|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
35-782 |
0e+00 |
|
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle]
Pssm-ID: 273561 [Multi-domain] Cd Length: 745 Bit Score: 1459.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 35 YAKLLTNLDKIKQITNNAPLTLAEKILYSHLCDPEESITSSDLSTIRGNKYLKLNPDRVAMQDASAQMALLQFMTTGLNQ 114
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNSRPLTLAEKILYSHLDDPEESLLSQDIGDVRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 115 TSVPASIHCDHLIVGKDGETKDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLENFSAPGLMMLGTDSHTPN 194
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 195 AGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSC 274
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 275 TGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFT 354
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSFFKLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 355 PDLSTPISQYAEKSLKENWPQKVSAGLIGSCTNSSYQDMSRVVDLVKQASKAGLKPRIPFFVTPGSEQIRATLERDGIID 434
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 435 IFQENGAKVLANACGPCIGQWNREDVsKTSKETNTIFTSFNRNFRARNDGNRNTMNFLTSPEIVTAMSYSGDAQFNPLTD 514
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDD-VKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 515 SIKLPNGKDFKFQPPKGDELPKRGFEHGRDKFYPEMDPkPDSNVEIKVDPNSDRLQLLEPFKPWNGKELK-TNVLLKVEG 593
Cdd:TIGR01340 480 SLTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGS-PNPNVEVAVSPSSDRLQLLEPFEPWNGKDLSgLRVLIKVTG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 594 KCTTDHISAAGVWLKYKGHLENISYNTLIGAQNKETGEVNKAYDLDGTEYDIPGLMMKWKSDGRPWTVIAEHNYGEGSAR 673
Cdd:TIGR01340 559 KCTTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYDLDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSAR 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 674 EHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLETLNLVDMIAkdGNNGGEIDVKITKPN 753
Cdd:TIGR01340 639 EHAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLK--NGGGGEVDLRVTKKN 716
|
730 740
....*....|....*....|....*....
gi 547592 754 GESFTIKAKHTMSKDQIDFFKAGSAINYI 782
Cdd:TIGR01340 717 GKVFEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
53-782 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 854.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 53 PLTLAEKILYSHLCDPEesitssdlsTIRGnKYLKLNPDRVAMQDASAQMALLQFMTTGLNQTSVPASI-HCDHlivgkd 131
Cdd:PRK07229 2 GLTLTEKILYAHLVEGE---------LEPG-EEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 132 getkDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAV 211
Cdd:PRK07229 66 ----NLLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 212 DALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATT 291
Cdd:PRK07229 142 LAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 292 STFPYQEAHKRYLQATNRAEVaeaadvalnkFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEKslke 371
Cdd:PRK07229 222 SIFPSDERTREFLKAQGREDD----------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGI---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 372 nwpqKVSAGLIGSCTNSSYQDMSRVVDLVKqasKAGLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPC 451
Cdd:PRK07229 288 ----KVDQVLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPC 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 452 IGqwnrEDVSKTSKetNTIFTSFNRNFRARNdGNRNTMNFLTSPEIVTAMSYSGDAQfNPLTDsiKLPNGKDFKFQPPKG 531
Cdd:PRK07229 361 IG----MGQAPATG--NVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRTL--ALENGEYPKLEEPEG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 532 DELPKRGFEhgrdkfYPemdPKPDSNVEIKVDPNSDRLQLLEPFKpwNGKELKtnVLLKVEGKCTTDHISAAGV-WLKYK 610
Cdd:PRK07229 431 FAVDDAGII------AP---AEDGSDVEVVRGPNIKPLPLLEPLP--DLLEGK--VLLKVGDNITTDHIMPAGAkWLPYR 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 611 GHLENISYNTLIGAQNKETGEVnkaydldgteydipglmmkWKSDGrpWTVIAEHNYGEGSAREHAALSPRFLGGEILLV 690
Cdd:PRK07229 498 SNIPNISEFVFEGVDNTFPERA-------------------KEQGG--GIVVGGENYGQGSSREHAALAPRYLGVKAVLA 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 691 KSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLETLNLVDMIAkdgnnGGEIDVKITKPNgesFTIKAKHTMSKDQI 770
Cdd:PRK07229 557 KSFARIHKANLINFGILPLTFADPADYDKIEEGDVLEIEDLREFLP-----GGPLTVVNVTKD---EEIEVRHTLSERQI 628
|
730
....*....|..
gi 547592 771 DFFKAGSAINYI 782
Cdd:PRK07229 629 EILLAGGALNLI 640
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
92-506 |
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: 709.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 92 RVAMQDASAQMALLQFMTTGLNQTSVPASIHCDHLIVGKDGETKDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIH 171
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 172 QIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGL 251
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 252 LTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADValNKFNFLRADKD 331
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADE--FKDDLLVADEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 332 AQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEKSLKENWPQKVSAGLIGSCTNSSYQDMSRVVDLVKQASKAGLKPR 411
Cdd:cd01584 239 AEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 412 IPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNREDVSKtsKETNTIFTSFNRNFRARNDGNRNTMNF 491
Cdd:cd01584 319 SIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKK--GEKNTIVTSYNRNFTGRNDANPATHAF 396
|
410
....*....|....*
gi 547592 492 LTSPEIVTAMSYSGD 506
Cdd:cd01584 397 VASPEIVTAMAIAGT 411
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
54-782 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 683.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 54 LTLAEKILYSHL---CDPEeSITSSDLSTI-------RGNKYLKLNPDRVAMQDASAQMALLQFMTTGLNQTS------- 116
Cdd:COG1048 36 LPYSLKILLENLlrnEDGE-TVTEEDIKALanwlpkaRGDDEIPFRPARVLMQDFTGVPAVVDLAAMRDAVARlggdpkk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 117 ----VPASIHCDHLIV-----GKDGETKDLPSSIATNQEVFDFLESCAKRY-GIQFWGPGSGIIHQIVLENFS------- 179
Cdd:COG1048 115 inplVPVDLVIDHSVQvdyfgTPDALEKNLELEFERNRERYQFLKWGQQAFdNFRVVPPGTGIVHQVNLEYLAfvvwtre 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 180 ------APGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLT 253
Cdd:COG1048 195 edgetvAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 254 VRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRAD---K 330
Cdd:COG1048 275 KKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIELVEAYAKAQGLWRDpdaP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 331 DAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEK------SLKENWPQK-----------------VSAGLIGSCTN 387
Cdd:COG1048 355 EPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAfraalaAPVGEELDKpvrvevdgeefelghgaVVIAAITSCTN 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 388 SSYQDMSRVVDLV-KQASKAGL--KPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNR--EDVSK 462
Cdd:COG1048 435 TSNPSVMIAAGLLaKKAVEKGLkvKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlpPEISE 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 463 TSKE---TNTIFTSFNRNFRARNdGNRNTMNFLTSPEIVTAMSYSGDAQFNPLTDSI-KLPNGKDFKFQP--PKGDELPK 536
Cdd:COG1048 515 AIEEndlVVAAVLSGNRNFEGRI-HPDVKANFLASPPLVVAYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 537 RGFEHGRDKFY-------------------PEMD--PKPDSNVEIKVDPNSDRLQLL-EPFKPWNGkeLKtnVLLKVEGK 594
Cdd:COG1048 594 AVFKAVTPEMFraryadvfdgderwqalevPAGElyDWDPDSTYIRRPPFFEGLQLEpEPFKDIKG--AR--VLAKLGDS 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 595 CTTDHISAAG-----------------------VWLKYKGHLENISYNTLIG-------AQNKETGEVNkaYDLDGTEYD 644
Cdd:COG1048 670 ITTDHISPAGaikadspagryllehgvepkdfnSYGSRRGNHEVMMRGTFANiriknllAPGTEGGYTK--HQPTGEVMS 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 645 IPGLMMKWKSDGRPWTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKIS-SG 723
Cdd:COG1048 748 IYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESLGlTG 827
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 724 DvlETLNLVDmIAKDGNNGGEIDVKITKPNGESFTIKAKHTM-SKDQIDFFKAGSAINYI 782
Cdd:COG1048 828 D--ETFDIEG-LDEGLAPGKTVTVTATRADGSTEEFPVLHRIdTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
58-505 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 575.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 58 EKILYSHLCDPEESITSsdlstirgnkYLklnPDRVAMQDASAQMALLQFMTTGLNQ-----------TSVPASIHCDHl 126
Cdd:pfam00330 1 EKIWDAHLVEELDGSLL----------YI---PDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 127 ivGKDGETKDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLEN-FSAPGLMMLGTDSHTPNAGGLGAIAIGV 205
Cdd:pfam00330 67 --APDALDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTTHGGLGALAFGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 206 GGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGA 285
Cdd:pfam00330 145 GGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 286 EIGATTSTFPYQEAHKRYLQATNRAEVAEAAD-VALNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQ- 363
Cdd:pfam00330 225 EYGATAGLFPPDETTFEYLRATGRPEAPKGEAyDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSEl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 364 ------------YAEKS-----LKENWPQ---KVSAGLIGSCTNSSYQDMSRVVDLVKQASKAGLK--PRIPFFVTPGSE 421
Cdd:pfam00330 305 vpdpfadavkrkAAERAleymgLGPGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKvaPGVKASVVPGSE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 422 QIRATLERDGIIDIFQENGAKVLANACGPCIGQWNRedvsktSKETNTIFTSFNRNFRARNdgNRNTMNFLTSPEIVTAM 501
Cdd:pfam00330 385 VVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDR------LPPGERCVSSSNRNFEGRQ--GPGGRTHLASPALVAAA 456
|
....
gi 547592 502 SYSG 505
Cdd:pfam00330 457 AIAG 460
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
55-789 |
5.91e-142 |
|
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized. [Energy metabolism, TCA cycle]
Pssm-ID: 130409 [Multi-domain] Cd Length: 658 Bit Score: 433.26 E-value: 5.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 55 TLAEKILYSHLCD----PEESITssdlstirgnkylkLNPDRVAMQDASAQMALLQFMTTGLN--QTSVPASiHCDHLIV 128
Cdd:TIGR01342 1 TLAEKIIDDHLVEgdlePGEEIA--------------IEIDQTLSQDATGTMCWLEFEALEMDevKTELAAQ-YCDHNML 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 129 GKDGEtkdlpssiatNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGA 208
Cdd:TIGR01342 66 QFDFK----------NADDHKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 209 DAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIG 288
Cdd:TIGR01342 136 DIAAAMAGEAFYLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 289 ATTSTFPYQEAHKRYLQATNRAevaeaadvalNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEks 368
Cdd:TIGR01342 216 ATSSIFPSDDITEAWLAAFDRE----------DDFVDLLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIAG-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 369 lkenwpQKVSAGLIGSCTNSSYQDMSRVVDLVKQASkagLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANAC 448
Cdd:TIGR01342 284 ------IEVDQVMIGSCTNGAFEDLLPAAKLLEGRE---VHKDTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAAC 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 449 GPCIGqwnredVSKTSKETNTIFTSFNRNFRARNdGNRNTMNFLTSPEIVTAMSYSGDaqfnpLTDSIKLpnGKDFKFQP 528
Cdd:TIGR01342 355 GACIG------IGFAPASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGE-----IIDPRDL--ADDEGDLE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 529 PKGDELPKRgFEHGRDK-FYPEMDPKPDSNVEIKVDPNSDRLQLLEPFkpwnGKELKTNVLLKVEGKCTTDHISAAGV-W 606
Cdd:TIGR01342 421 AIGFEMGEK-FPGGYDAaDIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEGETALIMEDNITTDHIIPAGAdI 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 607 LKYKGHLENISyntligaqnketgevnkAYDLDGTEYDIPGLMMKWKSDGRPWTVIAEHNYGEGSAREHAALSPRFLGGE 686
Cdd:TIGR01342 496 LKFRSNIEAIS-----------------EFTLHRIDDEFAERAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVE 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 687 ILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLETLNLVDMIAKDgnngGEIDVKITKPNGESFTikAKHTMS 766
Cdd:TIGR01342 559 AVIAKSFARIHHANLFNFGILPLEFDNEEDYAKFELGDDIEIPDDLAAALAD----GEDEFTINKNDDEEAL--ATLDAS 632
|
730 740
....*....|....*....|...
gi 547592 767 KDQIDFFKAGSAINYIGNIRRNE 789
Cdd:TIGR01342 633 EREKEILAAGGKLNLIKNKHREE 655
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
92-500 |
5.44e-125 |
|
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: 379.53 E-value: 5.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 92 RVAMQDASAQMALLQFMTTG-LNQTSVPASIHCDHlivgkdgeTKDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGII 170
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAaLGKVADPSQIACVH--------DHAVQLEKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 171 HQIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAG 250
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 251 LLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRaevAEAADVALNKFNFLRADK 330
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR---PLLKNLWLAFPEELLADE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 331 DAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEKSLKEnwpqkvsaGLIGSCTNSSYQDMSRVVDLVKQASkagLKP 410
Cdd:cd01351 230 GAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEGTKIDQ--------VLIGSCTNNRYSDMLAAAKLLKGAK---VAP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 411 RIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNRedvskTSKETNTIFTSFNRNFRARNdGNRNTMN 490
Cdd:cd01351 299 GVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR-----LVADGEVGVSSGNRNFPGRL-GTYERHV 372
|
410
....*....|
gi 547592 491 FLTSPEIVTA 500
Cdd:cd01351 373 YLASPELAAA 382
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
91-505 |
4.11e-114 |
|
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: 350.98 E-value: 4.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 91 DRVAMQDASAQMALLQFMTTGLNQTSVPASI-HCDHLIVGKDGEtkdlpssiatNQEVFDFLESCAKRYGIQFWGPGSGI 169
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVsYVDHNTLQTDFE----------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 170 IHQIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLA 249
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 250 GLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAevaeaadvalNKFNFLRAD 329
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRE----------DDWVELAAD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 330 KDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAekslkenwPQKVSAGLIGSCTNSSYQDMSRVVDLVKQASkagLK 409
Cdd:cd01585 221 ADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREVA--------GIKVDQVAIGSCTNSSYEDLMTVAAILKGRR---VH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 410 PRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNREDVSKTSKETntiftsFNRNFRARNdGNRNTM 489
Cdd:cd01585 290 PHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTGGVSVRT------FNRNFEGRS-GTKDDL 362
|
410
....*....|....*.
gi 547592 490 NFLTSPEIVTAMSYSG 505
Cdd:cd01585 363 VYLASPEVAAAAALTG 378
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
53-500 |
9.29e-89 |
|
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: 286.16 E-value: 9.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 53 PLTLAEKILYSHLCDpeesitssdlsTIRGNKYLKLNPDRVAMQDASAQMALLQFMTTGLNQTSVPASIH--CDHLIVGK 130
Cdd:COG0065 2 GMTLAEKILARHAGR-----------EVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPTK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 131 DGETkdlpssiATNQEVF-DFlescAKRYGIQFWGPGS-GIIHQIVLEN-FSAPGLMMLGTDSHTPNAGGLGAIAIGVGG 207
Cdd:COG0065 71 DPKS-------AEQVKTLrEF----AKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHGAFGAFAFGIGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 208 ADAVDAL-TGTPWeLKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAE 286
Cdd:COG0065 140 TDVAHVLaTGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 287 IGATTSTFPYQEAHKRYLQATNRAevaeaadvalnKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAE 366
Cdd:COG0065 219 AGAKAGIIAPDETTFEYLKGRPFA-----------PWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 367 KslkenwpqKVSAGLIGSCTNSSYQDMSRVVDLVKqaskaGLK--PRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVL 444
Cdd:COG0065 288 I--------KIDQVFIGSCTNGRIEDLRAAAEILK-----GRKvaPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWR 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 547592 445 ANACGPCIGqwNREDVskTSKETNTIFTSfNRNFRARNdGNRNTMNFLTSPEIVTA 500
Cdd:COG0065 355 EPGCGMCLG--MNMGV--LAPGERCASTS-NRNFEGRM-GSPGSRTYLASPATAAA 404
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
92-500 |
4.17e-78 |
|
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: 256.73 E-value: 4.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 92 RVAMQDASAQMALLQFMTTGLNQTSVPASIHC--DHLIvgkdgETKDLPSsiATNQevfDFLESCAKRYGIQFWGPG-SG 168
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNV-----PTPDIKA--AEQV---KTLRKFAKEFGINFFDVGrQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 169 IIHQIVLEN-FSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDAL-TGTPWeLKAPKILGVKLTGKLNGWSTPKDVIT 246
Cdd:cd01583 71 ICHVILPEKgLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLaTGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 247 KLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAevaeaadvalnKFNFL 326
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-----------YWKEL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 327 RADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAekslkenwPQKVSAGLIGSCTNSSYQDMSRVVDLVKqasKA 406
Cdd:cd01583 219 KSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVE--------GIKIDQVFIGSCTNGRLEDLRAAAEILK---GR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 407 GLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIG----QWNREDVSktsketntIFTSfNRNFRARN 482
Cdd:cd01583 288 KVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGghmgVLAPGERC--------VSTS-NRNFKGRM 358
|
410
....*....|....*...
gi 547592 483 dGNRNTMNFLTSPEIVTA 500
Cdd:cd01583 359 -GSPGARIYLASPATAAA 375
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
53-500 |
4.44e-77 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 255.10 E-value: 4.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 53 PLTLAEKILYSHLCDPEEsitssdlstirGNKYLKLNPDRVAMQDASAQMALLQFMTTGLNQTSVPASIH--CDHLIVGK 130
Cdd:PRK00402 2 GMTLAEKILARHSGRDVS-----------PGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 131 DGETkdlpssiATNQ-EVFDFlescAKRYGIQ-FWGPGSGIIHQIVLEN-FSAPGLMMLGTDSHTPNAGGLGAIAIGVGG 207
Cdd:PRK00402 71 DIKS-------AEQQkILREF----AKEQGIPnFFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCTYGALGAFATGMGS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 208 AD-AVDALTGTPWeLKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAE 286
Cdd:PRK00402 140 TDmAAAMATGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 287 IGATTSTFPYQEAHKRYLQAtnraevaeaadVALNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAE 366
Cdd:PRK00402 219 AGAKAGIFAPDEKTLEYLKE-----------RAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 367 KslkenwpqKVSAGLIGSCTNSSYQDMSRVVDLVKqasKAGLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLAN 446
Cdd:PRK00402 288 T--------KVDQVFIGSCTNGRLEDLRIAAEILK---GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTP 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 547592 447 ACGPCIGQWN----REDVSktsketntIFTSfNRNFRARNdGNRNTMNFLTSPEIVTA 500
Cdd:PRK00402 357 TCGPCLGGHMgvlaPGEVC--------LSTT-NRNFKGRM-GSPESEVYLASPAVAAA 404
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
90-782 |
5.64e-68 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 241.76 E-value: 5.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 90 PDRVAMQDASAQMAL--LQFMTTGLNQT---------SVPASIHCDH-LIVGKDGEtkdlPSSIATNQEVFDflESCAKR 157
Cdd:PRK12881 83 PARVVMQDFTGVPALvdLAAMRDAAAEAggdpakinpLVPVDLVVDHsVAVDYFGQ----KDALDLNMKIEF--QRNAER 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 158 YgiQF--WG-----------PGSGIIHQIVLENFsAPGL--------------MMLGTDSHTPNAGGLGAIAIGVGGADA 210
Cdd:PRK12881 157 Y--QFlkWGmqafdnfrvvpPGTGIMHQVNLEYL-ARVVhtkeddgdtvaypdTLVGTDSHTTMINGIGVLGWGVGGIEA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 211 VDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGAT 290
Cdd:PRK12881 234 EAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGAT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 291 TSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRADKDA--QYDKVIEIDLSAIEPHVNGPFTP-------DLSTPI 361
Cdd:PRK12881 314 MGFFPVDEQTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKAepRYTRTLELDLSTVAPSLAGPKRPqdrialgNVKSAF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 362 SQYAEKSLKENWPQK--------------VSAGLIGSCTNSSyqDMSRVVD---LVKQASKAGLKPRiPFFVT---PGSE 421
Cdd:PRK12881 394 SDLFSKPVAENGFAKkaqtsngvdlpdgaVAIAAITSCTNTS--NPSVLIAaglLAKKAVERGLTVK-PWVKTslaPGSK 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 422 QIRATLERDGIIDIFQENGAKVLANACGPCIGqwN----REDVSKTSKETNTIFT---SFNRNFRARNDGNRnTMNFLTS 494
Cdd:PRK12881 471 VVTEYLERAGLLPYLEKLGFGIVGYGCTTCIG--NsgplTPEIEQAITKNDLVAAavlSGNRNFEGRIHPNI-KANFLAS 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 495 PEIVTAMSYSGDAQFNPLTDsiklPNGKDFKFQP-------PKG---DELPKRGF--EHGRdKFYPEMDPKPDSNVEIKV 562
Cdd:PRK12881 548 PPLVVAYALAGTVRRDLMTE----PLGKGKDGRPvylkdiwPSSaeiDALVAFAVdpEDFR-KNYAEVFKGSELWAAIEA 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 563 --------DPNSDRLQlLEPFkpWNGKELKTNVLLKVEG---------KCTTDHIS---------AAGVWLKYKGHLENI 616
Cdd:PRK12881 623 pdgplydwDPKSTYIR-RPPF--FDFSMGPAASIATVKGarplavlgdSITTDHISpagaikadsPAGKYLKENGVPKAD 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 617 --SY---------------------NTLIGAqnKETGevNKAYDLDGTEYDIPGLMMKWKSDGRPWTVIAEHNYGEGSAR 673
Cdd:PRK12881 700 fnSYgsrrgnhevmmrgtfanvrikNLMIPG--KEGG--LTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSR 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 674 EHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYD--KISSGDVLETLNLVDMIAKdgnnGGEIDVKITK 751
Cdd:PRK12881 776 DWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQslGLTGGETFDIEGLPGEIKP----RQDVTLVIHR 851
|
810 820 830
....*....|....*....|....*....|..
gi 547592 752 PNGESFTIKAKHTM-SKDQIDFFKAGSAINYI 782
Cdd:PRK12881 852 ADGSTERVPVLCRIdTPIEVDYYKAGGILPYV 883
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
55-505 |
1.83e-66 |
|
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: 226.56 E-value: 1.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 55 TLAEKILYSHlcdPEESITSSDLSTIrgnkylklNPDRVAMQDASAQMALLQFMTTGLNQTSVPASIHC--DHLIvgkdg 132
Cdd:TIGR01343 1 TIAEKILSKK---SGKEVYAGDLIEA--------EIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 133 etkdlPSSIATNQEVFDFLESCAKRYGIQ-FWGPGSGIIHQIVLEN-FSAPGLMMLGTDSHTPNAGGLGAIAIGVGGAD- 209
Cdd:TIGR01343 65 -----PADTIKAAEMQKLAREFVKKQGIKyFYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDm 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 210 AVDALTGTPWeLKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGA 289
Cdd:TIGR01343 140 AYAIATGKTW-FKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 290 TTSTFPYQEAHKRYLQATNRAevaeaadvalnKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEKsl 369
Cdd:TIGR01343 219 KTGIIEPDEKTIQYLKERRKE-----------PFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGT-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 370 kenwpqKVSAGLIGSCTNSSYQDMSRVVDLVKqasKAGLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACG 449
Cdd:TIGR01343 286 ------EIDQVFIGSCTNGRLEDLRVAAKILK---GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCG 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 547592 450 PCIGQwnredVSKTSKETNTIFTSFNRNFRARNdGNRNTMNFLTSPEIVTAMSYSG 505
Cdd:TIGR01343 357 PCLGS-----HQGVLAPGEVCISTSNRNFKGRM-GHPNAEIYLASPATAAASAVKG 406
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
144-782 |
1.16e-65 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 235.29 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 144 NQEVFDFLEscakrygiqfWG-----------PGSGIIHQIVLEN-----FSAPGLM----MLGTDSHTPNAGGLGAIAI 203
Cdd:PTZ00092 160 NLERFEFLK----------WGskafknllivpPGSGIVHQVNLEYlarvvFNKDGLLypdsVVGTDSHTTMINGLGVLGW 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 204 GVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNM 283
Cdd:PTZ00092 230 GVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 284 GAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRADKDAQ--YDKVIEIDLSAIEPHVNGP--------- 352
Cdd:PTZ00092 310 APEYGATMGFFPIDEKTLDYLKQTGRSEEKVELIEKYLKANGLFRTYAEQieYSDVLELDLSTVVPSVAGPkrphdrvpl 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 353 ------FTPDLSTPIS--------QYAEKSLKENWPQK--------VSAGLIGSCTNSSYQD-MSRVVDLVKQASKAGLK 409
Cdd:PTZ00092 390 sdlkkdFTACLSAPVGfkgfgipeEKHEKKVKFTYKGKeytlthgsVVIAAITSCTNTSNPSvMLAAGLLAKKAVEKGLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 410 PrIPFFVT---PGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGqwNR----EDVSKTSKETNTIFTSF---NRNFR 479
Cdd:PTZ00092 470 V-PPYIKTslsPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIG--NSgdldPEVSEAITNNDLVAAAVlsgNRNFE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 480 AR-NDGNRntMNFLTSPEIVTAMSYSGDAQFNPLTDSI-KLPNGKDFKFQppkgDELPKRGF--EHGRDKFYPEMDPKPD 555
Cdd:PTZ00092 547 GRvHPLTR--ANYLASPPLVVAYALAGRVNIDFETEPLgSDKTGKPVFLR----DIWPSREEiqALEAKYVKPEMFKEVY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 556 SNVEiKVDPNSDRLQLLE-PFKPWN-------------GKELKTNVLLKVEG-KC--------TTDHISAAGV------- 605
Cdd:PTZ00092 621 SNIT-QGNKQWNELQVPKgKLYEWDekstyihnppffqTMELEPPPIKSIENaYCllnlgdsiTTDHISPAGNiaknspa 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 606 --WLKYKGhLENISYNTLiGAQ--NKE---------TGEVNKAYDLDG--TEYdIPG--LM------MKWKSDGRPWTVI 662
Cdd:PTZ00092 700 akYLMERG-VERKDFNTY-GARrgNDEvmvrgtfanIRLINKLCGKVGpnTVH-VPTgeKMsiydaaEKYKQEGVPLIVL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 663 AEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANesdydkissGDVLETLNLvdmiakDGN-- 740
Cdd:PTZ00092 777 AGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLN---------GENADSLGL------TGKeq 841
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 547592 741 -----NGGEI----DVKITKPNGESFTIKAKHTmSKDQIDFFKAGSAINYI 782
Cdd:PTZ00092 842 fsidlNSGELkpgqDVTVKTDTGKTFDTILRID-TEVEVEYFKHGGILQYV 891
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
144-782 |
1.76e-65 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 234.63 E-value: 1.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 144 NQEVFDFLEscakrygiqfWG-----------PGSGIIHQIVLEnFSAPGLM-------------MLGTDSHTPNAGGLG 199
Cdd:PRK09277 154 NEERYQFLK----------WGqkafdnfrvvpPGTGICHQVNLE-YLAPVVWtredgelvaypdtLVGTDSHTTMINGLG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 200 AIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMAT 279
Cdd:PRK09277 223 VLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRAT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 280 ICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFN--FLRADKDAQYDKVIEIDLSAIEPHVNGP----- 352
Cdd:PRK09277 303 IANMAPEYGATCGFFPIDEETLDYLRLTGRDEEQVALVEAYAKAQglWRDPLEEPVYTDVLELDLSTVEPSLAGPkrpqd 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 353 --FTPDLSTPISQYAEKSLKENWPQKVSAGL-------------IGSCTNSSYqdmSRVVD----LVKQASKAGLKPRiP 413
Cdd:PRK09277 383 riPLSDVKEAFAKSAELGVQGFGLDEAEEGEdyelpdgavviaaITSCTNTSN---PSVMIaaglLAKKAVEKGLKVK-P 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 414 FFVT---PGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGqwN----REDVSKTSKETNTIFT---SFNRNFRARNd 483
Cdd:PRK09277 459 WVKTslaPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIG--NsgplPPEIEKAINDNDLVVTavlSGNRNFEGRI- 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 484 gNRNT-MNFLTSPEIVTAMSYSGDAQFNPLTDSI-KLPNGKDFKFQP--PKGDELpkrgfehgrDKFY-----PEMDPKP 554
Cdd:PRK09277 536 -HPLVkANYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEI---------DAVVakavkPEMFRKE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 555 DSNV--------EIKV--------DPNSDRLQlLEPFkpWNG-----KELKT----NVLLKVEGKCTTDHIS-------- 601
Cdd:PRK09277 606 YADVfegderwnAIEVpegplydwDPDSTYIR-NPPY--FEGmlaepGPVRDikgaRVLALLGDSITTDHISpagaikad 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 602 -AAGVWLKYKG---------------HL-------ENISYNTLIgAQNKE--------TGEVNKAYDldgteydipgLMM 650
Cdd:PRK09277 683 sPAGKYLLEHGvepkdfnsygsrrgnHEvmmrgtfANIRIRNEM-VPGVEggytrhfpEGEVMSIYD----------AAM 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 651 KWKSDGRPWTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANesdydkissGDVLETLN 730
Cdd:PRK09277 752 KYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKP---------GESRKTLG 822
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 547592 731 L-----VDMIAKDG-NNGGEIDVKITKPNGESFTIKAKHTM-SKDQIDFFKAGSAINYI 782
Cdd:PRK09277 823 LdgtetFDIEGLEDlKPGATVTVVITRADGEVVEFPVLCRIdTAVEVDYYRNGGILQYV 881
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
590-734 |
6.34e-64 |
|
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: 210.40 E-value: 6.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 590 KVEGKCTTDHISAAGVWLKYKGHLENISYNTLIGAQNKETGEVNKAYDLDGTEYD-IPGLMMKWKSDGRPWTVIAEHNYG 668
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGpVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547592 669 EGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLETLNLVDM 734
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDF 146
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
144-782 |
1.39e-57 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 212.36 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 144 NQEVFDFLEscakrygiqfWG-----------PGSGIIHQIVLEN-----FSAPGLM----MLGTDSHTPNAGGLGAIAI 203
Cdd:PLN00070 192 NKERFAFLK----------WGstafqnmlvvpPGSGIVHQVNLEYlgrvvFNTDGILypdsVVGTDSHTTMIDGLGVAGW 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 204 GVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNM 283
Cdd:PLN00070 262 GVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANM 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 284 GAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVAlnkfnFLRADK----------DAQYDKVIEIDLSAIEPHVNGPF 353
Cdd:PLN00070 342 SPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEA-----YLRANKmfvdynepqqERVYSSYLELDLEDVEPCISGPK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 354 TPDLSTPIsqyaeKSLKENW-------------------------------PQKVSAG-----LIGSCTNSSYQDMSRVV 397
Cdd:PLN00070 417 RPHDRVPL-----KEMKADWhscldnkvgfkgfavpkeaqskvakfsfhgqPAELRHGsvviaAITSCTNTSNPSVMLGA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 398 DLV-KQASKAGL--KPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNR--EDVSKTSKETNTI-- 470
Cdd:PLN00070 492 GLVaKKACELGLevKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGEldESVASAITENDIVaa 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 471 -FTSFNRNFRARNDGnRNTMNFLTSPEIVTAMSYSGDAQFNPLTDSIKL-PNGKDFKFQP--PKGDE---------LP-- 535
Cdd:PLN00070 572 aVLSGNRNFEGRVHP-LTRANYLASPPLVVAYALAGTVDIDFEKEPIGTgKDGKDVFFRDiwPSNEEvaevvqssvLPdm 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 536 -KRGFEhGRDKFYPEMDPKP-DSNVEIKVDPNSDRLQllEP--FK-----PWNGKELK-TNVLLKVEGKCTTDHISAAGV 605
Cdd:PLN00070 651 fKSTYE-AITKGNPMWNQLSvPSGTLYSWDPKSTYIH--EPpyFKnmtmsPPGPHGVKdAYCLLNFGDSITTDHISPAGS 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 606 WLK-----------------------YKGHLENISYNTL--IGAQNKE-TGEV--NKAYDLDGTEYDIPGLMMKWKSDGR 657
Cdd:PLN00070 728 IHKdspaakylmergvdrkdfnsygsRRGNDEIMARGTFanIRIVNKLlKGEVgpKTVHIPTGEKLSVFDAAMKYKSEGH 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 658 PWTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKIS-SGDVLETLNLVDMIA 736
Cdd:PLN00070 808 DTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGlTGHERYTIDLPSNIS 887
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 547592 737 --KDGNnggeiDVKITKPNGESFTIKAKHTmSKDQIDFFKAGSAINYI 782
Cdd:PLN00070 888 eiKPGQ-----DVTVTTDNGKSFTCTLRFD-TEVELAYFDHGGILPYV 929
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
585-714 |
1.59e-55 |
|
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: 186.80 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 585 TNVLLKVEGKCTTDHISAAGVWLKYKGHLENISYNTLIGAQNKETGEVNKAYDLDGTEY-DIPGLMMKWKSDGRPWTVIA 663
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENpDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 547592 664 EHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANE 714
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
117-505 |
3.85e-44 |
|
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: 164.40 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 117 VPASIHCDH-LIVGKDGETKdlpsSIATNQEVFdfLESCAKRYGIQFWG-----------PGSGIIHQIVLEnFSAPGLM 184
Cdd:cd01586 37 IPVDLVIDHsVQVDFYGTAD----ALAKNMKLE--FERNRERYEFLKWGqkafknlrvvpPGTGIIHQVNLE-YLARVVF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 185 M--------------LGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAG 250
Cdd:cd01586 110 TseedgdgvaypdsvVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 251 LLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYqeahkrylqatnraevaeaadvalnkfnflradk 330
Cdd:cd01586 190 MLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPV---------------------------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 331 DAQydkVIEIDLSAIEPHVNGPFTPDLSTPISqyaekslkenwpQKVSAGLIGSCTNSSYQDMSRVVDLV-KQASKAGLK 409
Cdd:cd01586 236 DTQ---VVELDLSTVEPSVSGPKRPQDRVPLH------------GSVVIAAITSCTNTSNPSVMLAAGLLaKKAVELGLK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 410 PRiPFFVT---PGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGqwN----REDVSKTSKETNTIFT---SFNRNFR 479
Cdd:cd01586 301 VK-PYVKTslaPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIG--NsgplPEEVEEAIKENDLVVAavlSGNRNFE 377
|
410 420
....*....|....*....|....*..
gi 547592 480 AR-NDGNRntMNFLTSPEIVTAMSYSG 505
Cdd:cd01586 378 GRiHPLVR--ANYLASPPLVVAYALAG 402
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
124-505 |
1.33e-40 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 155.83 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 124 DHLIVGKDGETKDLPSSIATNQeVFDFLESCAkRYGIQFWG---PGSGIIHQIVLE-NFSAPGLMMLGTDSHTPNAGGLG 199
Cdd:PRK12466 63 DHVVPTRPGRDRGITDPGGALQ-VDYLRENCA-DFGIRLFDvddPRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 200 AIAIGVGGADAVDAL-TGTPWeLKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMA 278
Cdd:PRK12466 141 ALAFGIGTSEVEHVLaTQTLV-YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 279 TICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLS 358
Cdd:PRK12466 220 TLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 359 TPIS-------QYAEKSLKENWPQ----------------KVSAGLIGSCTNSSYQDMSRVVDLVKQASKAglkPRIPFF 415
Cdd:PRK12466 300 VPITgrvpdpaAEADPARRAAMERaldymgltpgtplagiPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVA---PGVRAM 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 416 VTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQwN------REDVSKTSketntiftsfNRNFRARNdgNRNTM 489
Cdd:PRK12466 377 VVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAM-NddvlapGERCASTT----------NRNFEGRQ--GPGAR 443
|
410
....*....|....*.
gi 547592 490 NFLTSPEIVTAMSYSG 505
Cdd:PRK12466 444 THLMSPAMVAAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
105-505 |
1.17e-39 |
|
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: 150.46 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 105 LQFMTTGLNQTSVPASIHC--DHlivgkdgetkDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLEN-FSAP 181
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH----------DVQNKSEKNLKKYKNIESFAKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 182 GLMMLGTDSHTPNAGGLGAIAIGVGGADAVDA-LTGTPWeLKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGY 260
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIwATGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 261 IVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHkrylqatnraevaeaadvalnkfnflradkdaqydkvIEI 340
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKH-------------------------------------LIL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 341 DLSAIEPHVNGPFTPDLSTPISQYAEKSLKENwpqkvSAGLIgSCTNSSYQDMSRVVDLVK-QASKAGLKPRIP---FFV 416
Cdd:cd01582 205 DLSTLSPYVSGPNSVKVSTPLKELEAQNIKIN-----KAYLV-SCTNSRASDIAAAADVVKgKKEKNGKIPVAPgveFYV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 417 TPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWnredvSKTSKETNTIFTSFNRNFRARNdGNRNTMNFLTSPE 496
Cdd:cd01582 279 AAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLG-----QGLLEPGEVGISATNRNFKGRM-GSTEALAYLASPA 352
|
....*....
gi 547592 497 IVTAMSYSG 505
Cdd:cd01582 353 VVAASAISG 361
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
124-441 |
2.98e-39 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 151.81 E-value: 2.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 124 DHlIVGKDGETKDLPSSIATNQevFDFLESCAKRYGIQFWGPGS---GIIHQIVLEN-FSAPGLMMLGTDSHTPNAGGLG 199
Cdd:PRK05478 62 DH-NVPTTDRDLPIADPVSRIQ--VETLEKNCKEFGITLFDLGDprqGIVHVVGPEQgLTLPGMTIVCGDSHTSTHGAFG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 200 AIAIGVGGADAVDAL-TGTPWeLKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMA 278
Cdd:PRK05478 139 ALAFGIGTSEVEHVLaTQTLL-QKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRM 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 279 TICNMGAEIGATT-------STFPY------------QEAHKRYLQAtnraevaeaadvalnkfnfLRADKDAQYDKVIE 339
Cdd:PRK05478 218 TICNMSIEAGARAglvapdeTTFEYlkgrpfapkgedWDKAVAYWKT-------------------LKSDEDAVFDKVVT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 340 IDLSAIEPHVNGPFTPDLSTPISQY---------------AEKS-----LKENWP---QKVSAGLIGSCTNSSYQDMSRV 396
Cdd:PRK05478 279 LDAADIEPQVTWGTNPGQVISIDGKvpdpedfadpvkrasAERAlaymgLKPGTPitdIKIDKVFIGSCTNSRIEDLRAA 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 547592 397 VDLVKQASKAglkPRIPFFVTPGSEQIRATLERDGIIDIFQENGA 441
Cdd:PRK05478 359 AAVVKGRKVA---PGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
153-781 |
1.14e-35 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 144.77 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 153 SCAKRYGIQFWGPGSGIIHQIVLENFSAPGLMMLGTDSHTpNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLT 232
Cdd:PRK11413 113 SAAQKYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 233 GKLNGWSTPKDVITKLAGLLTvrgGTGY----IVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATN 308
Cdd:PRK11413 192 GKPAPGVGPQDVALAIIGAVF---KNGYvknkVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 309 RAevaeaadvalNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEK--------------------- 367
Cdd:PRK11413 269 RG----------QDYCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNltdilreveieservahgkak 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 368 -SLK---ENWPQKVSAGLIGSCTNSSYQDMSRVVDLVKqaSKAGLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKV 443
Cdd:PRK11413 339 lSLLdkiENGRLKVQQGIIAGCSGGNYENVIAAANALR--GQSCGNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAII 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 444 LANACGPCIGQWNREDVSKTSKETNTiftsfnRNFRARnDGNRNTMNFLTSPEIVTAMSYSGDA----QFNPLTDSIKLP 519
Cdd:PRK11413 417 RTAFCGPCFGAGDTPANNGLSIRHTT------RNFPNR-EGSKPANGQMSAVALMDARSIAATAanggYLTSATELDCWD 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 520 NGKDFKFQPPKGDELPKRGFEhgrdkfypemdpKPDSNVEIKVDPNsdrlqllepFKPWNGKE-LKTNVLLKVEGK---- 594
Cdd:PRK11413 490 NVPEYAFDVTPYKNRVYQGFG------------KGATQQPLIYGPN---------IKDWPEMGaLTDNILLKVCSKildp 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 595 -CTTDHISAAGVWLKYKGHLENISYNTL------------------IGAQNKETGEVNKAYDLDGTEYDIPGLMMKWKSD 655
Cdd:PRK11413 549 vTTTDELIPSGETSSYRSNPLGLAEFTLsrrdpgyvgrskavaeleNQRLAGNVSELTEVFARIKQIAGQEHIDPLQTEI 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 656 GrpwTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFA-RIHETNLKKQGVLPLTFANESDYDKissGDVLETLNLVDM 734
Cdd:PRK11413 629 G---SMVYAVKPGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEEPTFEV---GDYIYIPGIRAA 702
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 547592 735 IAKDGNnggEIDVKITKPNG--ESFTIKAKhTMSKDQIDFFKAGSAINY 781
Cdd:PRK11413 703 LDNPGT---TFKGYVIHEDApvTEITLYME-SLTAEEREIIKAGCLINY 747
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
590-727 |
6.29e-31 |
|
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: 117.54 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 590 KVEGKCTTDHISAAGV-WLKYKGHLENISYNTLIGAqNKETGEVNKAYDldgteydiPGLmmkwksdgrpwtVIAEHNYG 668
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHRV-DPTFAERAKAAG--------PGF------------IVGGENYG 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 547592 669 EGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLE 727
Cdd:cd01579 60 QGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLE 118
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
590-727 |
2.49e-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: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 590 KVEGKCTTDHISAAGvwlkykghlenisyntligaqnketgevnkaydldgteydipglmmkwksdgrPWTVIAEHNYGE 669
Cdd:cd00404 1 KVAGNITTDHISPAG-----------------------------------------------------PGVVIGDENYGT 27
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 547592 670 GSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLE 727
Cdd:cd00404 28 GSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELD 85
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
138-505 |
3.79e-18 |
|
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: 87.94 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 138 PSSIATNQEVFDFLEScakRYGIQFwGPGSGIIHQiVLENFSAPGLMMLGTDSHTPNAGGlgaIAIGVG-GADAVDALTG 216
Cdd:cd01581 68 PVDVKTHRTLPDFISN---RGGVAL-RPGDGVIHS-WLNRMLLPDTVGTGGDSHTRFPIG---ISFPAGsGLVAFAAATG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 217 TpWELKAPKILGVKLTGKLNGWSTPKDVITKL------AGLLTVRGG------TGYIVEYfgEGVSTLSCTGMATICNMG 284
Cdd:cd01581 140 V-MPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqQGLLTVEKKgkknvfNGRILEI--EGLPDLKVEQAFELTDAS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 285 AEIGATTST--------FPYQEAHKRYLQ---------ATNRAEVAEAADVALNKFNFLRADKDAQYDKVIEIDLSAI-E 346
Cdd:cd01581 217 AERSAAACTvrldkepvIEYLESNVVLMKimiangyddARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIkE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 347 PHVNGPFTPDLSTPISQYAEKslkenwpqKVSAGLIGSC-TN-SSYQDMSRVVDLVKQAskaglKPRIpfFVTPGSEQIR 424
Cdd:cd01581 297 PILACPNDPDDVKLLSEVAGK--------KIDEVFIGSCmTNiGHFRAAAKILRGKEFK-----PTRL--WVAPPTRMDW 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 425 ATLERDGIIDIFQENGAKVLANACGPCIGqwNREDVSKTSketnTIFTSFNRNFRARNdgNRNTMNFLTSPEIVTAMSYS 504
Cdd:cd01581 362 AILQEEGYYSIFGDAGARTEMPGCSLCMG--NQARVADGA----TVFSTSTRNFDNRV--GKGAEVYLGSAELAAVCALL 433
|
.
gi 547592 505 G 505
Cdd:cd01581 434 G 434
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
138-498 |
6.93e-15 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 78.68 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 138 PSSIATNQEVFDFLescAKRYGIQFwGPGSGIIHQiVLENFSAPGLMMLGTDSHT--------PNAGGLGAIAigvggad 209
Cdd:PRK09238 440 PVDVKTHHTLPDFI---MNRGGVSL-RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGLVAFA------- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 210 avdALTGT-PweLKAPKILGVKLTGKLNGWSTPKDVITKL------AGLLTV--RGG----TGYIVEYfgEGVSTLSCTG 276
Cdd:PRK09238 508 ---AATGVmP--LDMPESVLVRFKGEMQPGITLRDLVHAIpyyaikQGLLTVekKGKknifSGRILEI--EGLPDLKVEQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 277 MATICNMGAEIGATTSTFP--------YQEAHKRYLQA------------TNRAEVAEAAdvaLNKFNFLRADKDAQYDK 336
Cdd:PRK09238 581 AFELTDASAERSAAGCTIKlskepiieYLRSNIVLLKWmiaegygdartlERRIAAMEEW---LANPELLEADADAEYAA 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 337 VIEIDLSAI-EPHVNGPFTPDLSTPISQYAEKSLKEnwpqkvsaGLIGSC-TN-SSYQDMSRVVDLVKQASKAglkpriP 413
Cdd:PRK09238 658 VIEIDLAEIkEPILACPNDPDDVRLLSEVAGTKIDE--------VFIGSCmTNiGHFRAAGKLLEGKKGQLPT------R 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 414 FFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGqwNREDVSKTSketnTIFTSFNRNF--RARNDGNrntmNF 491
Cdd:PRK09238 724 LWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG--NQARVADGA----TVFSTSTRNFpnRLGKGAN----VY 793
|
....*..
gi 547592 492 LTSPEIV 498
Cdd:PRK09238 794 LGSAELA 800
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
596-731 |
1.60e-12 |
|
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: 66.53 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 596 TTDHISAAGVWL------KY-------------------------KGHLENISY-NTLIGaqnkETGEVNKAYDLDGTEY 643
Cdd:cd01580 7 TTDHISPAGSIAkdspagKYlaergvkprdfnsygsrrgndevmmRGTFANIRLrNKLVP----GTEGGTTHHPPTGEVM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 644 DIPGLMMKWKSDGRPWTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANesdydkissG 723
Cdd:cd01580 83 SIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPP---------G 153
|
....*...
gi 547592 724 DVLETLNL 731
Cdd:cd01580 154 ENADSLGL 161
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
138-505 |
1.06e-11 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 68.80 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 138 PSSIATNQEVFDFLEScakRYGIQFwGPGSGIIHQIvLENFSAPGLMMLGTDSHTPNAGGlgaIAIGVG-GADAVDALTG 216
Cdd:PLN00094 514 PVDVVTHHTLPDFIRN---RGGVSL-RPGDGVIHSW-LNRMLLPDTVGTGGDSHTRFPIG---ISFPAGsGLVAFGAATG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 217 TpWELKAPKILGVKLTGKLNGWSTPKDVITKL------AGLLTV--RGGT----GYIVEYfgEGVSTLSCTGMATICNMG 284
Cdd:PLN00094 586 V-IPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiqDGLLTVekKGKKnvfsGRILEI--EGLPHLKCEQAFELSDAS 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 285 AEIGATTSTFPYQEAH-KRYLQAT----------------NRAEVAEAADVALNKFNFLRADKDAQYDKVIEIDLSAI-E 346
Cdd:PLN00094 663 AERSAAGCTIKLDKEPiIEYLNSNvvmlkwmiaegygdrrTLERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIkE 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 347 PHVNGPFTPDlstpisqyAEKSLKENWPQKVSAGLIGSC-TNSSYqdmSRVVDLVKQASKAGLKPRIpfFVTPGSEQIRA 425
Cdd:PLN00094 743 PILCAPNDPD--------DARLLSEVTGDKIDEVFIGSCmTNIGH---FRAAGKLLNDNLSQLPTRL--WVAPPTKMDEA 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 426 TLERDGIIDIFQENGAKVLANACGPCIGqwNREDVSktskETNTIFTSFNRNFRARNDGNRNTmnFLTSPEIVTAMSYSG 505
Cdd:PLN00094 810 QLKAEGYYSTFGTVGARTEMPGCSLCMG--NQARVA----EKSTVVSTSTRNFPNRLGKGANV--YLASAELAAVAAILG 881
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
661-782 |
2.95e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 53.68 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 661 VIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGvLPLTFANEsDYDKISSGDVLEtlnlVDMiakdgn 740
Cdd:PRK00439 52 IVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPVLECDE-AVDKIEDGDEVE----VDL------ 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 547592 741 NGGEIdVKITKpnGESFTIKAKHTMSKDQIdffKAGSAINYI 782
Cdd:PRK00439 120 ETGVI-TNLTT--GEEYKFKPIPEFMLEIL---KAGGLIEYL 155
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
661-727 |
2.89e-07 |
|
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: 48.74 E-value: 2.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547592 661 VIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANE-SDYDKISSGDVLE 727
Cdd:cd01577 21 IVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEdVEEVEAKPGDEVE 88
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
654-727 |
5.12e-06 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 47.49 E-value: 5.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547592 654 SDGRPWTV-IAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPltFANESDYDKISSGDVLE 727
Cdd:PRK14023 45 STVRPGDIlVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDEVE 117
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
661-775 |
9.09e-05 |
|
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: 44.01 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547592 661 VIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTfANESDYDKissgdvletlnLVDMIAKDGN 740
Cdd:COG0066 68 LVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDA-----------LFAAIEANPG 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 547592 741 NGGEIDV---KITKPNGESFTIK----AKH-----------TMSK-DQIDFFKA 775
Cdd:COG0066 136 DELTVDLeagTVTNGTGETYPFEidpfRREcllnglddiglTLKHaDAIAAFEA 189
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
661-727 |
6.28e-04 |
|
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: 40.87 E-value: 6.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547592 661 VIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGvLPLTFANEsdyDKISSGDVLE 727
Cdd:TIGR02087 51 IVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIG-LPLIEAKT---EGIKDGDEVT 113
|
|
| |
