|
Name |
Accession |
Description |
Interval |
E-value |
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
2-851 |
0e+00 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 1873.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 2 RAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELLG 81
Cdd:COG1049 12 RAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEATSPLISPEKAVELLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 82 TMLGGYNIGPLVQLLDDAEVGTIAADALKKTLLMFDAFHDVKEKADKGNANAKSVLQSWADAEWFTSRPEVPQSLTVTVF 161
Cdd:COG1049 92 TMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKAGNAYAKQVLQSWADAEWFTSRPELPEKITVTVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 162 KVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSSRKSA 241
Cdd:COG1049 172 KVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG------------PLKTIAELKAKGHPVAYVGDVVGTGSSRKSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 242 TNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIK-NGETIAEFTV 320
Cdd:COG1049 240 TNSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVIDIYPYEGKITKeNGEVISTFEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 321 KSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLpegQGIRPGTYCEPK 400
Cdd:COG1049 320 KPDTLLDEVRAGGRIPLIIGRGLTDKAREALGLPPSDVFRRPEAPADSGKGYTLAQKMVGKACGV---EGVRPGTYCEPK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 401 MTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLNRML 480
Cdd:COG1049 397 MTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIHSWLNRML 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 481 LPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLTVAK 560
Cdd:COG1049 477 LPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQGLLTVEK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 561 QGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRRIKA 640
Cdd:COG1049 557 KGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDARTLERRIAA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 641 MEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLLEGK 720
Cdd:COG1049 637 MEEWLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEGK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 721 RDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYLGSA 800
Cdd:COG1049 717 GNLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLGSA 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 704427622 801 ELAAICSRLGRIPTREEYMADMGVINKSGDQIYQYLNFDRIPDYKDVADVI 851
Cdd:COG1049 797 ELAAVCALLGRLPTVEEYMEYVKKIDPMADDIYRYLNFDQIEEYQEKADVV 847
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
1-838 |
0e+00 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 1767.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 1 DRAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELL 80
Cdd:PRK09238 11 ERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPLISPEKAVELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 81 GTMLGGYNIGPLVQLLDDAEVGTIAADALKKTLLMFDAFHDVKEKADKGNANAKSVLQSWADAEWFTSRPEVPQSLTVTV 160
Cdd:PRK09238 91 GTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAGNAYAKEVLESWADAEWFTSRPELPEKITVTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 161 FKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSSRKS 240
Cdd:PRK09238 171 FKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG------------PIKQIEELKKKGHPVAYVGDVVGTGSSRKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 241 ATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIK-NGETIAEFT 319
Cdd:PRK09238 239 ATNSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSGALPIELDVSKLNMGDVIDIYPYKGKIRNeTGEVIATFK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 320 VKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLPegqGIRPGTYCEP 399
Cdd:PRK09238 319 LKTDVLLDEVRAGGRIPLIIGRGLTTKAREALGLPPSDVFRKPKQPADSGKGFTLAQKMVGRACGVP---GVRPGTYCEP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 400 KMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLNRM 479
Cdd:PRK09238 396 KMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 480 LLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLTVA 559
Cdd:PRK09238 476 LLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQGLLTVE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 560 KQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRRIK 639
Cdd:PRK09238 556 KKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDARTLERRIA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 640 AMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLLEG 719
Cdd:PRK09238 636 AMEEWLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEG 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 720 KR-DIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYLG 798
Cdd:PRK09238 716 KKgQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLG 795
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 704427622 799 SAELAAICSRLGRIPTREEYMADMGVINKSGDQIYQYLNF 838
Cdd:PRK09238 796 SAELAAVCALLGRIPTVEEYQEYVAEIDATADDIYRYLNF 835
|
|
| acnB |
TIGR00117 |
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This ... |
1-846 |
0e+00 |
|
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This model describes aconitase 2, AcnB, which has weak similarity to aconitase 1. It is found almost exclusively in the Proteobacteria. [Energy metabolism, TCA cycle]
Pssm-ID: 129223 [Multi-domain] Cd Length: 844 Bit Score: 1416.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 1 DRAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELL 80
Cdd:TIGR00117 11 ERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKCPLISPEKAIELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 81 GTMLGGYNIGPLVQLLD--DAEVGTIAADALKKTLLMFDAFHDVKEKAdKGNANAKSVLQSWADAEWFTSRPEVPQSLTV 158
Cdd:TIGR00117 91 GTMQGGYNVHPLIDALDsqDANIAPIAAKALSHTLLVFDNFYDVEEKS-KTNEYAKQVMQSWADAEWFLNKPALAEKITV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 159 TVFKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaaFEPEedgkrgpvqfIESLKEKGHLVAYVGDVVGTGSSR 238
Cdd:TIGR00117 170 TVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREG--IEPQ----------IEALKQKGFPVAYVGDVVGTGSSR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 239 KSATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGK-AIKNGETIAE 317
Cdd:TIGR00117 238 KSATNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDSGALPIEVDVSNLNMGDVIDIYPYKGEiTNHEGELLAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 318 FTVKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLpegQGIRPGTYC 397
Cdd:TIGR00117 318 FELKPETLLDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQPKAPAESDKGFTLAQKMVGRACGV---KGIRPGTYC 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 398 EPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLN 477
Cdd:TIGR00117 395 EPKMTTVGSQDTTGPMTRDELKELACLGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGVIHSWLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 478 RMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLT 557
Cdd:TIGR00117 475 RMLLPDTVGTGGDSHTRFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAIKQGLLT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 558 VAKQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRR 637
Cdd:TIGR00117 555 VEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 638 IKAMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLL 717
Cdd:TIGR00117 635 IQGMEKWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSCMTNIGHFRAAGKIL 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 718 EGKRDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYL 797
Cdd:TIGR00117 715 DAAGQLPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVADGATVFSTSTRNFPNRMGTGANVYL 794
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 704427622 798 GSAELAAICSRLGRIPTREEYMADMGVINKSG-DQIYQYLNFDRIPDYKD 846
Cdd:TIGR00117 795 GSAELAAVCALLGKIPTPEEYQTYVSEKDKTAvDKTYRYLNFNQLSNFTE 844
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
374-812 |
0e+00 |
|
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: 859.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 374 LAQKMVGRACGlpeGQGIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTL 453
Cdd:cd01581 1 LAQKIVGRACG---VKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 454 PQFISTRGGISLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM 533
Cdd:cd01581 78 PDFISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 534 QPGVTLRDLVNAIPLYAIKQGLLTVAKQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYI 613
Cdd:cd01581 158 QPGITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 614 NSNIVMLKWMIANGYEDERSLGRRIKAMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGA 693
Cdd:cd01581 238 ESNVVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 694 KIDEVFIGSCMTNIGHFRAASKLLEGKRDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVRE 773
Cdd:cd01581 318 KIDEVFIGSCMTNIGHFRAAAKILRGKEFKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVAD 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 704427622 774 GATVMSTSTRNFPNRLGKNTNVYLGSAELAAICSRLGRI 812
Cdd:cd01581 398 GATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| Aconitase_2_N |
pfam06434 |
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several ... |
158-372 |
9.29e-135 |
|
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several bacterial Aconitate hydratase 2 proteins and is found in conjunction with pfam00330.
Pssm-ID: 461912 [Multi-domain] Cd Length: 204 Bit Score: 399.28 E-value: 9.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 158 VTVFKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSS 237
Cdd:pfam06434 1 VTVFKVEGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG------------PLKTIAELKKKGHPLAYVGDVVGTGSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 238 RKSATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIK-NGETIA 316
Cdd:pfam06434 69 RKSATNSVLWHIGEDIPYVPNKRTGGVVIGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVITIYPYEGKITNeNGEVIS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 704427622 317 EFTVKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGY 372
Cdd:pfam06434 149 TFSLKPNTLLDEVRAGGRIPLIIGRGLTDKAREALGLEPSDVFTRPKQPADSGKGY 204
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
373-817 |
2.48e-36 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 142.59 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 373 TLAQKMVGRACGlpegQGIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAyPKPVDVKTHHT 452
Cdd:NF040615 2 TLAEKILSKKLG----KEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP-ANTVKAANMQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 453 LPQFISTRGGIS--LRPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDM 521
Cdd:NF040615 77 ITREFVKEQGIKnfYLGGEGICHQVLpeKGHVLPNMVIAGGDSHTcthgafgAFATGF----GATDMGYIYATGKTWIKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 522 PESVLVRFKGKmQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEIEG--LPDLKVEQAFELSDASAERSAag 599
Cdd:NF040615 153 PKTIRVNIVGK-NENISGKDII------------LKVCKEIGRRGATYMAIEYGGevVKNMDMDGRMVLCNMAIEMGG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 600 csvrlhKEPIIEYINSNIVMLKwmiangyeDERSLGRRIkameAWLADPKLLEPDADADYAAVIEIDLADIhEPIVACPN 679
Cdd:NF040615 218 ------KTGIIEADEITYEYLR--------KEGVSEEEI----AELKKNRITVNEKEENYYKEIEIDITDM-EEQVACPH 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 680 DPDDVKTLSDVAGAKIDEVFIGSCmTN--IGHFRAASKLLEGK---RDipVKLWVAPPTKMDAQQLTEEGHYGVFGTAGA 754
Cdd:NF040615 279 HPDNVKPVSEVEGTEIDQVFIGSC-TNgrLSDLRIAAKYLKGKkvhKD--VRLIVIPASKKVFKQALKEGLIEIFVKAGA 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704427622 755 RTEMPGCSLCMG-NQAQVREGATVMSTSTRNFPNRLG-KNTNVYLGSAELAAICSRLGRIpTREE 817
Cdd:NF040615 356 MICTPGCGPCLGaHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYI-TNEE 419
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
2-851 |
0e+00 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 1873.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 2 RAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELLG 81
Cdd:COG1049 12 RAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEATSPLISPEKAVELLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 82 TMLGGYNIGPLVQLLDDAEVGTIAADALKKTLLMFDAFHDVKEKADKGNANAKSVLQSWADAEWFTSRPEVPQSLTVTVF 161
Cdd:COG1049 92 TMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKAGNAYAKQVLQSWADAEWFTSRPELPEKITVTVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 162 KVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSSRKSA 241
Cdd:COG1049 172 KVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG------------PLKTIAELKAKGHPVAYVGDVVGTGSSRKSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 242 TNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIK-NGETIAEFTV 320
Cdd:COG1049 240 TNSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVIDIYPYEGKITKeNGEVISTFEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 321 KSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLpegQGIRPGTYCEPK 400
Cdd:COG1049 320 KPDTLLDEVRAGGRIPLIIGRGLTDKAREALGLPPSDVFRRPEAPADSGKGYTLAQKMVGKACGV---EGVRPGTYCEPK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 401 MTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLNRML 480
Cdd:COG1049 397 MTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIHSWLNRML 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 481 LPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLTVAK 560
Cdd:COG1049 477 LPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQGLLTVEK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 561 QGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRRIKA 640
Cdd:COG1049 557 KGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDARTLERRIAA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 641 MEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLLEGK 720
Cdd:COG1049 637 MEEWLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEGK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 721 RDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYLGSA 800
Cdd:COG1049 717 GNLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLGSA 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 704427622 801 ELAAICSRLGRIPTREEYMADMGVINKSGDQIYQYLNFDRIPDYKDVADVI 851
Cdd:COG1049 797 ELAAVCALLGRLPTVEEYMEYVKKIDPMADDIYRYLNFDQIEEYQEKADVV 847
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
1-838 |
0e+00 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 1767.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 1 DRAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELL 80
Cdd:PRK09238 11 ERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPLISPEKAVELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 81 GTMLGGYNIGPLVQLLDDAEVGTIAADALKKTLLMFDAFHDVKEKADKGNANAKSVLQSWADAEWFTSRPEVPQSLTVTV 160
Cdd:PRK09238 91 GTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAGNAYAKEVLESWADAEWFTSRPELPEKITVTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 161 FKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSSRKS 240
Cdd:PRK09238 171 FKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG------------PIKQIEELKKKGHPVAYVGDVVGTGSSRKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 241 ATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIK-NGETIAEFT 319
Cdd:PRK09238 239 ATNSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSGALPIELDVSKLNMGDVIDIYPYKGKIRNeTGEVIATFK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 320 VKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLPegqGIRPGTYCEP 399
Cdd:PRK09238 319 LKTDVLLDEVRAGGRIPLIIGRGLTTKAREALGLPPSDVFRKPKQPADSGKGFTLAQKMVGRACGVP---GVRPGTYCEP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 400 KMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLNRM 479
Cdd:PRK09238 396 KMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 480 LLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLTVA 559
Cdd:PRK09238 476 LLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQGLLTVE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 560 KQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRRIK 639
Cdd:PRK09238 556 KKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDARTLERRIA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 640 AMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLLEG 719
Cdd:PRK09238 636 AMEEWLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEG 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 720 KR-DIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYLG 798
Cdd:PRK09238 716 KKgQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLG 795
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 704427622 799 SAELAAICSRLGRIPTREEYMADMGVINKSGDQIYQYLNF 838
Cdd:PRK09238 796 SAELAAVCALLGRIPTVEEYQEYVAEIDATADDIYRYLNF 835
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
1-853 |
0e+00 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 1448.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 1 DRAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELL 80
Cdd:PLN00094 80 ERAQEGIAPKPLDAKQVSELIAQLEAPKSEDADRLVDLLVNRVPPGVDEAAYVKASWLAAVAKGETRSPLISRARAVEIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 81 GTMLGGYNIGPLVQLLDDAEVGTIAADALKKTLLMFDAFHDVKEKADKGNANAKSVLQSWADAEWFTSRPEVPQSLTVTV 160
Cdd:PLN00094 160 GTMQGGYNISPLVDALDDDELGRIAADQLSHTLLVFDAFHDVQAKAKKGNAYATQVMESWADAEWFTKKPPVPEKITVTV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 161 FKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGAafepeedgkRGPVQFIESLKEKGHLVAYVGDVVGTGSSRKS 240
Cdd:PLN00094 240 FKVTGETNTDDLSPAQDAWSRPDIPLHALAMLKNPREGI---------QGPIAQIEELKKKGHPLAYVGDVVGTGSSRKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 241 ATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIKNG--ETIAEF 318
Cdd:PLN00094 311 ATNSVLWFMGDDIPNVPNKRTGGVCIGGKIAPIFFNTMEDSGALPIEMDVKNLNMGDVIDIYPYEGVVKRHGtdEVITTF 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 319 TVKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLPEGqgIRPGTYCE 398
Cdd:PLN00094 391 SLKTPVLLDEVRAGGRIPLIIGRGLTSKAREALGLDASDVFRMPSVPESKPKGFTLAQKMVGKACGVDEG--ILPGTYCE 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 399 PKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLNR 478
Cdd:PLN00094 469 PRMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVVTHHTLPDFIRNRGGVSLRPGDGVIHSWLNR 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 479 MLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLTV 558
Cdd:PLN00094 549 MLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIPYTAIQDGLLTV 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 559 AKQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRRI 638
Cdd:PLN00094 629 EKKGKKNVFSGRILEIEGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIEYLNSNVVMLKWMIAEGYGDRRTLERRI 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 639 KAMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLL- 717
Cdd:PLN00094 709 ARMQQWLADPELLEADPDAEYAAVIEIDMDEIKEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCMTNIGHFRAAGKLLn 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 718 EGKRDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYL 797
Cdd:PLN00094 789 DNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARVAEKSTVVSTSTRNFPNRLGKGANVYL 868
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 704427622 798 GSAELAAICSRLGRIPTREEYMADMGVINKSGDQIYQYLNFDRIPDYKDVADVIEV 853
Cdd:PLN00094 869 ASAELAAVAAILGRLPTVEEYLSYMEKLDATASDTYRYLNFDELPEYVESAEKVEI 924
|
|
| acnB |
TIGR00117 |
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This ... |
1-846 |
0e+00 |
|
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This model describes aconitase 2, AcnB, which has weak similarity to aconitase 1. It is found almost exclusively in the Proteobacteria. [Energy metabolism, TCA cycle]
Pssm-ID: 129223 [Multi-domain] Cd Length: 844 Bit Score: 1416.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 1 DRAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELL 80
Cdd:TIGR00117 11 ERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKCPLISPEKAIELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 81 GTMLGGYNIGPLVQLLD--DAEVGTIAADALKKTLLMFDAFHDVKEKAdKGNANAKSVLQSWADAEWFTSRPEVPQSLTV 158
Cdd:TIGR00117 91 GTMQGGYNVHPLIDALDsqDANIAPIAAKALSHTLLVFDNFYDVEEKS-KTNEYAKQVMQSWADAEWFLNKPALAEKITV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 159 TVFKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaaFEPEedgkrgpvqfIESLKEKGHLVAYVGDVVGTGSSR 238
Cdd:TIGR00117 170 TVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREG--IEPQ----------IEALKQKGFPVAYVGDVVGTGSSR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 239 KSATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGK-AIKNGETIAE 317
Cdd:TIGR00117 238 KSATNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDSGALPIEVDVSNLNMGDVIDIYPYKGEiTNHEGELLAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 318 FTVKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGYTLAQKMVGRACGLpegQGIRPGTYC 397
Cdd:TIGR00117 318 FELKPETLLDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQPKAPAESDKGFTLAQKMVGRACGV---KGIRPGTYC 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 398 EPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLN 477
Cdd:TIGR00117 395 EPKMTTVGSQDTTGPMTRDELKELACLGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGVIHSWLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 478 RMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGLLT 557
Cdd:TIGR00117 475 RMLLPDTVGTGGDSHTRFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAIKQGLLT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 558 VAKQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWMIANGYEDERSLGRR 637
Cdd:TIGR00117 555 VEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 638 IKAMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNIGHFRAASKLL 717
Cdd:TIGR00117 635 IQGMEKWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSCMTNIGHFRAAGKIL 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 718 EGKRDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYL 797
Cdd:TIGR00117 715 DAAGQLPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVADGATVFSTSTRNFPNRMGTGANVYL 794
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 704427622 798 GSAELAAICSRLGRIPTREEYMADMGVINKSG-DQIYQYLNFDRIPDYKD 846
Cdd:TIGR00117 795 GSAELAAVCALLGKIPTPEEYQTYVSEKDKTAvDKTYRYLNFNQLSNFTE 844
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
374-812 |
0e+00 |
|
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: 859.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 374 LAQKMVGRACGlpeGQGIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTL 453
Cdd:cd01581 1 LAQKIVGRACG---VKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 454 PQFISTRGGISLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM 533
Cdd:cd01581 78 PDFISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 534 QPGVTLRDLVNAIPLYAIKQGLLTVAKQGKKNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYI 613
Cdd:cd01581 158 QPGITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 614 NSNIVMLKWMIANGYEDERSLGRRIKAMEAWLADPKLLEPDADADYAAVIEIDLADIHEPIVACPNDPDDVKTLSDVAGA 693
Cdd:cd01581 238 ESNVVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 694 KIDEVFIGSCMTNIGHFRAASKLLEGKRDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVRE 773
Cdd:cd01581 318 KIDEVFIGSCMTNIGHFRAAAKILRGKEFKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVAD 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 704427622 774 GATVMSTSTRNFPNRLGKNTNVYLGSAELAAICSRLGRI 812
Cdd:cd01581 398 GATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| Aconitase_2_N |
pfam06434 |
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several ... |
158-372 |
9.29e-135 |
|
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several bacterial Aconitate hydratase 2 proteins and is found in conjunction with pfam00330.
Pssm-ID: 461912 [Multi-domain] Cd Length: 204 Bit Score: 399.28 E-value: 9.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 158 VTVFKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSS 237
Cdd:pfam06434 1 VTVFKVEGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPG------------PLKTIAELKKKGHPLAYVGDVVGTGSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 238 RKSATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRPYDGKAIK-NGETIA 316
Cdd:pfam06434 69 RKSATNSVLWHIGEDIPYVPNKRTGGVVIGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVITIYPYEGKITNeNGEVIS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 704427622 317 EFTVKSDVLFDEVRAGGRIPLIIGRGLTAKAREALGLPPSTLFRLPNNPADTGKGY 372
Cdd:pfam06434 149 TFSLKPNTLLDEVRAGGRIPLIIGRGLTDKAREALGLEPSDVFTRPKQPADSGKGY 204
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
403-804 |
4.77e-117 |
|
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: 361.04 E-value: 4.77e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 403 SVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYP--KPVDVKTHHTLPQFISTRGGISLRPGDGVIHSWLNRML 480
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGKVADPSQIACVHDHAVQleKPVNNEGHKFLSFFAALQGIAFYRPGVGIIHQIMVENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 481 -LPDTVGTGGDSHTRF---PIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVNAIPLYAIKQGll 556
Cdd:cd01351 81 aLPGDLLVGSDSHTTSyggLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 557 tvakqgkkniFSGRILEIEGLP--DLKVEQAFELSDASAERSAAGCSVRLHKEPIIEYINSNIVMLKWmiangyedersl 634
Cdd:cd01351 159 ----------VLNRIVEFYGEGvsSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKN------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 635 grrikameAWLADPKLLEPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCMTNI-GHFRAA 713
Cdd:cd01351 217 --------LWLAFPEELLADEGAEYDQVIEIDLSEL-EPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRySDMLAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 714 SKLLEG-KRDIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQA-QVREGATVMSTSTRNFPNRLG- 790
Cdd:cd01351 288 AKLLKGaKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGArLVADGEVGVSSGNRNFPGRLGt 367
|
410
....*....|....
gi 704427622 791 KNTNVYLGSAELAA 804
Cdd:cd01351 368 YERHVYLASPELAA 381
|
|
| Aconitase_B_N |
pfam11791 |
Aconitate B N-terminal domain; This family represents the N-terminal domain of Aconitase B. |
1-146 |
5.42e-88 |
|
Aconitate B N-terminal domain; This family represents the N-terminal domain of Aconitase B.
Pssm-ID: 463349 [Multi-domain] Cd Length: 151 Bit Score: 275.48 E-value: 5.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 1 DRAALGIPPLPLSAQQTADLIELLKNPPDGEAQNLLELLTYRVPAGVDDAAKVKASYLAAVAFGTESCALIDRAKATELL 80
Cdd:pfam11791 7 ERAALGIPPLPLDAEQTAELIELLKNPPAGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAIAKGEASSPLISPEEAVELL 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704427622 81 GTMLGGYNIGPLVQLLDDAEVGTIAADALKKTLLMFDAFHDVKEKAdKGNANAKSVLQSWADAEWF 146
Cdd:pfam11791 87 GTMLGGYNVAPLIDLLDDAELAAEAAEALKKTLLVYDAFHDVAELA-KANAYAKEVLESWANAEWF 151
|
|
| AcnB_Swivel |
cd01576 |
Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of ... |
161-303 |
5.84e-74 |
|
Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of the TCA cycle. It catalyses the formation of cis-aconitate from citrate. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The domain structure of Aconitase B is different from other Aconitases in that he swivel domain that is found at N-terminus of B family is normally found at C-terminus for other Aconitases. In most members of the family, there is also a HEAT domain before domain 4, which is believed to play a role in protein-protein interaction.
Pssm-ID: 238808 [Multi-domain] Cd Length: 131 Bit Score: 237.37 E-value: 5.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 161 FKVPGETNTDDLSPAPDATTRPDIPMHALAMLKNKRDGaafepeedgkrgPVQFIESLKEKGHLVAYVGDVVGTGSSRKS 240
Cdd:cd01576 1 FKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNKREG------------EIVAIAQLKPKGHPVAYVGDVVGTGSSRKS 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704427622 241 ATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSKMEMGDVVELRP 303
Cdd:cd01576 69 ATNSVLWHTGKDIPFVPNKRAGGVVLGGKIAPIFFNTAEDSGALPIQLDVSVLDMGDILNIDG 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
468-812 |
1.33e-53 |
|
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: 190.86 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 468 GDGVIHSWLNRM--LLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVT 538
Cdd:cd01583 68 RQGICHVILPEKglTLPGMTIVGGDSHTcthgafgAFATGI----GTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 539 LRDLVnaipLYAIkqGLLTVAKQGKKNI-FSGrileiEGLPDLKVEQAFELSDASAERSA-AGcsvrlhkepiieYINSN 616
Cdd:cd01583 144 AKDVI----LYII--GKIGVDGATYKAMeFAG-----EAIESLSMEERMTLCNMAIEAGAkAG------------IVAPD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 617 IVMLKWMIANGYederslgrrikameawlADPKLLEPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVAGAKID 696
Cdd:cd01583 201 ETTFEYLKGRGK-----------------AYWKELKSDEDAEYDKVVEIDASEL-EPQVAWPHSPDNVVPVSEVEGIKID 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 697 EVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMG-NQAQVR 772
Cdd:cd01583 263 QVFIGSC-TNgrLEDLRAAAEILKGRKVADgVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLA 341
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 704427622 773 EGATVMSTSTRNFPNRLGKNTN-VYLGSAELAAICSRLGRI 812
Cdd:cd01583 342 PGERCVSTSNRNFKGRMGSPGArIYLASPATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
371-812 |
7.16e-53 |
|
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: 189.86 E-value: 7.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 371 GYTLAQKMVGRACGlpegQGIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVKT 449
Cdd:COG0065 2 GMTLAEKILARHAG----REVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKvWDPDRIVAVFDHNVPTKDPKSAEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 450 HHTLPQFIStRGGISL-RPGD-GVIHswlnrMLLP--------DTVgTGGDSHT-------RFPIGIsfpaGSGLVAFAA 512
Cdd:COG0065 78 VKTLREFAK-EFGITFfDVGDpGICH-----VVLPeqglvlpgMTI-VGGDSHTcthgafgAFAFGI----GTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 513 ATGVMPLDMPESVLVRFKGKMQPGVTLRDLVnaipLYAIkqGLLTVAkqGkkniFSGRILEI--EGLPDLKVEQAFELSD 590
Cdd:COG0065 147 ATGTLWFKVPETMRIEVTGKLPPGVTAKDLI----LAII--GKIGAD--G----ATGKAIEFagEAIRALSMEERMTLCN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 591 ASAERSA-AGcsvrlhkepIIEYinsnivmlkwmiangyeDERSLgrrikameAWL-----ADPKLLEPDADADYAAVIE 664
Cdd:COG0065 215 MAIEAGAkAG---------IIAP-----------------DETTF--------EYLkgrpfAPWRTLKSDEDAVYDKEVE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 665 IDLADIhEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLT 741
Cdd:COG0065 261 IDASDL-EPQVAWPHSPDNVVPVSELEGIKIDQVFIGSC-TNgrIEDLRAAAEILKGRKVAPgVRAIVVPGSQEVYRQAE 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704427622 742 EEGHYGVFGTAGARTEMPGCSLCMG-NQAQVREGATVMSTSTRNFPNRLGKNT-NVYLGSAELAAICSRLGRI 812
Cdd:COG0065 339 AEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAPGERCASTSNRNFEGRMGSPGsRTYLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
371-819 |
9.81e-51 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 183.84 E-value: 9.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 371 GYTLAQKMVGRACGLPEgqgiRPGTYCEPKMTSVGSQDTTGPMTRDELKDLaclG----FSADLVMQSFCHtaAYPKPvD 446
Cdd:PRK00402 2 GMTLAEKILARHSGRDV----SPGDIVEAKVDLVMAHDITGPLAIKEFEKI---GgdkvFDPSKIVIVFDH--FVPAK-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 447 VKTH------------HTLPQFISTRGGIS---------LRPGDGVIhswlnrmllpdtvgtGGDSHT-------RFPIG 498
Cdd:PRK00402 72 IKSAeqqkilrefakeQGIPNFFDVGEGIChqvlpekglVRPGDVVV---------------GADSHTctygalgAFATG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 499 IsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVnaipLYAIkqGLLTVakqgkkNIFSGRILEI--EG 576
Cdd:PRK00402 137 M----GSTDMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVI----LHII--GDIGV------DGATYKALEFtgET 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 577 LPDLKVEQAFELSDASAERSA-AGcsvrlhkepIIEYINSNIVMLKwmiangyederslgrrikamEAWLADPKLLEPDA 655
Cdd:PRK00402 201 IEALSMDERMTLANMAIEAGAkAG---------IFAPDEKTLEYLK--------------------ERAGRDYKPWKSDE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 656 DADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPP 732
Cdd:PRK00402 252 DAEYEEVYEIDLSKL-EPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSC-TNgrLEDLRIAAEILKGRKVAPgVRLIVIPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 733 TKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQV-REGATVMSTSTRNFPNRLGKNT-NVYLGSAELAAICSRLG 810
Cdd:PRK00402 330 SQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVlAPGEVCLSTTNRNFKGRMGSPEsEVYLASPAVAAASAVTG 409
|
....*....
gi 704427622 811 RIPTREEYM 819
Cdd:PRK00402 410 KITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
373-812 |
6.95e-50 |
|
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: 181.49 E-value: 6.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 373 TLAQKMVGRAcglpEGQGIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVKTHH 451
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKvWNPEKIVIVFDHQVPADTIKAAEMQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 452 TLPQFISTRGGISL-RPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDM 521
Cdd:TIGR01343 77 LAREFVKKQGIKYFyDVGEGICHQVLpeKGLVKPGDLVVGADSHTctygafgAFATGM----GSTDMAYAIATGKTWFKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 522 PESVLVRFKGKMQPGVTLRDLVnaipLYAIKQglltVAKQGKknifSGRILEIEG--LPDLKVEQAFELSDASAERSAag 599
Cdd:TIGR01343 153 PETIRVNITGKLNPGVTAKDVI----LEVIGE----IGVDGA----TYMAMEFGGetVKNMDMEGRLTLANMAIEAGG-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 600 csvrlhKEPIIEyinsnivmlkwmiangyEDERSLGRRIKAMEAwlaDPKLLEPDADADYAAVIEIDLADIhEPIVACPN 679
Cdd:TIGR01343 219 ------KTGIIE-----------------PDEKTIQYLKERRKE---PFRVYKSDEDAEYAKEIEIDASQI-EPVVACPH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 680 DPDDVKTLSDVAGAKIDEVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLTEEGHYGVFGTAGART 756
Cdd:TIGR01343 272 NVDNVKPVSEVEGTEIDQVFIGSC-TNgrLEDLRVAAKILKGRKVAPdVRLIVIPASRAVYLQALKEGLIEIFVKAGAVV 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 704427622 757 EMPGCSLCMG-NQAQVREGATVMSTSTRNFPNRLG-KNTNVYLGSAELAAICSRLGRI 812
Cdd:TIGR01343 351 STPGCGPCLGsHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYI 408
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
373-817 |
1.13e-48 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 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: 273960 Cd Length: 413 Bit Score: 178.03 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 373 TLAQKMVGRACGLPegqgIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLG-FSADLVMQSFCHTAAYPKPVDVKTHH 451
Cdd:TIGR02086 2 TLAEKILSEKVGRP----VCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARvWDPEKIVIAFDHNVPPPTVEAAEMQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 452 TLPQFISTRGGISLRPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMP 522
Cdd:TIGR02086 78 EIREFAKRHGIKNFDVGEGICHQILaeEGYALPGMVVVGGDSHTctsgafgAFATGM----GATDMAIALATGKTWIKVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 523 ESVLVRFKGKMQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEIEGLP--DLKVEQAFELSDASAERSAAGC 600
Cdd:TIGR02086 154 ETIRVVVEGKPEEGVTAKDVA------------LHIVGELGADGATYMAIEFFGLPieNMDMDGRLTLCNMAVEMGAKAG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 601 SVRLHKEPiieyinsnivmlkwmiangYEDERSLGRRikameawlaDPKLLEPDADADYAAVIEIDLADIhEPIVACPND 680
Cdd:TIGR02086 222 IIEPDEET-------------------YEYLKKRRGL---------EFRILVPDPGANYYKEIEIDLSDL-EPQVAVPHS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 681 PDDVKTLSDVAGAKIDEVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTE 757
Cdd:TIGR02086 273 VDNVKPVSDVEGTEIDQVFIGSC-TNgrLEDLRIAAEILKGRRVHPdVRLIVIPASRKVYLRALEEGIILTLVRAGAMIC 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704427622 758 MPGCSLCMGNQAQV-REGATVMSTSTRNFPNRLG-KNTNVYLGSAELAAICSRLGRIPTREE 817
Cdd:TIGR02086 352 PPGCGPCLGAHMGVlGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITDPED 413
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
404-804 |
1.78e-42 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 161.43 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 404 VGSQDTTGPMTrdeLKDLACLG---FSADLVMQSFCHTAaypkPVDVKTHHTLP-----------------QFI---STR 460
Cdd:pfam00330 23 VLMHDVTSPQA---FVDLRAAGravRRPGGTPATIDHLV----PTDLVIDHAPDaldkniedeisrnkeqyDFLewnAKK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 461 GGISL-RPGDGVIHSWL--NRMLLPDTVGTGGDSHTR---------FPIGisfpaGSGLVAfAAATGVMPLDMPESVLVR 528
Cdd:pfam00330 96 FGIRFvPPGQGIVHQVGleYGLALPGMTIVGTDSHTTthgglgalaFGVG-----GSEAEH-VLATQPLEMKKPKVVGVK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 529 FKGKMQPGVTLRDLVNAIplyaikQGLLTVAKqgkkniFSGRILEI--EGLPDLKVEQAFELSDASAERSA-AGcsvrlh 605
Cdd:pfam00330 170 LTGKLPPGVTAKDVILAI------IGKLGVKG------GTGKVVEFfgPGVRSLSMEGRATICNMAIEYGAtAG------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 606 kepiieYINSNIVMLKWMiangyedeRSLGRR-IKAMEAWL--ADPKLLEPDADADYAAVIEIDLADIhEPIVACPNDPD 682
Cdd:pfam00330 232 ------LFPPDETTFEYL--------RATGRPeAPKGEAYDkaVAWKTLASDPGAEYDKVVEIDLSTI-EPMVTGPTRPQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 683 DVKTLSDVA-----------------------------GAKIDEVFIGSCmTN--IGHFRAASKLLE-----GKRDIP-V 725
Cdd:pfam00330 297 DAVPLSELVpdpfadavkrkaaeraleymglgpgtplsDGKVDIAFIGSC-TNssIEDLRAAAGLLKkavekGLKVAPgV 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704427622 726 KLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVREGATVMSTSTRNFPNRLGKNTNVYLGSAELAA 804
Cdd:pfam00330 376 KASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVA 454
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
406-812 |
3.33e-41 |
|
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: 155.68 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 406 SQDTTGPMtrdelkdlACLGFSA--------DLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVIHS-WL 476
Cdd:cd01585 5 TQDATGTM--------AYLQFEAmgvdrvrtELSVSYVDHNTLQTDFENADDHRFLQTVAARYGIYFSRPGNGICHQvHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 477 NRMLLPDTVGTGGDSHTRFPIGISFPA--GSGL-VAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLV-NAIPLYAIK 552
Cdd:cd01585 77 ERFAVPGKTLLGSDSHTPTAGGLGMLAigAGGLdVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIlELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 553 QGLltvakqgkknifsGRILEI--EGLPDLKVEQAFELSDASAERSAAgCSVrlhkepiieyINSNIVMLKWMIANGYED 630
Cdd:cd01585 157 GGV-------------GKIFEYtgPGVATLSVPERATITNMGAELGAT-TSI----------FPSDERTREFLAAQGRED 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 631 ErslgrrikameaWLAdpklLEPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVAGAKIDEVFIGSCmTNIGH- 709
Cdd:cd01585 213 D------------WVE----LAADADAEYDEEIEIDLSEL-EPLIARPHSPDNVVPVREVAGIKVDQVAIGSC-TNSSYe 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 710 -FRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMG-NQAQVREGATVmSTSTRNFP 786
Cdd:cd01585 275 dLMTVAAILKGRRVHPhVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGmGQAPPTGGVSV-RTFNRNFE 353
|
410 420
....*....|....*....|....*..
gi 704427622 787 NRLG-KNTNVYLGSAELAAICSRLGRI 812
Cdd:cd01585 354 GRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
407-812 |
8.74e-37 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 147.60 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 407 QDTTGPMtrdelkdlACLGFSA--------DLvmqsfchTAAYpkpVDvkthHTLPQ----------FIST---RGGISL 465
Cdd:PRK07229 35 QDATGTM--------AYLQFEAmgldrvktEL-------SVQY---VD----HNLLQadfenaddhrFLQSvaaKYGIYF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 466 -RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfpigisfPAGSGL-----------VAFAAATGVMPLDMPESVLVRFKGK 532
Cdd:PRK07229 93 sKPGNGICHQvHLERFAFPGKTLLGSDSHT--------PTAGGLgmlaigaggldVALAMAGGPYYLKMPKVVGVKLTGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 533 MQPGVTLRDLVnaipLYAIkqGLLTVaKQGKknifsGRILEI--EGLPDLKVEQAFELSDASAERSAAgCSVrlhkepii 610
Cdd:PRK07229 165 LPPWVSAKDVI----LELL--RRLTV-KGGV-----GKIIEYfgPGVATLSVPERATITNMGAELGAT-TSI-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 611 eyINSNIVMLKWMIANGYEDErslgrrikAMEawladpklLEPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDV 690
Cdd:PRK07229 224 --FPSDERTREFLKAQGREDD--------WVE--------LLADPDAEYDEVIEIDLSEL-EPLIAGPHSPDNVVPVSEV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 691 AGAKIDEVFIGSCmTNIGH--FRAASKLLEGKR-DIPVKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSLCMGN 767
Cdd:PRK07229 285 AGIKVDQVLIGSC-TNSSYedLMRAASILKGKKvHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 704427622 768 QAQVREGATVMSTSTRNFPNRLG-KNTNVYLGSAELAAICSRLGRI 812
Cdd:PRK07229 364 GQAPATGNVSLRTFNRNFPGRSGtKDAQVYLASPETAAASALTGVI 409
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
373-817 |
2.48e-36 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 142.59 E-value: 2.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 373 TLAQKMVGRACGlpegQGIRPGTYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAyPKPVDVKTHHT 452
Cdd:NF040615 2 TLAEKILSKKLG----KEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP-ANTVKAANMQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 453 LPQFISTRGGIS--LRPGDGVIHSWL--NRMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDM 521
Cdd:NF040615 77 ITREFVKEQGIKnfYLGGEGICHQVLpeKGHVLPNMVIAGGDSHTcthgafgAFATGF----GATDMGYIYATGKTWIKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 522 PESVLVRFKGKmQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEIEG--LPDLKVEQAFELSDASAERSAag 599
Cdd:NF040615 153 PKTIRVNIVGK-NENISGKDII------------LKVCKEIGRRGATYMAIEYGGevVKNMDMDGRMVLCNMAIEMGG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 600 csvrlhKEPIIEYINSNIVMLKwmiangyeDERSLGRRIkameAWLADPKLLEPDADADYAAVIEIDLADIhEPIVACPN 679
Cdd:NF040615 218 ------KTGIIEADEITYEYLR--------KEGVSEEEI----AELKKNRITVNEKEENYYKEIEIDITDM-EEQVACPH 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 680 DPDDVKTLSDVAGAKIDEVFIGSCmTN--IGHFRAASKLLEGK---RDipVKLWVAPPTKMDAQQLTEEGHYGVFGTAGA 754
Cdd:NF040615 279 HPDNVKPVSEVEGTEIDQVFIGSC-TNgrLSDLRIAAKYLKGKkvhKD--VRLIVIPASKKVFKQALKEGLIEIFVKAGA 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704427622 755 RTEMPGCSLCMG-NQAQVREGATVMSTSTRNFPNRLG-KNTNVYLGSAELAAICSRLGRIpTREE 817
Cdd:NF040615 356 MICTPGCGPCLGaHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYI-TNEE 419
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
479-812 |
1.33e-22 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 101.91 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 479 MLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGVTLRDLVnaipLYAI 551
Cdd:PRK12466 119 LTLPGMVIVCGDSHTttygalgALAFGI----GTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLI----LALI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 552 KQgLLTVAKQGKKNIFSG---RILEIEG---LPDLKVEqafelsdASAeRSAagcsvrlhkepiieyinsnivmlkwMIA 625
Cdd:PRK12466 191 AR-IGADGATGYAIEFAGeaiRALSMEGrmtLCNMAVE-------AGA-RGG-------------------------LIA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 626 ngyEDERSL----GR----RIKAMEAWLADPKLLEPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSD-------- 689
Cdd:PRK12466 237 ---PDETTFdylrGRprapKGALWDAALAYWRTLRSDADAVFDREVEIDAADI-APQVTWGTSPDQAVPITGrvpdpaae 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 690 -----------------------VAGAKIDEVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLTEE 743
Cdd:PRK12466 313 adparraameraldymgltpgtpLAGIPIDRVFIGSC-TNgrIEDLRAAAAVLRGRKVAPgVRAMVVPGSGAVRRQAEAE 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 744 GHYGVFGTAGARTEMPGCSLCMG-NQAQVREGATVMSTSTRNFPNRLGKNTNVYLGSAELAAICSRLGRI 812
Cdd:PRK12466 392 GLARIFIAAGFEWREPGCSMCLAmNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHI 461
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
639-804 |
5.06e-20 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 94.03 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 639 KAMEAWladpKLLEPDADADYAAVIEIDLADIhEPIV--------------ACPnDPDDVKTLSDVAGA----------- 693
Cdd:PRK05478 257 KAVAYW----KTLKSDEDAVFDKVVTLDAADI-EPQVtwgtnpgqvisidgKVP-DPEDFADPVKRASAeralaymglkp 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 694 -------KIDEVFIGSCmTN--IGHFRAASKLLEGKRDIP-VKLWVAPPTKMDAQQLTEEGHYGVFGTAGARTEMPGCSL 763
Cdd:PRK05478 331 gtpitdiKIDKVFIGSC-TNsrIEDLRAAAAVVKGRKVAPgVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSM 409
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 704427622 764 CMG-NQAQVREGATVMSTSTRNFPNRLGKNTNVYLGSAELAA 804
Cdd:PRK05478 410 CLAmNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAA 451
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
222-303 |
8.58e-12 |
|
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: 61.72 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 222 GHLVAYVGDVVGTGSSRKSATNSVLWFTGEdipfvpnkrfggVCLGSKIAPIFYNTMEDAGALPIELDVS----KMEMGD 297
Cdd:cd00404 15 GPGVVIGDENYGTGSSREHAALELRLLGGR------------AVIAKSFARIFFRNLVDQGLLPLEFADPedylKLHTGD 82
|
....*.
gi 704427622 298 VVELRP 303
Cdd:cd00404 83 ELDIYP 88
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
467-689 |
4.28e-10 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 63.67 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 467 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAG---SGLVAFAAATGvMPLDM--PESVLVRFK 530
Cdd:PLN00070 214 PGSGIVHQvnleYLGRvvfntdgILYPDSV-VGTDSHTTMIDGLGV-AGwgvGGIEAEAAMLG-QPMSMvlPGVVGFKLS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 531 GKMQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEI--EGLPDLKVEQAFELSDASAERSAAgcsvrlhkep 608
Cdd:PLN00070 291 GKLRDGVTATDLV------------LTVTQMLRKHGVVGKFVEFygEGMSELSLADRATIANMSPEYGAT---------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 609 iIEYINSNIVMLKWMIANGYEDErslgrRIKAMEAWLADPKLL----EPDADADYAAVIEIDLADIhEPIVACPNDPDDV 684
Cdd:PLN00070 349 -MGFFPVDHVTLQYLKLTGRSDE-----TVAMIEAYLRANKMFvdynEPQQERVYSSYLELDLEDV-EPCISGPKRPHDR 421
|
....*
gi 704427622 685 KTLSD 689
Cdd:PLN00070 422 VPLKE 426
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
458-812 |
9.39e-09 |
|
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: 58.39 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 458 STRGGISLRP-GDGVIHSWL--NRMLLPDTVGTGGDSHTRFPIGISfPAGSGLVAFAAA----TGVMPLDMPESVLVRFK 530
Cdd:cd01582 55 AKKHGIDFYPaGRGIGHQIMieEGYAFPGTLAVASDSHSNMYGGVG-CLGTPIVRTDAAaiwaTGQTWWQIPPVAKVELK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 531 GKMQPGVTLRDLVNAIPLYAIKQGLLTVAKQgkkniFSGrileiEGLPDLKVEQAFELSDASAErsaagcsvrlhkepii 610
Cdd:cd01582 134 GQLPKGVTGKDVIVALCGLFNKDQVLNHAIE-----FTG-----SGLNSLSVDTRLTIANMTTE---------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 611 eyinsnivmlkwmiangyederslgrrikameaWLADPKLLEPDADAdyaavIEIDLADIhEPIVACPNDPDDVKTLSDV 690
Cdd:cd01582 188 ---------------------------------WGALSGLFPTDAKH-----LILDLSTL-SPYVSGPNSVKVSTPLKEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 691 AGA--KIDEVFIGSCM-TNIGHFRAASKLLEGKRDIPVKLWVAP-----------PTKMDAQqltEEGHYGVFGTAGART 756
Cdd:cd01582 229 EAQniKINKAYLVSCTnSRASDIAAAADVVKGKKEKNGKIPVAPgvefyvaaassEVQAAAE---KNGDWQTLLEAGATP 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704427622 757 EMPGCSLCMG-NQAQVREGATVMSTSTRNFPNRLG-KNTNVYLGSAELAAICSRLGRI 812
Cdd:cd01582 306 LPAGCGPCIGlGQGLLEPGEVGISATNRNFKGRMGsTEALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
466-812 |
5.08e-08 |
|
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: 56.29 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 466 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfpigisfPAGSGL------VAFAAATGVMP-----LDMPESVLVRFKGKM 533
Cdd:cd01584 73 KPGSGIIHQIvLENYAFPGLLMIGTDSHT--------PNAGGLggiaigVGGADAVDVMAgipweLKCPKVIGVKLTGKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 534 QPGVTLRDLVNAIplyaikQGLLTVaKQGkknifSGRILEI--EGLPDLKVEQAFELSDASAERSAAgCSVRLHKEPIIE 611
Cdd:cd01584 145 SGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYfgPGVDSLSCTGMGTICNMGAEIGAT-TSVFPYNERMKK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 612 YInsnivmlkwmiangyedeRSLGRRIKAMEAWLADPKLLEPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVA 691
Cdd:cd01584 212 YL------------------KATGRAEIADLADEFKDDLLVADEGAEYDQLIEINLSEL-EPHINGPFTPDLATPVSKFK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 692 GA--------KIDEVFIGSCmTNIGH---FRAAS-------KLLEGKrdipVKLWVAPPTKMDAQQLTEEGHYGVFGTAG 753
Cdd:cd01584 273 EVaekngwplDLRVGLIGSC-TNSSYedmGRAASiakqalaHGLKCK----SIFTITPGSEQIRATIERDGLLQTFRDAG 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704427622 754 ARTEMPGCSLCMG--NQAQVREGA--TVMSTSTRNFPNRLGKN--TNVYLGSAELAAICSRLGRI 812
Cdd:cd01584 348 GIVLANACGPCIGqwDRKDIKKGEknTIVTSYNRNFTGRNDANpaTHAFVASPEIVTAMAIAGTL 412
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
482-788 |
7.07e-08 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 56.48 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 482 PDT-VGTggDSHTRFPIGISFPA---GsGLVAFAAATGvMPLDM--PESVLVRFKGKMQPGVTLRDLVnaiplyaikqgl 555
Cdd:PRK12881 205 PDTlVGT--DSHTTMINGIGVLGwgvG-GIEAEAVMLG-QPVYMliPDVVGVELTGKLREGVTATDLV------------ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 556 LTVAKQGKKNIFSGRILEI--EGLPDLKVeqafelsdasAERSAagcsvrlhkepiieyinsnivmlkwmIAN-----G- 627
Cdd:PRK12881 269 LTVTEMLRKEGVVGKFVEFfgEGVASLTL----------GDRAT--------------------------IANmapeyGa 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 628 -----YEDERSL------GR---RIKAMEAWLADPKLL-EPDADADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVAG 692
Cdd:PRK12881 313 tmgffPVDEQTLdylrltGRteaQIALVEAYAKAQGLWgDPKAEPRYTRTLELDLSTV-APSLAGPKRPQDRIALGNVKS 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 693 AkIDEVF------------------------------IGSCmTNIGHFRA--ASKLLEGK---RDIPVKLWV----APPT 733
Cdd:PRK12881 392 A-FSDLFskpvaengfakkaqtsngvdlpdgavaiaaITSC-TNTSNPSVliAAGLLAKKaveRGLTVKPWVktslAPGS 469
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704427622 734 KMDAQQLTEEG------HYGvFGTAGArtempGCSLCMGN---------QAQVREGATVMS--TSTRNFPNR 788
Cdd:PRK12881 470 KVVTEYLERAGllpyleKLG-FGIVGY-----GCTTCIGNsgpltpeieQAITKNDLVAAAvlSGNRNFEGR 535
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
467-690 |
1.44e-06 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 51.94 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 467 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGISFpAGSGlVAFAAATGVM---PLDM--PESVLVRFK 530
Cdd:PTZ00092 182 PGSGIVHQvnleYLARvvfnkdgLLYPDSV-VGTDSHTTMINGLGV-LGWG-VGGIEAEAVMlgqPISMvlPEVVGFKLT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 531 GKMQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEI--EGLPDLKVEQAFELSDASAERSAAgcsvrLHKEP 608
Cdd:PTZ00092 259 GKLSEHVTATDLV------------LTVTSMLRKRGVVGKFVEFygPGVKTLSLADRATIANMAPEYGAT-----MGFFP 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 609 IIEYinsnivMLKWMIANGYEDErslgrRIKAMEAWLADPKLLEPDA-DADYAAVIEIDLADIhEPIVACPNDPDDVKTL 687
Cdd:PTZ00092 322 IDEK------TLDYLKQTGRSEE-----KVELIEKYLKANGLFRTYAeQIEYSDVLELDLSTV-VPSVAGPKRPHDRVPL 389
|
...
gi 704427622 688 SDV 690
Cdd:PTZ00092 390 SDL 392
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
467-812 |
1.77e-06 |
|
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: 51.15 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 467 PGDGVIHS----WLNR-----------MLLPDTVgTGGDSHTRFPIGISFpAGSGlVAFAAATGVM---PLDM--PESVL 526
Cdd:cd01586 91 PGTGIIHQvnleYLARvvftseedgdgVAYPDSV-VGTDSHTTMINGLGV-LGWG-VGGIEAEAVMlgqPISMllPEVVG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 527 VRFKGKMQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEI--EGLPDLKVeqafelsdasAERSAagcsvrl 604
Cdd:cd01586 168 VKLTGKLRPGVTATDLV------------LTVTQMLRKVGVVGKFVEFfgPGVAKLSV----------ADRAT------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 605 hkepiieyinsnivmlkwmIANgyederslgrriKAMEaWLADPKLLEPDADadyaaVIEIDLADIhEPIVACPNDPDD- 683
Cdd:cd01586 219 -------------------IAN------------MAPE-YGATCGFFPVDTQ-----VVELDLSTV-EPSVSGPKRPQDr 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 684 VKTLSDVAGAKIDevfigSCmTN-------IGHFRAASKLLEgkRDIPVKLWV----APPTKMDAQQLTEEG------HY 746
Cdd:cd01586 261 VPLHGSVVIAAIT-----SC-TNtsnpsvmLAAGLLAKKAVE--LGLKVKPYVktslAPGSRVVTKYLEASGllpyleKL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704427622 747 GvFGTAGArtempGCSLCMGNQAQVREG------------ATVMStSTRNFPNRLGKNTN-VYLGSAELAAICSRLGRI 812
Cdd:cd01586 333 G-FHVVGY-----GCTTCIGNSGPLPEEveeaikendlvvAAVLS-GNRNFEGRIHPLVRaNYLASPPLVVAYALAGTV 404
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
467-724 |
3.52e-06 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 50.89 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 467 PGDGVIHS----------WLNR----MLLPDT-VGTggDSHTRFPIGISFPA---GsGLVAFAAATGvMPLDM--PESVL 526
Cdd:PRK09277 176 PGTGICHQvnleylapvvWTREdgelVAYPDTlVGT--DSHTTMINGLGVLGwgvG-GIEAEAAMLG-QPSSMliPEVVG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 527 VRFKGKMQPGVTLRDLVnaiplyaikqglLTVAKQGKKNIFSGRILEI--EGLPDLKVeqafelsdasAERSAagcsvrl 604
Cdd:PRK09277 252 VKLTGKLPEGVTATDLV------------LTVTEMLRKKGVVGKFVEFfgEGLASLSL----------ADRAT------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 605 hkepiieyinsnivmlkwmIAN-----G------YEDERSL------GR---RIKAMEAWLADPKL-LEPDADADYAAVI 663
Cdd:PRK09277 303 -------------------IANmapeyGatcgffPIDEETLdylrltGRdeeQVALVEAYAKAQGLwRDPLEEPVYTDVL 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704427622 664 EIDLADIhEPIVACPNDPDDVKTLSDVAgakidEVFIGSCMTNIGHFRAASKLLEGKRDIP 724
Cdd:PRK09277 364 ELDLSTV-EPSLAGPKRPQDRIPLSDVK-----EAFAKSAELGVQGFGLDEAEEGEDYELP 418
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
482-691 |
9.19e-06 |
|
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: 49.33 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 482 PDT-VGTggDSHTrfP---------IGIsfpaGsGLVAFAAATGvMPLDM--PESVLVRFKGKMQPGVTLRDLVnaiply 549
Cdd:COG1048 203 PDTlVGT--DSHT--TminglgvlgWGV----G-GIEAEAAMLG-QPVSMliPEVVGVKLTGKLPEGVTATDLV------ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704427622 550 aikqglLTVAKQ-GKKNIfSGRILEI--EGLPDLKVeqafelsdasAERSA---------AGCSVRlhkePIIEyinsni 617
Cdd:COG1048 267 ------LTVTEMlRKKGV-VGKFVEFfgPGLASLSL----------ADRATianmapeygATCGFF----PVDE------ 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704427622 618 VMLKWMIANGYEDErslgrRIKAMEAWLADPKL-LEPDA-DADYAAVIEIDLADIhEPIVACPNDPDDVKTLSDVA 691
Cdd:COG1048 320 ETLDYLRLTGRSEE-----QIELVEAYAKAQGLwRDPDApEPYYSDVLELDLSTV-EPSLAGPKRPQDRIPLSDLK 389
|
|
| |
