 90 PARVLLQDFTGVPAVVDLaamrdamkRLGGDPAKinpLVPVDLVIDHSVQVDFSRSPDALELNQEieferNLERFEFLKw 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 153 TATAKYNIGFWKPGSGIIHQIVLE----------NYAFPGGLmIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELK 222
Cdd:PTZ00092 170 GSKAFKNLLIVPPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 223 APKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYD 302
Cdd:PTZ00092 249 LPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 303 YLKATKR-QHIGEFARSYAKELR----EDEGAEYDQLIEINLSELEPHINGP---------------FTPDLATPIS--- 359
Cdd:PTZ00092 329 YLKQTGRsEEKVELIEKYLKANGlfrtYAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGfkg 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 360 ------------KF----KEAVDANGwpeELKVGLIGSCTNSSYED-MSRAASIARDALNHGVKSKSLF--TVTPGSEQI 420
Cdd:PTZ00092 409 fgipeekhekkvKFtykgKEYTLTHG---SVVIAAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPYIktSLSPGSKVV 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 421 RATIERDGQLQTLEEFGGVILANACGPCIGQWDRKDVkkgEPNSIIS----------SYNRNFTGRndANPATHA-FVAS 489
Cdd:PTZ00092 486 TKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDP---EVSEAITnndlvaaavlSGNRNFEGR--VHPLTRAnYLAS 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 490 PDLVVAMCVAGTLKFNPLTDTV-KDKDGKEFKLAppsgDGLPSKGY-----------DAGRNTYQAPPQDRASINVAVSP 557
Cdd:PTZ00092 561 PPLVVAYALAGRVNIDFETEPLgSDKTGKPVFLR----DIWPSREEiqaleakyvkpEMFKEVYSNITQGNKQWNELQVP 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 558 TSDrlqllagFEAWDGK---------------DANGI-PI-----LIKCQGKTTTDHISMAG------PWLKY------- 603
Cdd:PTZ00092 637 KGK-------LYEWDEKstyihnppffqtmelEPPPIkSIenaycLLNLGDSITTDHISPAGniaknsPAAKYlmergve 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 604 ------------------RGHLDNIS-NNMLIGAVNaengeANKVKNKfTGEYGAVPATARDYKARGVKWVVIGDWNYGE 664
Cdd:PTZ00092 710 rkdfntygarrgndevmvRGTFANIRlINKLCGKVG-----PNTVHVP-TGEKMSIYDAAEKYKQEGVPLIVLAGKEYGS 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 665 GSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKI----QPEDTVDLLCTELEVGKPMTLRVhp 740
Cdd:PTZ00092 784 GSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSLgltgKEQFSIDLNSGELKPGQDVTVKT-- 861
|
810 820 830
....*....|....*....|....*....|....
gi 3661614 741 KNGSTFDVKLNHTfNESQIEWFKDGSALNTMARK 774
Cdd:PTZ00092 862 DTGKTFDTILRID-TEVEVEYFKHGGILQYVLRK 894
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
89-774 |
5.83e-67 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 239.32 E-value: 5.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 89 RPDRVACQDATAQMAI--LQFMSAGMPSVA---------TPTTVHCDHLIEAQVGGEKDLARAN-----EINKEVYDFLA 152
Cdd:PLN00070 121 KPARVLLQDFTGVPAVvdLACMRDAMNNLGgdpnkinplVPVDLVIDHSVQVDVARSENAVQANmelefQRNKERFAFLK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 153 -TATAKYNIGFWKPGSGIIHQIVLENYA----------FPGGLmIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWEL 221
Cdd:PLN00070 201 wGSTAFQNMLVVPPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 222 KAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMY 301
Cdd:PLN00070 280 VLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 302 DYLKATKRQH-----IGEFARS------YAKELREDEgaeYDQLIEINLSELEPHINGPFTPDLATPISKF--------- 361
Cdd:PLN00070 360 QYLKLTGRSDetvamIEAYLRAnkmfvdYNEPQQERV---YSSYLELDLEDVEPCISGPKRPHDRVPLKEMkadwhscld 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 362 -----------KEAVDA------NGWPEELKVG-----LIGSCTNSSYED-MSRAASIARDALNHGVKSKSLF--TVTPG 416
Cdd:PLN00070 437 nkvgfkgfavpKEAQSKvakfsfHGQPAELRHGsvviaAITSCTNTSNPSvMLGAGLVAKKACELGLEVKPWIktSLAPG 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 417 SEQIRATIERDGQLQTLEEFGGVILANACGPCIG---QWDRKDVKKGEPNSIIS----SYNRNFTGRndANPATHA-FVA 488
Cdd:PLN00070 517 SGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGnsgELDESVASAITENDIVAaavlSGNRNFEGR--VHPLTRAnYLA 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 489 SPDLVVAMCVAGTLKFNPLTDTV-KDKDGKE--FKLAPPSGDG---------LPskgyDAGRNTYQAPPQDRASINVAVS 556
Cdd:PLN00070 595 SPPLVVAYALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEvaevvqssvLP----DMFKSTYEAITKGNPMWNQLSV 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 557 PTSDRLqllagfeAWDGKD------------------ANGIP---ILIKCQGKTTTDHISMAG------PWLKY------ 603
Cdd:PLN00070 671 PSGTLY-------SWDPKStyiheppyfknmtmsppgPHGVKdayCLLNFGDSITTDHISPAGsihkdsPAAKYlmergv 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 604 -------------------RGHLDNIS--NNMLIGAVNAengeanKVKNKFTGEYGAVPATARDYKARGVKWVVIGDWNY 662
Cdd:PLN00070 744 drkdfnsygsrrgndeimaRGTFANIRivNKLLKGEVGP------KTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEY 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 663 GEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKI----QPEDTVDLLCTELEVGKPMTLRV 738
Cdd:PLN00070 818 GSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLgltgHERYTIDLPSNISEIKPGQDVTV 897
|
810 820 830
....*....|....*....|....*....|....*.
gi 3661614 739 HPKNGSTFDVKLNHTfNESQIEWFKDGSALNTMARK 774
Cdd:PLN00070 898 TTDNGKSFTCTLRFD-TEVELAYFDHGGILPYVIRN 932
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
124-501 |
8.22e-56 |
|
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: 197.14 E-value: 8.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 124 DHLIEAQVGGEKDLARAN-----EINKEVYDFLATATAKY-NIGFWKPGSGIIHQIVLE--------------NYAFPGG 183
Cdd:cd01586 44 DHSVQVDFYGTADALAKNmklefERNRERYEFLKWGQKAFkNLRVVPPGTGIIHQVNLEylarvvftseedgdGVAYPDS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 184 LmIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIE 263
Cdd:cd01586 124 V-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 264 YHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNdrmydylkatkrqhigefarsyakelredegaeyDQLIEINLSELE 343
Cdd:cd01586 203 FFGPGVAKLSVADRATIANMAPEYGATCGFFPVD----------------------------------TQVVELDLSTVE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 344 PHINGPFTPDlatpiskfkEAVDANGwpeELKVGLIGSCTNSSYED-MSRAASIARDALNHGVKSKSLF--TVTPGSEQI 420
Cdd:cd01586 249 PSVSGPKRPQ---------DRVPLHG---SVVIAAITSCTNTSNPSvMLAAGLLAKKAVELGLKVKPYVktSLAPGSRVV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 421 RATIERDGQLQTLEEFGGVILANACGPCIG------QWDRKDVKKGE--PNSIISSyNRNFTGRndANPATHA-FVASPD 491
Cdd:cd01586 317 TKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpEEVEEAIKENDlvVAAVLSG-NRNFEGR--IHPLVRAnYLASPP 393
|
410
....*....|
gi 3661614 492 LVVAMCVAGT 501
Cdd:cd01586 394 LVVAYALAGT 403
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
580-709 |
5.17e-53 |
|
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: 179.87 E-value: 5.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 580 PILIKCQGKTTTDHISMAGPWLKYRGHLDNISNNMLIGAVNAENGEANKVKNKFTGEYGAVPATARDYKARGVKWVVIGD 659
Cdd:pfam00694 2 PVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIGG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 3661614 660 WNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADP 709
Cdd:pfam00694 82 KNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
140-502 |
1.90e-43 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 163.75 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 140 ANEINKEVYDFLATATAKYNIGFWKPGS---GIIHQIVLENYA-FPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMA 215
Cdd:PRK05478 75 ADPVSRIQVETLEKNCKEFGITLFDLGDprqGIVHVVGPEQGLtLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 216 G--LPweLKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSM 293
Cdd:PRK05478 155 TqtLL--QKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 294 FPFNDRMYDYLKATKRQHIGEF---ARSYAKELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPIS-------KFKE 363
Cdd:PRK05478 233 VAPDETTFEYLKGRPFAPKGEDwdkAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDgkvpdpeDFAD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 364 AVDANGWPEELK-VGL---------------IGSCTNSSYEDMSRAASIARDalnHGVKSKSLFTVTPGSEQIRATIERD 427
Cdd:PRK05478 313 PVKRASAERALAyMGLkpgtpitdikidkvfIGSCTNSRIEDLRAAAAVVKG---RKVAPGVRALVVPGSGLVKAQAEAE 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 428 GQLQTLEEFG------GvilanaCGPCIGQWDRKdVKKGEpnSIISSYNRNFTGRNDANPATHafVASPDLVVAMCVAGT 501
Cdd:PRK05478 390 GLDKIFIEAGfewrepG------CSMCLAMNPDK-LPPGE--RCASTSNRNFEGRQGKGGRTH--LVSPAMAAAAAITGH 458
|
.
gi 3661614 502 L 502
Cdd:PRK05478 459 F 459
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
165-502 |
2.57e-41 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 157.76 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 165 PGSGIIHQIVLE-NYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKD 243
Cdd:PRK12466 105 PRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 244 IILKVAGLLTVKGGTGAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRQHIG---EFARSYA 320
Cdd:PRK12466 185 LILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKGalwDAALAYW 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 321 KELREDEGAEYDQLIEINLSELEPHINGPFTPDLATPIS-------KFKEAVDANGWPEELK-VGL-------------- 378
Cdd:PRK12466 265 RTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpaAEADPARRAAMERALDyMGLtpgtplagipidrv 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 379 -IGSCTNSSYEDMSRAASIARDalnHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGQWDRKdV 457
Cdd:PRK12466 345 fIGSCTNGRIEDLRAAAAVLRG---RKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV-L 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 3661614 458 KKGEpnSIISSYNRNFTGRNDANPATHafVASPDLVVAMCVAGTL 502
Cdd:PRK12466 421 APGE--RCASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAGHI 461
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
104-502 |
3.68e-40 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 152.00 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 104 ILQFMSAGMPSVATPTTVHC--DHlieaqvggekDLARANEINKEVYDFLATATAKYNIGFWKPGSGIIHQIVLEN-YAF 180
Cdd:cd01582 12 ALKFMSIGATKIHNPDQIVMtlDH----------DVQNKSEKNLKKYKNIESFAKKHGIDFYPAGRGIGHQIMIEEgYAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 181 PGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMA-GLPWeLKAPKVIGVKLTGEMSGWTTPKDIILKVAGLLTVKGGTG 259
Cdd:cd01582 82 PGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 260 AIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNdrmydylkatkrqhigefarsyAKELRedegaeydqlieINL 339
Cdd:cd01582 161 HAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD----------------------AKHLI------------LDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 340 SELEPHINGPFTPDLATPISKFkEAVDAngwpeELKVGLIGSCTNSSYEDMSRAASIARDA--------LNHGVKskslF 411
Cdd:cd01582 207 STLSPYVSGPNSVKVSTPLKEL-EAQNI-----KINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGVE----F 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 412 TVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGqwdrkdVKKG--EPNSI-ISSYNRNFTGRNdANPATHAFVA 488
Cdd:cd01582 277 YVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG------LGQGllEPGEVgISATNRNFKGRM-GSTEALAYLA 349
|
410
....*....|....
gi 3661614 489 SPDLVVAMCVAGTL 502
Cdd:cd01582 350 SPAVVAASAISGKI 363
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
86-714 |
6.03e-33 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 136.29 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 86 LKLRPDRVACQDATAqMAILQFMSA-GMPSVATPTTVHCDHLIEAQVGGEkdlaraneINKEVYDFLATATAKYNIGFWK 164
Cdd:PRK11413 54 LKIKFDSLASHDITF-VGIIQTAKAsGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGIFVP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 165 PGSGIIHQIVLENYAFPGGLMIGTDSHTpNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDI 244
Cdd:PRK11413 125 PHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 245 ILKVAGLLTVKGGT-GAIIEYHGPGVNSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRqhigefARSYaKEL 323
Cdd:PRK11413 204 ALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGR------GQDY-CEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 324 REDEGAEYDQLIEINLSELEPHINGPFTPDLATPISKFKE-------------AVDANGWPE----------ELKV--GL 378
Cdd:PRK11413 277 NPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQnltdilreveiesERVAHGKAKlslldkiengRLKVqqGI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 379 IGSCTNSSYEDMSRAASIARDalnHGVKSKSL-FTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGPCIGQWDrkdv 457
Cdd:PRK11413 357 IAGCSGGNYENVIAAANALRG---QSCGNDTFsLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGD---- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 458 kkgEPN----SIISSyNRNFTGRNDANPATHAfVASPDLVVAMCVAGTLKFNPLTDTVKDKDGKEFKLAppsgdglpskg 533
Cdd:PRK11413 430 ---TPAnnglSIRHT-TRNFPNREGSKPANGQ-MSAVALMDARSIAATAANGGYLTSATELDCWDNVPE----------- 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 534 YDAGRNTYQAppqdRASINVAVSPTSDRLQLLAGFEAWDGKDANGIPILIKCQGK-----TTTDHISMAGPWLKYRghld 608
Cdd:PRK11413 494 YAFDVTPYKN----RVYQGFGKGATQQPLIYGPNIKDWPEMGALTDNILLKVCSKildpvTTTDELIPSGETSSYR---- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 609 niSNNMLIG----------------AVNA-----ENGEANKVKNKFtgeygAVPATARDYKARGVKWVVIGDWNY----G 663
Cdd:PRK11413 566 --SNPLGLAeftlsrrdpgyvgrskAVAElenqrLAGNVSELTEVF-----ARIKQIAGQEHIDPLQTEIGSMVYavkpG 638
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 3661614 664 EGSSREHAALEPRHLGGLAIITRSFA-RIHETNLKKQGMLPLTFADPADYDK 714
Cdd:PRK11413 639 DGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEEPTFEV 690
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
584-723 |
2.77e-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: 107.14 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 584 KCQGKTTTDHISMAGP-WLKYRGHLDNISnnmligavnaengeankvknKFTGEYgAVPATARDYKARGVKWVVIGDwNY 662
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAIS--------------------EFVFHR-VDPTFAERAKAAGPGFIVGGE-NY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3661614 663 GEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKIQPEDTVDL 723
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLEL 119
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
654-723 |
2.76e-23 |
|
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: 94.46 E-value: 2.76e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 654 WVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKIQPEDTVDL 723
Cdd:cd00404 17 GVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDI 86
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
588-724 |
4.08e-17 |
|
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: 79.63 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 588 KTTTDHISMAG------PWLKY-------------------------RGHLDNISN-NMLigavnAENGEANKVKNKFTG 635
Cdd:cd01580 5 SVTTDHISPAGsiakdsPAGKYlaergvkprdfnsygsrrgndevmmRGTFANIRLrNKL-----VPGTEGGTTHHPPTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 636 EYGAVPATARDYKARGVKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADP--ADYD 713
Cdd:cd01580 80 EVMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSL 159
|
170
....*....|.
gi 3661614 714 KIQPEDTVDLL 724
Cdd:cd01580 160 GLTGEETYDII 170
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
164-502 |
1.85e-12 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 70.22 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 164 KPGSGIIHQiVLENYAFPGGLMIGTDSHTPNAGGLAMAAIG--VGGADAVDVMAglpweLKAPKVIGVKLTGEMSGWTTP 241
Cdd:cd01581 90 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTRFPIGISFPAGSglVAFAAATGVMP-----LDMPESVLVRFKGKMQPGITL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 242 KDIILKV------AGLLTV--KGG----TGAIIEYHGpgVNSLSCTGMGTICNMGAEIGATTSMFPFNDR-MYDYLKATK 308
Cdd:cd01581 164 RDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEpVIEYLESNV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 309 RQHIGEFARSY-----------AKE--------LREDEGAEYDQLIEINLSEL-EPHINGPFTPDLATPISkfkEAVDAN 368
Cdd:cd01581 242 VLMKIMIANGYddartllrriiAMEewlanpplLEPDADAEYAAVIEIDLDDIkEPILACPNDPDDVKLLS---EVAGKK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 369 gwpeeLKVGLIGSC-TNSSyeDMSRAASIARDALNhgvkSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANACGP 447
Cdd:cd01581 319 -----IDEVFIGSCmTNIG--HFRAAAKILRGKEF----KPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSL 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 3661614 448 CIGQWDRkdVKKGEpnSIISSYNRNFTGR--NDANpathAFVASPDLVVAMCVAGTL 502
Cdd:cd01581 388 CMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
655-723 |
3.97e-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: 59.91 E-value: 3.97e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3661614 655 VVIGDwNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKIQPED---TVDL 723
Cdd:cd01577 21 IVAGK-NFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGdevEVDL 91
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
164-497 |
5.22e-10 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 62.89 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 164 KPGSGIIHQiVLENYAFPGGLMIGTDSHT--------PNAGGLamaaigVGGADAVDVMAglpweLKAPKVIGVKLTGEM 235
Cdd:PRK09238 462 RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGEM 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 236 SGWTTPKDI---ILKVA---GLLTV--KGG----TGAIIEYHGpgVNSLSCTGMGTICNMGAEIGATTSMFPFND-RMYD 302
Cdd:PRK09238 530 QPGITLRDLvhaIPYYAikqGLLTVekKGKknifSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKePIIE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 303 YLKATK---RQHIGEF---ARSYAKE-------------LREDEGAEYDQLIEINLSEL-EPHINGPFTPDLATPISKFK 362
Cdd:PRK09238 608 YLRSNIvllKWMIAEGygdARTLERRiaameewlanpelLEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLSEVA 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 363 EavdangwpEELKVGLIGSC-TNssYEDMSRAASIARdalNHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVIL 441
Cdd:PRK09238 688 G--------TKIDEVFIGSCmTN--IGHFRAAGKLLE---GKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIE 754
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 3661614 442 ANACGPCIGQWDRkdVKKGEpnSIISSYNRNFTGR--NDANpathAFVASPDLvVAMC 497
Cdd:PRK09238 755 MPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKGAN----VYLGSAEL-AAVC 803
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
655-723 |
6.86e-09 |
|
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: 56.33 E-value: 6.86e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3661614 655 VVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTfADPADYDKI------QPED--TVDL 723
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDelTVDL 142
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
655-743 |
1.62e-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: 54.35 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 655 VVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGmLPLTFAdPADYDKIQPEDTVDLLCTELEVGKPM 734
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIG-LPLIEA-KTEGIKDGDEVTVDLETGEIRVNGNE 127
|
....*....
gi 3661614 735 TLRVHPKNG 743
Cdd:TIGR02087 128 EYKGEPLPD 136
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
655-723 |
1.87e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 54.45 E-value: 1.87e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3661614 655 VVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGmLPLtFADPADYDKIQPEDTVDL 723
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV-LECDEAVDKIEDGDEVEV 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
655-731 |
1.44e-07 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 51.73 E-value: 1.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3661614 655 VVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPltFADPADYDKIQPEDTVDLlctELEVG 731
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDEVEL---DLETG 123
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
164-502 |
6.47e-07 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 53.00 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 164 KPGSGIIHQIvLENYAFPGGLMIGTDSHTPNAGGLAMAA----IGVGGADAVdvmagLPweLKAPKVIGVKLTGEMSGWT 239
Cdd:PLN00094 536 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTRFPIGISFPAgsglVAFGAATGV-----IP--LDMPESVLVRFTGTMQPGI 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 240 TPKDIILKV------AGLLTV-KGG-----TGAIIEYHGpgVNSLSCTGMGTICNMGAEIGATTSMFPFNDR-MYDYLKA 306
Cdd:PLN00094 608 TLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEpIIEYLNS 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 307 -----------------TKRQHIGEFARSYA--KELREDEGAEYDQLIEINLSEL-EPHINGPFTPDLATPISKFK-EAV 365
Cdd:PLN00094 686 nvvmlkwmiaegygdrrTLERRIARMQQWLAdpELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTgDKI 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 366 DangwpeELkvgLIGSC-TNSSYedmSRAAsiARDALNHGVKSKSLFTVTPGSEQIRATIERDGQLQTLEEFGGVILANA 444
Cdd:PLN00094 766 D------EV---FIGSCmTNIGH---FRAA--GKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPG 831
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 3661614 445 CGPCIGQWDRkdvkKGEPNSIISSYNRNFTGRndANPATHAFVASPDLVVAMCVAGTL 502
Cdd:PLN00094 832 CSLCMGNQAR----VAEKSTVVSTSTRNFPNR--LGKGANVYLASAELAAVAAILGRL 883
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
661-723 |
5.94e-06 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 47.81 E-value: 5.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3661614 661 NYGEGSSREHA--ALEprHLGGLAIITRSFARIHETNLKKQGMLPLTfADPADYDKIQ------PED--TVDL 723
Cdd:PRK01641 76 NFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELFklveanPGAelTVDL 145
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
650-737 |
1.69e-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: 43.27 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 650 RGVKWVVIGDwNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFADPADYDKIQP------EDTVDL 723
Cdd:TIGR00171 68 QGASILLARE-NFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQvenqglQMTVDL 146
|
90
....*....|....
gi 3661614 724 LCTELEVGKPMTLR 737
Cdd:TIGR00171 147 ENQLIHDSEGKVYS 160
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
655-753 |
1.30e-03 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 41.38 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3661614 655 VVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGmlpltfadpadydKIQPEDTVDLLCTELEVGKPM 734
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATG-------------EVYPLESEVRICEECKTGDVV 198
|
90
....*....|....*....
gi 3661614 735 TLRVHPkngstfDVKLNHT 753
Cdd:PLN00072 199 TVELGN------SVLINHT 211
|
|
| |
