|
Name |
Accession |
Description |
Interval |
E-value |
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
1-850 |
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: 1701.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 1 MMQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPV 80
Cdd:COG1049 1 MLEAYRKHVAERAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEATSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 81 ITKKDAVFFLGTMLGGYNVKPLVDLLTDAELGADAAEALKQTILIYGSFEDVLALSK-SNANAKAVIQSWADAEWFTSKP 159
Cdd:COG1049 81 ISPEKAVELLGTMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKaGNAYAKQVLQSWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 160 EFPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSAC 239
Cdd:COG1049 161 ELPEKITVTVFKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPLKTIAELKAKGHPVAYVGDVVGTGSSRKSAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 240 NSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKLS 319
Cdd:COG1049 241 NSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVIDIYPYEGKITKENGEVISTFELK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 320 PATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVpKKGQGFTLAQKIIGKACGVEGVLPGTACEPVMTT 399
Cdd:COG1049 321 PDTLLDEVRAGGRIPLIIGRGLTDKAREALGLPPSDVFRRPEAPA-DSGKGYTLAQKMVGKACGVEGVRPGTYCEPKMTT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 400 VGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRLLLPD 479
Cdd:COG1049 400 VGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIHSWLNRMLLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 480 TLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVPKQNK 559
Cdd:COG1049 480 TVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQGLLTVEKKGK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 560 KNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIEDAEK 639
Cdd:COG1049 560 KNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDARTLERRIAAMEE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 640 WLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWEGAAYP 719
Cdd:COG1049 640 WLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEGKGNL 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 720 KTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAELT 799
Cdd:COG1049 720 PTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELA 799
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 800 AVTALMGELPTPAEYFMLYKsKIEPKQAEVYRYLEFDKMGDFELSYIERVA 850
Cdd:COG1049 800 AVCALLGRLPTVEEYMEYVK-KIDPMADDIYRYLNFDQIEEYQEKADVVIP 849
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
1-835 |
0e+00 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 1571.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 1 MMQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPV 80
Cdd:PRK09238 1 MLEAYRKHVAERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 81 ITKKDAVFFLGTMLGGYNVKPLVDLLTDAELGADAAEALKQTILIYGSFEDVLALSKS-NANAKAVIQSWADAEWFTSKP 159
Cdd:PRK09238 81 ISPEKAVELLGTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAgNAYAKEVLESWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 160 EFPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSAC 239
Cdd:PRK09238 161 ELPEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPIKQIEELKKKGHPVAYVGDVVGTGSSRKSAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 240 NSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKLS 319
Cdd:PRK09238 241 NSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSGALPIELDVSKLNMGDVIDIYPYKGKIRNETGEVIATFKLK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 320 PATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVPKkGQGFTLAQKIIGKACGVEGVLPGTACEPVMTT 399
Cdd:PRK09238 321 TDVLLDEVRAGGRIPLIIGRGLTTKAREALGLPPSDVFRKPKQPADS-GKGFTLAQKMVGRACGVPGVRPGTYCEPKMTT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 400 VGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRLLLPD 479
Cdd:PRK09238 400 VGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 480 TLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVPKQNK 559
Cdd:PRK09238 480 TVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQGLLTVEKKGK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 560 KNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIEDAEK 639
Cdd:PRK09238 560 KNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDARTLERRIAAMEE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 640 WLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWEGAAYP 719
Cdd:PRK09238 640 WLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEGKKGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 720 -KTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAEL 798
Cdd:PRK09238 720 lPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLGSAEL 799
|
810 820 830
....*....|....*....|....*....|....*..
gi 1561167075 799 TAVTALMGELPTPAEYFMLYKSKIEPKqAEVYRYLEF 835
Cdd:PRK09238 800 AAVCALLGRIPTVEEYQEYVAEIDATA-DDIYRYLNF 835
|
|
| acnB |
TIGR00117 |
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This ... |
1-843 |
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: 1282.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 1 MMQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPV 80
Cdd:TIGR00117 1 MLEEYRKHVAERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKCPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 81 ITKKDAVFFLGTMLGGYNVKPLVDLL--TDAELGADAAEALKQTILIYGSFEDVLALSKSNANAKAVIQSWADAEWFTSK 158
Cdd:TIGR00117 81 ISPEKAIELLGTMQGGYNVHPLIDALdsQDANIAPIAAKALSHTLLVFDNFYDVEEKSKTNEYAKQVMQSWADAEWFLNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 159 PEFPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSA 238
Cdd:TIGR00117 161 PALAEKITVTVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREGIEPQIEALKQKGFPVAYVGDVVGTGSSRKSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 239 CNSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKL 318
Cdd:TIGR00117 241 TNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDSGALPIEVDVSNLNMGDVIDIYPYKGEITNHEGELLATFEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 319 SPATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVpKKGQGFTLAQKIIGKACGVEGVLPGTACEPVMT 398
Cdd:TIGR00117 321 KPETLLDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQPKAPA-ESDKGFTLAQKMVGRACGVKGIRPGTYCEPKMT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 399 TVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRLLLP 478
Cdd:TIGR00117 400 TVGSQDTTGPMTRDELKELACLGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGVIHSWLNRMLLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 479 DTLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVPKQN 558
Cdd:TIGR00117 480 DTVGTGGDSHTRFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAIKQGLLTVEKKG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 559 KKNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIEDAE 638
Cdd:TIGR00117 560 KKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGME 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 639 KWLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWEGAAY 718
Cdd:TIGR00117 640 KWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSCMTNIGHFRAAGKILDAAGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 719 PKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAEL 798
Cdd:TIGR00117 720 LPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVADGATVFSTSTRNFPNRMGTGANVYLGSAEL 799
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1561167075 799 TAVTALMGELPTPAEYFMLYKSKIEPKQAEVYRYLEFDKMGDFEL 843
Cdd:TIGR00117 800 AAVCALLGKIPTPEEYQTYVSEKDKTAVDKTYRYLNFNQLSNFTE 844
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
373-808 |
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: 773.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 373 LAQKIIGKACGVEGVLPGTACEPVMTTVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDF 452
Cdd:cd01581 1 LAQKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTLPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 453 VTLRKGVALRPGDGVIHSWLNRLLLPDTLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPG 532
Cdd:cd01581 81 ISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 533 ITLRDAVNAIPYWAIKQGLLTVPKQNKKNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSN 612
Cdd:cd01581 161 ITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYLESN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 613 IALMKKMIAAGYRHADTLKKRIEDAEKWLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKID 692
Cdd:cd01581 241 VVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGKKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 693 EIFIGSCMTNIGHFRAAGKIWEGAAYPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAH 772
Cdd:cd01581 321 EVFIGSCMTNIGHFRAAAKILRGKEFKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVADGAT 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1561167075 773 VLSTSTRNFPNRIGDESQVYLGSAELTAVTALMGEL 808
Cdd:cd01581 401 VFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| Aconitase_2_N |
pfam06434 |
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several ... |
167-371 |
5.38e-118 |
|
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: 356.13 E-value: 5.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 167 LKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSACNSVMWKI 246
Cdd:pfam06434 1 VTVFKVEGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPLKTIAELKKKGHPLAYVGDVVGTGSSRKSATNSVLWHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 247 GQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKLSPATIKDE 326
Cdd:pfam06434 81 GEDIPYVPNKRTGGVVIGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVITIYPYEGKITNENGEVISTFSLKPNTLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1561167075 327 YRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVPkKGQGF 371
Cdd:pfam06434 161 VRAGGRIPLIIGRGLTDKAREALGLEPSDVFTRPKQPAD-SGKGY 204
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
372-806 |
7.66e-34 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 134.88 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 372 TLAQKIIGKACGVEgVLPGTACEPVMTTVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHT--AAYPKKADvaMHKSL 449
Cdd:NF040615 2 TLAEKILSKKLGKE-VYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNvpANTVKAAN--MQKIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 450 PDFVTlRKGVA--LRPGDGVIHSWL--NRLLLPDTLGTGGDSHT-------RFPIGLslpaGSGLVAFAGALGFMPLDVP 518
Cdd:NF040615 79 REFVK-EQGIKnfYLGGEGICHQVLpeKGHVLPNMVIAGGDSHTcthgafgAFATGF----GATDMGYIYATGKTWIKVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 519 ESVLVKFKGKfNPGITLRDAVnaipywaikqglLTVPKQNKKNIFNGRILEMEG--LPDLTVEQAFELTDATAERSAAGG 596
Cdd:NF040615 154 KTIRVNIVGK-NENISGKDII------------LKVCKEIGRRGATYMAIEYGGevVKNMDMDGRMVLCNMAIEMGGKTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 597 TIKLSEKSVSgFLRsNIALMKKMIAagyrhadTLKKriedaekwlaNPVLLERDEnAEYAAVIEIDLAEITEPIlACPND 676
Cdd:NF040615 221 IIEADEITYE-YLR-KEGVSEEEIA-------ELKK----------NRITVNEKE-ENYYKEIEIDITDMEEQV-ACPHH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 677 PDDVKLLSEVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEGAAYPK-TKIWLTPPTLMDQMQLMEEGYYSIYASVGARTE 753
Cdd:NF040615 280 PDNVKPVSEVEGTEIDQVFIGSC-TNgrLSDLRIAAKYLKGKKVHKdVRLIVIPASKKVFKQALKEGLIEIFVKAGAMIC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1561167075 754 IPGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMG 806
Cdd:NF040615 359 TPGCGPCLGaHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKG 413
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
1-850 |
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: 1701.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 1 MMQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPV 80
Cdd:COG1049 1 MLEAYRKHVAERAALGIPPLPLNAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEATSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 81 ITKKDAVFFLGTMLGGYNVKPLVDLLTDAELGADAAEALKQTILIYGSFEDVLALSK-SNANAKAVIQSWADAEWFTSKP 159
Cdd:COG1049 81 ISPEKAVELLGTMLGGYNVQPLIELLDDAELAPEAAEALSHTLLVFDAFHDVEEKAKaGNAYAKQVLQSWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 160 EFPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSAC 239
Cdd:COG1049 161 ELPEKITVTVFKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPLKTIAELKAKGHPVAYVGDVVGTGSSRKSAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 240 NSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKLS 319
Cdd:COG1049 241 NSVLWHMGEDIPFVPNKRTGGVVLGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVIDIYPYEGKITKENGEVISTFELK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 320 PATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVpKKGQGFTLAQKIIGKACGVEGVLPGTACEPVMTT 399
Cdd:COG1049 321 PDTLLDEVRAGGRIPLIIGRGLTDKAREALGLPPSDVFRRPEAPA-DSGKGYTLAQKMVGKACGVEGVRPGTYCEPKMTT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 400 VGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRLLLPD 479
Cdd:COG1049 400 VGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFISSRGGVSLRPGDGIIHSWLNRMLLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 480 TLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVPKQNK 559
Cdd:COG1049 480 TVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPYYAIKQGLLTVEKKGK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 560 KNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIEDAEK 639
Cdd:COG1049 560 KNIFSGRILEIEGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPVIEYLRSNIALLKWMIAEGYGDARTLERRIAAMEE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 640 WLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWEGAAYP 719
Cdd:COG1049 640 WLANPELLEADADAEYAAVIEIDLNEIKEPILACPNDPDDVKLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEGKGNL 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 720 KTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAELT 799
Cdd:COG1049 720 PTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELA 799
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 800 AVTALMGELPTPAEYFMLYKsKIEPKQAEVYRYLEFDKMGDFELSYIERVA 850
Cdd:COG1049 800 AVCALLGRLPTVEEYMEYVK-KIDPMADDIYRYLNFDQIEEYQEKADVVIP 849
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
1-835 |
0e+00 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 1571.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 1 MMQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPV 80
Cdd:PRK09238 1 MLEAYRKHVAERAALGIPPLPLDAEQTAELVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 81 ITKKDAVFFLGTMLGGYNVKPLVDLLTDAELGADAAEALKQTILIYGSFEDVLALSKS-NANAKAVIQSWADAEWFTSKP 159
Cdd:PRK09238 81 ISPEKAVELLGTMLGGYNVEPLIDLLDDAELAPEAAEALKHTLLVFDAFHDVAEKAKAgNAYAKEVLESWADAEWFTSRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 160 EFPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSAC 239
Cdd:PRK09238 161 ELPEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPIKQIEELKKKGHPVAYVGDVVGTGSSRKSAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 240 NSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKLS 319
Cdd:PRK09238 241 NSVLWHMGEDIPYVPNKRAGGVVLGGKIAPIFFNTMEDSGALPIELDVSKLNMGDVIDIYPYKGKIRNETGEVIATFKLK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 320 PATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVPKkGQGFTLAQKIIGKACGVEGVLPGTACEPVMTT 399
Cdd:PRK09238 321 TDVLLDEVRAGGRIPLIIGRGLTTKAREALGLPPSDVFRKPKQPADS-GKGFTLAQKMVGRACGVPGVRPGTYCEPKMTT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 400 VGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRLLLPD 479
Cdd:PRK09238 400 VGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 480 TLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVPKQNK 559
Cdd:PRK09238 480 TVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVHAIPYYAIKQGLLTVEKKGK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 560 KNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIEDAEK 639
Cdd:PRK09238 560 KNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYLRSNIVLLKWMIAEGYGDARTLERRIAAMEE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 640 WLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWEGAAYP 719
Cdd:PRK09238 640 WLANPELLEADADAEYAAVIEIDLAEIKEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNIGHFRAAGKLLEGKKGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 720 -KTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAEL 798
Cdd:PRK09238 720 lPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARVADGATVFSTSTRNFPNRLGKGANVYLGSAEL 799
|
810 820 830
....*....|....*....|....*....|....*..
gi 1561167075 799 TAVTALMGELPTPAEYFMLYKSKIEPKqAEVYRYLEF 835
Cdd:PRK09238 800 AAVCALLGRIPTVEEYQEYVAEIDATA-DDIYRYLNF 835
|
|
| acnB |
TIGR00117 |
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This ... |
1-843 |
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: 1282.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 1 MMQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPV 80
Cdd:TIGR00117 1 MLEEYRKHVAERAAEGIPPLPLNANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKCPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 81 ITKKDAVFFLGTMLGGYNVKPLVDLL--TDAELGADAAEALKQTILIYGSFEDVLALSKSNANAKAVIQSWADAEWFTSK 158
Cdd:TIGR00117 81 ISPEKAIELLGTMQGGYNVHPLIDALdsQDANIAPIAAKALSHTLLVFDNFYDVEEKSKTNEYAKQVMQSWADAEWFLNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 159 PEFPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSA 238
Cdd:TIGR00117 161 PALAEKITVTVFKVTGETNTDDLSPAPDAWTRPDIPLHALAMLKNAREGIEPQIEALKQKGFPVAYVGDVVGTGSSRKSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 239 CNSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKL 318
Cdd:TIGR00117 241 TNSVLWHMGDDIPFVPNKRGGGLCLGGKIAPIFFNTMEDSGALPIEVDVSNLNMGDVIDIYPYKGEITNHEGELLATFEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 319 SPATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVpKKGQGFTLAQKIIGKACGVEGVLPGTACEPVMT 398
Cdd:TIGR00117 321 KPETLLDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQPKAPA-ESDKGFTLAQKMVGRACGVKGIRPGTYCEPKMT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 399 TVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRLLLP 478
Cdd:TIGR00117 400 TVGSQDTTGPMTRDELKELACLGFSADLVLQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVALRPGDGVIHSWLNRMLLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 479 DTLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVPKQN 558
Cdd:TIGR00117 480 DTVGTGGDSHTRFPLGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVNAIPLYAIKQGLLTVEKKG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 559 KKNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIEDAE 638
Cdd:TIGR00117 560 KKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGME 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 639 KWLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWEGAAY 718
Cdd:TIGR00117 640 KWLANPELLEADADAEYAAVIEIDLAEIKEPILAAPNDPDDVRPLSEVQGDKIDEVFIGSCMTNIGHFRAAGKILDAAGQ 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 719 PKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAEL 798
Cdd:TIGR00117 720 LPTRLWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMGNQARVADGATVFSTSTRNFPNRMGTGANVYLGSAEL 799
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1561167075 799 TAVTALMGELPTPAEYFMLYKSKIEPKQAEVYRYLEFDKMGDFEL 843
Cdd:TIGR00117 800 AAVCALLGKIPTPEEYQTYVSEKDKTAVDKTYRYLNFNQLSNFTE 844
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
2-841 |
0e+00 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 1185.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 2 MQDYLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPVI 81
Cdd:PLN00094 71 LAEYEAHVAERAQEGIAPKPLDAKQVSELIAQLEAPKSEDADRLVDLLVNRVPPGVDEAAYVKASWLAAVAKGETRSPLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 82 TKKDAVFFLGTMLGGYNVKPLVDLLTDAELGADAAEALKQTILIYGSFEDVLALSKS-NANAKAVIQSWADAEWFTSKPE 160
Cdd:PLN00094 151 SRARAVEILGTMQGGYNISPLVDALDDDELGRIAADQLSHTLLVFDAFHDVQAKAKKgNAYATQVMESWADAEWFTKKPP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 161 FPKSFKLKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGN---TTIDKFREEGFEAGFVGDVVGTGSSRKS 237
Cdd:PLN00094 231 VPEKITVTVFKVTGETNTDDLSPAQDAWSRPDIPLHALAMLKNPREGIQgpiAQIEELKKKGHPLAYVGDVVGTGSSRKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 238 ACNSVMWKIGQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEA-GKVISTF 316
Cdd:PLN00094 311 ATNSVLWFMGDDIPNVPNKRTGGVCIGGKIAPIFFNTMEDSGALPIEMDVKNLNMGDVIDIYPYEGVVKRHGtDEVITTF 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 317 KLSPATIKDEYRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPvPKKGQGFTLAQKIIGKACGV-EGVLPGTACEP 395
Cdd:PLN00094 391 SLKTPVLLDEVRAGGRIPLIIGRGLTSKAREALGLDASDVFRMPSVP-ESKPKGFTLAQKMVGKACGVdEGILPGTYCEP 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 396 VMTTVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDFVTLRKGVALRPGDGVIHSWLNRL 475
Cdd:PLN00094 470 RMTTVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVVTHHTLPDFIRNRGGVSLRPGDGVIHSWLNRM 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 476 LLPDTLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGLLTVP 555
Cdd:PLN00094 550 LLPDTVGTGGDSHTRFPIGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIPYTAIQDGLLTVE 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 556 KQNKKNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKKMIAAGYRHADTLKKRIE 635
Cdd:PLN00094 630 KKGKKNVFSGRILEIEGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIEYLNSNVVMLKWMIAEGYGDRRTLERRIA 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 636 DAEKWLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNIGHFRAAGKIWE- 714
Cdd:PLN00094 710 RMQQWLADPELLEADPDAEYAAVIEIDMDEIKEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCMTNIGHFRAAGKLLNd 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 715 -GAAYPkTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYL 793
Cdd:PLN00094 790 nLSQLP-TRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARVAEKSTVVSTSTRNFPNRLGKGANVYL 868
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1561167075 794 GSAELTAVTALMGELPTPAEYfMLYKSKIEPKQAEVYRYLEFDKMGDF 841
Cdd:PLN00094 869 ASAELAAVAAILGRLPTVEEY-LSYMEKLDATASDTYRYLNFDELPEY 915
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
373-808 |
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: 773.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 373 LAQKIIGKACGVEGVLPGTACEPVMTTVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAMHKSLPDF 452
Cdd:cd01581 1 LAQKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTLPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 453 VTLRKGVALRPGDGVIHSWLNRLLLPDTLGTGGDSHTRFPIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPG 532
Cdd:cd01581 81 ISNRGGVALRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 533 ITLRDAVNAIPYWAIKQGLLTVPKQNKKNIFNGRILEMEGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSN 612
Cdd:cd01581 161 ITLRDLVNAIPYYAIQQGLLTVEKKGKKNVFNGRILEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYLESN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 613 IALMKKMIAAGYRHADTLKKRIEDAEKWLANPVLLERDENAEYAAVIEIDLAEITEPILACPNDPDDVKLLSEVAGNKID 692
Cdd:cd01581 241 VVLMKIMIANGYDDARTLLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKEPILACPNDPDDVKLLSEVAGKKID 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 693 EIFIGSCMTNIGHFRAAGKIWEGAAYPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAH 772
Cdd:cd01581 321 EVFIGSCMTNIGHFRAAAKILRGKEFKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVADGAT 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1561167075 773 VLSTSTRNFPNRIGDESQVYLGSAELTAVTALMGEL 808
Cdd:cd01581 401 VFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| Aconitase_2_N |
pfam06434 |
Aconitate hydratase 2 N-terminus; This family represents the N-terminal region of several ... |
167-371 |
5.38e-118 |
|
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: 356.13 E-value: 5.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 167 LKIFKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSACNSVMWKI 246
Cdd:pfam06434 1 VTVFKVEGETNTDDLSPAPDAWSRPDIPLHALAMLKNRRPGPLKTIAELKKKGHPLAYVGDVVGTGSSRKSATNSVLWHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 247 GQDIPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDTEKCEVRDEAGKVISTFKLSPATIKDE 326
Cdd:pfam06434 81 GEDIPYVPNKRTGGVVIGGKIAPIFFNTAEDSGALPIECDVSKLNTGDVITIYPYEGKITNENGEVISTFSLKPNTLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1561167075 327 YRAGGRLNLIIGRQLTVKARKALGLPESTVFTATVNPVPkKGQGF 371
Cdd:pfam06434 161 VRAGGRIPLIIGRGLTDKAREALGLEPSDVFTRPKQPAD-SGKGY 204
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
400-808 |
3.79e-102 |
|
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: 321.75 E-value: 3.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 400 VGSQDTTGPMTRDEITELACLEFQASMFMQSFCHTAAYPKKADVAM--HKSLPDFVTLRKGVALRPGDGVIHSWLNR-LL 476
Cdd:cd01351 2 VMLQDATGPMAMKAFEILAALGKVADPSQIACVHDHAVQLEKPVNNegHKFLSFFAALQGIAFYRPGVGIIHQIMVEnLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 477 LPDTLGTGGDSHTRF---PIGLSLPAGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIPYWAIKQGllt 553
Cdd:cd01351 82 LPGDLLVGSDSHTTSyggLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 554 vpkqnkkniFNGRILEMEGLP--DLTVEQAFELTDATAERSAAGGTIKLSEKSVSGFLRSNIALMKkmiaagyrhadtlk 631
Cdd:cd01351 159 ---------VLNRIVEFYGEGvsSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLK-------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 632 kriedaEKWLANPVLLERDENAEYAAVIEIDLAEItEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCMTNI-GHFRAAG 710
Cdd:cd01351 216 ------NLWLAFPEELLADEGAEYDQVIEIDLSEL-EPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRySDMLAAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 711 KIWEGA-AYPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQP-KAHVLSTSTRNFPNRIGD- 787
Cdd:cd01351 289 KLLKGAkVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVAdGEVGVSSGNRNFPGRLGTy 368
|
410 420
....*....|....*....|.
gi 1561167075 788 ESQVYLGSAELTAVTALMGEL 808
Cdd:cd01351 369 ERHVYLASPELAAATAIAGKI 389
|
|
| Aconitase_B_N |
pfam11791 |
Aconitate B N-terminal domain; This family represents the N-terminal domain of Aconitase B. |
5-155 |
4.04e-85 |
|
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: 267.78 E-value: 4.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 5 YLKHVEERKAQGIPPLPLSPEFTAEVCKMLENPAKEQADFLKELIVNRVSPGVDPAAEVKAAWLERVAKGAVKCPVITKK 84
Cdd:pfam11791 1 YRKHVAERAALGIPPLPLDAEQTAELIELLKNPPAGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAIAKGEASSPLISPE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 85 DAVFFLGTMLGGYNVKPLVDLLTDAELGADAAEALKQTILIYGSFEDVLALSKSNANAKAVIQSWADAEWF 155
Cdd:pfam11791 81 EAVELLGTMLGGYNVAPLIDLLDDAELAAEAAEALKKTLLVYDAFHDVAELAKANAYAKEVLESWANAEWF 151
|
|
| AcnB_Swivel |
cd01576 |
Aconitase B swivel domain. Aconitate hydratase B is involved in energy metabolism as part of ... |
170-300 |
4.54e-65 |
|
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: 213.49 E-value: 4.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 170 FKADGETNTDDFSPAKHAWSRPDIPLHALAMGETSWPQGNTTIDKFREEGFEAGFVGDVVGTGSSRKSACNSVMWKIGQD 249
Cdd:cd01576 1 FKVPGETNTDDLSPAPDAWSRPDIPLHALAMLKNKREGEIVAIAQLKPKGHPVAYVGDVVGTGSSRKSATNSVLWHTGKD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 250 IPFVPNKRRGGVILGGVIAPIFFNTTEDSGGLPIICDVNNIKTGDVVIVDT 300
Cdd:cd01576 81 IPFVPNKRAGGVVLGGKIAPIFFNTAEDSGALPIQLDVSVLDMGDILNIDG 131
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
372-811 |
7.81e-51 |
|
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: 184.19 E-value: 7.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 372 TLAQKIIGKACGVEgVLPGTACEPVMTTVGSQDTTGPMTRDEITELACLE-FQASMFMQSFCHTAAYPKKADVAMHKSLP 450
Cdd:TIGR01343 1 TIAEKILSKKSGKE-VYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKvWNPEKIVIVFDHQVPADTIKAAEMQKLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 451 DFVTlRKGVAL--RPGDGVIHSWL--NRLLLPDTLGTGGDSHT-------RFPIGLslpaGSGLVAFAGALGFMPLDVPE 519
Cdd:TIGR01343 80 EFVK-KQGIKYfyDVGEGICHQVLpeKGLVKPGDLVVGADSHTctygafgAFATGM----GSTDMAYAIATGKTWFKVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 520 SVLVKFKGKFNPGITLRDAVnaipywaikqglLTVPKQNKKNIFNGRILEMEG--LPDLTVEQAFELTDATAERSAAGGT 597
Cdd:TIGR01343 155 TIRVNITGKLNPGVTAKDVI------------LEVIGEIGVDGATYMAMEFGGetVKNMDMEGRLTLANMAIEAGGKTGI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 598 IKLSEKSvsgflrsnIALMKKMIAAGYRhadtlkkriedaekwlanpvLLERDENAEYAAVIEIDLAEItEPILACPNDP 677
Cdd:TIGR01343 223 IEPDEKT--------IQYLKERRKEPFR--------------------VYKSDEDAEYAKEIEIDASQI-EPVVACPHNV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 678 DDVKLLSEVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEG-AAYPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEI 754
Cdd:TIGR01343 274 DNVKPVSEVEGTEIDQVFIGSC-TNgrLEDLRVAAKILKGrKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVST 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1561167075 755 PGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMGELPTP 811
Cdd:TIGR01343 353 PGCGPCLGsHQGVLAPGEVCISTSNRNFKGRMGHpNAEIYLASPATAAASAVKGYIADP 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
370-814 |
4.12e-49 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 179.22 E-value: 4.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 370 GFTLAQKIIGKACGVEgVLPGTACEPVMTTVGSQDTTGPmtrdeiteLACLEFQASMFMQSFchtaaYPKKADVAM---- 445
Cdd:PRK00402 2 GMTLAEKILARHSGRD-VSPGDIVEAKVDLVMAHDITGP--------LAIKEFEKIGGDKVF-----DPSKIVIVFdhfv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 446 ----------HKSLPDFVtlrKGVALRP----GDGVIHSWL--NRLLLPDTLGTGGDSHT-------RFPIGLslpaGSG 502
Cdd:PRK00402 68 pakdiksaeqQKILREFA---KEQGIPNffdvGEGICHQVLpeKGLVRPGDVVVGADSHTctygalgAFATGM----GST 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 503 LVAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAVNAIpywaIkqGLLTVpkqnkkNIFNGRILEM--EGLPDLTVEQ 580
Cdd:PRK00402 141 DMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHI----I--GDIGV------DGATYKALEFtgETIEALSMDE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 581 AFELTDATAErsaAGGTiklseksvSGflrsnialmkkMIAAGYRHADTLKKRIEDAEKWLANpvllerDENAEYAAVIE 660
Cdd:PRK00402 209 RMTLANMAIE---AGAK--------AG-----------IFAPDEKTLEYLKERAGRDYKPWKS------DEDAEYEEVYE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 661 IDLAEItEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEG-AAYPKTKIWLTPPTLMDQMQLM 737
Cdd:PRK00402 261 IDLSKL-EPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSC-TNgrLEDLRIAAEILKGrKVAPGVRLIVIPASQKIYLQAL 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561167075 738 EEGYYSIYASVGARTEIPGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMGELPTPAEY 814
Cdd:PRK00402 339 KEGLIEIFVDAGAVVSTPTCGPCLGgHMGVLAPGEVCLSTTNRNFKGRMGSpESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
370-814 |
1.22e-48 |
|
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: 177.92 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 370 GFTLAQKIIGKACGVEgVLPGtacEPVMTTVG---SQDTTGPMTRDEITELACLE-FQASMFMQSFCHTAAYPKKADVAM 445
Cdd:COG0065 2 GMTLAEKILARHAGRE-VEPG---EIVLLYIDlhlVHDVTSPQAFEGLREAGGRKvWDPDRIVAVFDHNVPTKDPKSAEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 446 HKSLPDFVTlRKGVAL-RPGD-GVIHSWL--NRLLLPDTLGTGGDSHT---------RFPIGLSLpagsglVAFAGALGF 512
Cdd:COG0065 78 VKTLREFAK-EFGITFfDVGDpGICHVVLpeQGLVLPGMTIVGGDSHTcthgafgafAFGIGTTD------VAHVLATGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 513 MPLDVPESVLVKFKGKFNPGITLRDAVNAIpywaIkqGLLTVpkqnkkNIFNGRILEM--EGLPDLTVEQAFELTDATAE 590
Cdd:COG0065 151 LWFKVPETMRIEVTGKLPPGVTAKDLILAI----I--GKIGA------DGATGKAIEFagEAIRALSMEERMTLCNMAIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 591 rsaAGGTiklseksvSGflrsnialmkkMIAAGYRHADTLKKRIEDAEKWLANpvllerDENAEYAAVIEIDLAEItEPI 670
Cdd:COG0065 219 ---AGAK--------AG-----------IIAPDETTFEYLKGRPFAPWRTLKS------DEDAVYDKEVEIDASDL-EPQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 671 LACPNDPDDVKLLSEVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEG---AayPKTKIWLTPPTLMDQMQLMEEGYYSIY 745
Cdd:COG0065 270 VAWPHSPDNVVPVSELEGIKIDQVFIGSC-TNgrIEDLRAAAEILKGrkvA--PGVRAIVVPGSQEVYRQAEAEGLDEIF 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 746 ASVGARTEIPGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMGELPTPAEY 814
Cdd:COG0065 347 IEAGAEWREPGCGMCLGmNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
464-808 |
2.77e-48 |
|
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: 175.84 E-value: 2.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 464 GDGVIHSWL--NRLLLPDTLGTGGDSHT-------RFPIGLslpaGSGLVAFAGALGFMPLDVPESVLVKFKGKFNPGIT 534
Cdd:cd01583 68 RQGICHVILpeKGLTLPGMTIVGGDSHTcthgafgAFATGI----GTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 535 LRDAVNAIpywaIkqGLLTVpkqnkkNIFNGRILEM--EGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSvsgflrsn 612
Cdd:cd01583 144 AKDVILYI----I--GKIGV------DGATYKAMEFagEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETT-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 613 IALMKKMIAAGYRHadtlkkriedaekwlanpvlLERDENAEYAAVIEIDLAEItEPILACPNDPDDVKLLSEVAGNKID 692
Cdd:cd01583 204 FEYLKGRGKAYWKE--------------------LKSDEDAEYDKVVEIDASEL-EPQVAWPHSPDNVVPVSEVEGIKID 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 693 EIFIGSCmTN--IGHFRAAGKIWEGAAY-PKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMG-NQGRVQ 768
Cdd:cd01583 263 QVFIGSC-TNgrLEDLRAAAEILKGRKVaDGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLA 341
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1561167075 769 PKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMGEL 808
Cdd:cd01583 342 PGERCVSTSNRNFKGRMGSpGARIYLASPATAAASAITGEI 382
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
372-811 |
6.74e-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: 175.72 E-value: 6.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 372 TLAQKIIGKACGVEgVLPGTACEPVMTTVGSQDTTGPMTRDEITELACLEF----QASMFmqsFCHTAAYPKKADVAMHK 447
Cdd:TIGR02086 2 TLAEKILSEKVGRP-VCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVwdpeKIVIA---FDHNVPPPTVEAAEMQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 448 SLPDFVTLRKGVALRPGDGVIHSWL--NRLLLPDTLGTGGDSHT-------RFPIGLslpaGSGLVAFAGALGFMPLDVP 518
Cdd:TIGR02086 78 EIREFAKRHGIKNFDVGEGICHQILaeEGYALPGMVVVGGDSHTctsgafgAFATGM----GATDMAIALATGKTWIKVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 519 ESVLVKFKGKFNPGITLRDAVnaipywaikqglLTVPKQNKKNIFNGRILEMEGLP--DLTVEQAFELTDATAERSAAGG 596
Cdd:TIGR02086 154 ETIRVVVEGKPEEGVTAKDVA------------LHIVGELGADGATYMAIEFFGLPieNMDMDGRLTLCNMAVEMGAKAG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 597 TIKLSEKSVsgflrsnialmkkmiaagyrhaDTLKKRIEDAEKWLANpvllerDENAEYAAVIEIDLAEItEPILACPND 676
Cdd:TIGR02086 222 IIEPDEETY----------------------EYLKKRRGLEFRILVP------DPGANYYKEIEIDLSDL-EPQVAVPHS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 677 PDDVKLLSEVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEG-AAYPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTE 753
Cdd:TIGR02086 273 VDNVKPVSDVEGTEIDQVFIGSC-TNgrLEDLRIAAEILKGrRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMIC 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 754 IPGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMGELPTP 811
Cdd:TIGR02086 352 PPGCGPCLGaHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDP 411
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
463-806 |
7.50e-34 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 136.01 E-value: 7.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 463 PGDGVIHSWL--NRLLLPDTLGTGGDSHTRFpIGlslpagsglvAFaGALGF-------------MPLD--VPESVLVKF 525
Cdd:pfam00330 103 PGQGIVHQVGleYGLALPGMTIVGTDSHTTT-HG----------GL-GALAFgvggseaehvlatQPLEmkKPKVVGVKL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 526 KGKFNPGITLRDAVNAIpywaikQGLLTvpkqnkKNIFNGRILEM--EGLPDLTVEQAFELTDATAERSAAGGTIKLSEK 603
Cdd:pfam00330 171 TGKLPPGVTAKDVILAI------IGKLG------VKGGTGKVVEFfgPGVRSLSMEGRATICNMAIEYGATAGLFPPDET 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 604 SVSgFLRsnialmkkmiAAGyRHADTLKKRIEDAEKWLAnpvlLERDENAEYAAVIEIDLAEItEPILACPNDPDDVKLL 683
Cdd:pfam00330 239 TFE-YLR----------ATG-RPEAPKGEAYDKAVAWKT----LASDPGAEYDKVVEIDLSTI-EPMVTGPTRPQDAVPL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 684 SEVA-----------------------------GNKIDEIFIGSCmTN--IGHFRAAGKIWEGAAY------PKTKIWLT 726
Cdd:pfam00330 302 SELVpdpfadavkrkaaeraleymglgpgtplsDGKVDIAFIGSC-TNssIEDLRAAAGLLKKAVEkglkvaPGVKASVV 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 727 PPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGNQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAELTAVTALMG 806
Cdd:pfam00330 381 PGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
372-806 |
7.66e-34 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 134.88 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 372 TLAQKIIGKACGVEgVLPGTACEPVMTTVGSQDTTGPMTRDEITELACLEFQASMFMQSFCHT--AAYPKKADvaMHKSL 449
Cdd:NF040615 2 TLAEKILSKKLGKE-VYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNvpANTVKAAN--MQKIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 450 PDFVTlRKGVA--LRPGDGVIHSWL--NRLLLPDTLGTGGDSHT-------RFPIGLslpaGSGLVAFAGALGFMPLDVP 518
Cdd:NF040615 79 REFVK-EQGIKnfYLGGEGICHQVLpeKGHVLPNMVIAGGDSHTcthgafgAFATGF----GATDMGYIYATGKTWIKVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 519 ESVLVKFKGKfNPGITLRDAVnaipywaikqglLTVPKQNKKNIFNGRILEMEG--LPDLTVEQAFELTDATAERSAAGG 596
Cdd:NF040615 154 KTIRVNIVGK-NENISGKDII------------LKVCKEIGRRGATYMAIEYGGevVKNMDMDGRMVLCNMAIEMGGKTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 597 TIKLSEKSVSgFLRsNIALMKKMIAagyrhadTLKKriedaekwlaNPVLLERDEnAEYAAVIEIDLAEITEPIlACPND 676
Cdd:NF040615 221 IIEADEITYE-YLR-KEGVSEEEIA-------ELKK----------NRITVNEKE-ENYYKEIEIDITDMEEQV-ACPHH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 677 PDDVKLLSEVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEGAAYPK-TKIWLTPPTLMDQMQLMEEGYYSIYASVGARTE 753
Cdd:NF040615 280 PDNVKPVSEVEGTEIDQVFIGSC-TNgrLSDLRIAAKYLKGKKVHKdVRLIVIPASKKVFKQALKEGLIEIFVKAGAMIC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1561167075 754 IPGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGD-ESQVYLGSAELTAVTALMG 806
Cdd:NF040615 359 TPGCGPCLGaHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKG 413
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
402-808 |
4.02e-33 |
|
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: 132.19 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 402 SQDTTGPMtrdeitelACLEFQA-------SMFMQSFCHTAAY---PKKADvaMHKSLPDfVTLRKGVAL-RPGDGVIHS 470
Cdd:cd01585 5 TQDATGTM--------AYLQFEAmgvdrvrTELSVSYVDHNTLqtdFENAD--DHRFLQT-VAARYGIYFsRPGNGICHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 471 -WLNRLLLPDTLGTGGDSHTRFPIGLSLPA-GSG----LVAFAGALGFMPLdvPESVLVKFKGKFNPGITLRDAV-NAIP 543
Cdd:cd01585 74 vHLERFAVPGKTLLGSDSHTPTAGGLGMLAiGAGgldvALAMAGEPYYIPM--PKVVGVRLTGELPPWVTAKDVIlELLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 544 YWAIKQGLltvpkqnkknifnGRILEM--EGLPDLTVEQAFELTDATAERSAAGGtIKLSEKSVSGFLrsnialmkkmiA 621
Cdd:cd01585 152 RLTVKGGV-------------GKIFEYtgPGVATLSVPERATITNMGAELGATTS-IFPSDERTREFL-----------A 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 622 AGYRHADtlkkriedaekWlanpVLLERDENAEYAAVIEIDLAEItEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCmT 701
Cdd:cd01585 207 AQGREDD-----------W----VELAADADAEYDEEIEIDLSEL-EPLIARPHSPDNVVPVREVAGIKVDQVAIGSC-T 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 702 NIGH--FRAAGKIWEG-AAYPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMGnQGRVQPKAHV-LSTS 777
Cdd:cd01585 270 NSSYedLMTVAAILKGrRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIG-MGQAPPTGGVsVRTF 348
|
410 420 430
....*....|....*....|....*....|..
gi 1561167075 778 TRNFPNRIGDES-QVYLGSAELTAVTALMGEL 808
Cdd:cd01585 349 NRNFEGRSGTKDdLVYLASPEVAAAAALTGVI 380
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
370-830 |
2.69e-31 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 130.65 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 370 GFTLAQKIIgKACGVEGVL-PGT--ACEP--VMTtvgsQDTTGPMtrdeitelACLEFQAsmfMQ----------SFC-H 433
Cdd:PRK07229 2 GLTLTEKIL-YAHLVEGELePGEeiAIRIdqTLT----QDATGTM--------AYLQFEA---MGldrvktelsvQYVdH 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 434 --TAAYPKKADVamHKSLPDfVTLRKGVAL-RPGDGVIHS-WLNRLLLPDTLGTGGDSHTrfpiglslPAGSGL------ 503
Cdd:PRK07229 66 nlLQADFENADD--HRFLQS-VAAKYGIYFsKPGNGICHQvHLERFAFPGKTLLGSDSHT--------PTAGGLgmlaig 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 504 -----VAFAGALGFMPLDVPESVLVKFKGKFNPGITLRDAvnaIPYWAikqGLLTVpkqnKKNIfnGRILEM--EGLPDL 576
Cdd:PRK07229 135 aggldVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDV---ILELL---RRLTV----KGGV--GKIIEYfgPGVATL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 577 TVEQAFELTDATAErsaAGGTIKL--SEKSVSGFLRSNialmkkmiaagyrhadtlkKRIEDAEKWLAnpvllerDENAE 654
Cdd:PRK07229 203 SVPERATITNMGAE---LGATTSIfpSDERTREFLKAQ-------------------GREDDWVELLA-------DPDAE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 655 YAAVIEIDLAEItEPILACPNDPDDVKLLSEVAGNKIDEIFIGSCmTNIGH--FRAAGKIWEG-AAYPKTKIWLTPPTLM 731
Cdd:PRK07229 254 YDEVIEIDLSEL-EPLIAGPHSPDNVVPVSEVAGIKVDQVLIGSC-TNSSYedLMRAASILKGkKVHPKVSLVINPGSRQ 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 732 DQMQLMEEGYYSIYASVGARTEIPGCSLCMGNqGRVQPKAHV-LSTSTRNFPNRIGDES-QVYLGSAELTAVTALMGELP 809
Cdd:PRK07229 332 VLEMLARDGALADLIAAGARILENACGPCIGM-GQAPATGNVsLRTFNRNFPGRSGTKDaQVYLASPETAAASALTGVIT 410
|
490 500
....*....|....*....|.
gi 1561167075 810 TPAEYFMLYKSKIEPKQAEVY 830
Cdd:PRK07229 411 DPRTLALENGEYPKLEEPEGF 431
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
475-808 |
5.53e-13 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 72.25 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 475 LLLPDTLGTGGDSHTrfpiglslpagSGLVAFaGALGF---------------MPLDVPESVLVKFKGKFNPGITLRDAV 539
Cdd:PRK12466 119 LTLPGMVIVCGDSHT-----------TTYGAL-GALAFgigtsevehvlatqtLVYRKPKTMRVRVDGELPPGVTAKDLI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 540 NAIpywaIK----QGLLtvpkqnkknifnGRILEMEG--LPDLTVEQAFELTDATAERSAAGGTIKLSEKSVSgFLRsni 613
Cdd:PRK12466 187 LAL----IArigaDGAT------------GYAIEFAGeaIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFD-YLR--- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 614 almkkmiaaGYRHADTLKKRIEDAEKWLAnpvlLERDENAEYAAVIEIDLAEI-------TEPILACP---------NDP 677
Cdd:PRK12466 247 ---------GRPRAPKGALWDAALAYWRT----LRSDADAVFDREVEIDAADIapqvtwgTSPDQAVPitgrvpdpaAEA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 678 DDVKLLS--------------EVAGNKIDEIFIGSCmTN--IGHFRAAGKIWEG--AAyPKTKIWLTPPTLMDQMQLMEE 739
Cdd:PRK12466 314 DPARRAAmeraldymgltpgtPLAGIPIDRVFIGSC-TNgrIEDLRAAAAVLRGrkVA-PGVRAMVVPGSGAVRRQAEAE 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 740 GYYSIYASVGARTEIPGCSLCMG-NQGRVQPKAHVLSTSTRNFPNRIGDESQVYLGSAELTAVTALMGEL 808
Cdd:PRK12466 392 GLARIFIAAGFEWREPGCSMCLAmNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHI 461
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
650-814 |
1.75e-12 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 70.53 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 650 DENAEYAAVIEIDLAEI----------------TEPIlacPnDPDDVKLLSEVA------------------GNKIDEIF 695
Cdd:PRK05478 268 DEDAVFDKVVTLDAADIepqvtwgtnpgqvisiDGKV---P-DPEDFADPVKRAsaeralaymglkpgtpitDIKIDKVF 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 696 IGSCmTN--IGHFRAAGKIWEG---AayPKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTEIPGCSLCMG-NQGRVQP 769
Cdd:PRK05478 344 IGSC-TNsrIEDLRAAAAVVKGrkvA--PGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAmNPDKLPP 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1561167075 770 KAHVLSTSTRNFPNRIGDESQVYLGSAELTAVTALMGELPTPAEY 814
Cdd:PRK05478 421 GERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
462-808 |
3.10e-09 |
|
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: 60.15 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 462 RPGDGVIHSW-LNRLLLPDTLGTGGDSHTrfpiglslPAGSGL------VAFAGALGFMP-----LDVPESVLVKFKGKF 529
Cdd:cd01584 73 KPGSGIIHQIvLENYAFPGLLMIGTDSHT--------PNAGGLggiaigVGGADAVDVMAgipweLKCPKVIGVKLTGKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 530 NPGITLRDAVNAIpywaikQGLLTVPKQNkknifnGRILEM--EGLPDLTVEQAFELTDATAERSAAggtiklseKSVSG 607
Cdd:cd01584 145 SGWTSPKDVILKV------AGILTVKGGT------GAIVEYfgPGVDSLSCTGMGTICNMGAEIGAT--------TSVFP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 608 FlrsNIALMKKMIAAGYRHADTLKKRIEDAEkwlanpvlLERDENAEYAAVIEIDLAEItEPILACPNDPDDVKLLSEVA 687
Cdd:cd01584 205 Y---NERMKKYLKATGRAEIADLADEFKDDL--------LVADEGAEYDQLIEINLSEL-EPHINGPFTPDLATPVSKFK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 688 GN--------KIDEIFIGSCmTNIGH---FRAAGKIWEGAAY---PKTKIWLTPPTLMDQMQLMEEGYYSIYASVGARTE 753
Cdd:cd01584 273 EVaekngwplDLRVGLIGSC-TNSSYedmGRAASIAKQALAHglkCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVL 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561167075 754 IPGCSLCMGNQGRVQ----PKAHVLSTSTRNFPNRiGD---ESQVYLGSAELTAVTALMGEL 808
Cdd:cd01584 352 ANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGR-NDanpATHAFVASPEIVTAMAIAGTL 412
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
208-299 |
1.19e-06 |
|
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: 47.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 208 GNTTIDKFREEGFEAGFVGDVVGTGSSRKSACNSVMWKIGQdipfvpnkrrggVILGGVIAPIFFNTTEDSGGLPI---- 283
Cdd:cd00404 4 GNITTDHISPAGPGVVIGDENYGTGSSREHAALELRLLGGR------------AVIAKSFARIFFRNLVDQGLLPLefad 71
|
90
....*....|....*.
gi 1561167075 284 ICDVNNIKTGDVVIVD 299
Cdd:cd00404 72 PEDYLKLHTGDELDIY 87
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
463-806 |
1.23e-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: 51.54 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 463 PGDGVIHS----WLNR-----------LLLPDTLgTGGDSHTRFPIGLS-LPAG-SGLVAFAGALG---FMPLdvPESVL 522
Cdd:cd01586 91 PGTGIIHQvnleYLARvvftseedgdgVAYPDSV-VGTDSHTTMINGLGvLGWGvGGIEAEAVMLGqpiSMLL--PEVVG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 523 VKFKGKFNPGITLRDAVnaipywaikqglLTVPKQNKKNIFNGRILEM--EGLPDLTVEQafeltdataersaaggtikl 600
Cdd:cd01586 168 VKLTGKLRPGVTATDLV------------LTVTQMLRKVGVVGKFVEFfgPGVAKLSVAD-------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 601 seksvsgflRSNIALMKKMIAA--GYRHADTlkkriedaekwlanpvllerdenaeyaAVIEIDLAEItEPILACPNDPD 678
Cdd:cd01586 216 ---------RATIANMAPEYGAtcGFFPVDT---------------------------QVVELDLSTV-EPSVSGPKRPQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 679 D-VKLLSEVAGNKIDeifigSCmTNIGH---FRAAGKIWEGAAY------PKTKIWLTPPTLMDQMQLMEEGYYSIYASV 748
Cdd:cd01586 259 DrVPLHGSVVIAAIT-----SC-TNTSNpsvMLAAGLLAKKAVElglkvkPYVKTSLAPGSRVVTKYLEASGLLPYLEKL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 749 GARTEIPGCSLCMGNQGRVQPK------------AHVLStSTRNFPNRIGDESQ-VYLGSAELTAVTALMG 806
Cdd:cd01586 333 GFHVVGYGCTTCIGNSGPLPEEveeaikendlvvAAVLS-GNRNFEGRIHPLVRaNYLASPPLVVAYALAG 402
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
463-687 |
9.40e-05 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 46.27 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 463 PGDGVIHS----------WLNR----LLLPDTL-GTggDSHTRFPIGLSLPA---GsGLVAFAGALG---FMPLdvPESV 521
Cdd:PRK09277 176 PGTGICHQvnleylapvvWTREdgelVAYPDTLvGT--DSHTTMINGLGVLGwgvG-GIEAEAAMLGqpsSMLI--PEVV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 522 LVKFKGKFNPGITLRDAVnaipywaikqglLTVPKQ-NKKNIFnGRILEM--EGLPDLTVeqafeltdatAERSaaggTI 598
Cdd:PRK09277 251 GVKLTGKLPEGVTATDLV------------LTVTEMlRKKGVV-GKFVEFfgEGLASLSL----------ADRA----TI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 599 klseksvsgflrSNialMkkmiA------AGYRHAD--TLK---------KRIEDAEKWL-ANPVLLERDENAEYAAVIE 660
Cdd:PRK09277 304 ------------AN---M----ApeygatCGFFPIDeeTLDylrltgrdeEQVALVEAYAkAQGLWRDPLEEPVYTDVLE 364
|
250 260
....*....|....*....|....*..
gi 1561167075 661 IDLAEItEPILACPNDPDDVKLLSEVA 687
Cdd:PRK09277 365 LDLSTV-EPSLAGPKRPQDRIPLSDVK 390
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
463-720 |
2.51e-04 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 44.80 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 463 PGDGVIHS----WLNR-------LLLPDTLgTGGDSHTRFPIGLSLpAG---SGLVAFAGALGF-MPLDVPESVLVKFKG 527
Cdd:PLN00070 214 PGSGIVHQvnleYLGRvvfntdgILYPDSV-VGTDSHTTMIDGLGV-AGwgvGGIEAEAAMLGQpMSMVLPGVVGFKLSG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 528 KFNPGITLRDAVnaipywaikqglLTVPKQNKKNIFNGRILEM--EGLPDLTVEQAFELTDATAERSAAGG--------- 596
Cdd:PLN00070 292 KLRDGVTATDLV------------LTVTQMLRKHGVVGKFVEFygEGMSELSLADRATIANMSPEYGATMGffpvdhvtl 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 597 -TIKL---SEKSVS---GFLRSNialmkKMIAagyRHADTLKKRIedaekwlanpvllerdenaeYAAVIEIDLAEItEP 669
Cdd:PLN00070 360 qYLKLtgrSDETVAmieAYLRAN-----KMFV---DYNEPQQERV--------------------YSSYLELDLEDV-EP 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1561167075 670 ILACPNDPDDVKLLSEVagnKIDeifIGSCMTNIGHFRaagkiweGAAYPK 720
Cdd:PLN00070 411 CISGPKRPHDRVPLKEM---KAD---WHSCLDNKVGFK-------GFAVPK 448
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
478-806 |
1.14e-03 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 42.61 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 478 PDTL-GTggDSHTRFPIGLSLPA---GsGLVAFAGALGfMP--LDVPESVLVKFKGKFNPGITLRDAVnaipywaikqgl 551
Cdd:PRK12881 205 PDTLvGT--DSHTTMINGIGVLGwgvG-GIEAEAVMLG-QPvyMLIPDVVGVELTGKLREGVTATDLV------------ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 552 LTVPKQNKKNIFNGRILEM--EGLPDLTVEQAFELTDATAERSAAGGTIKLSEKSV-----SGFLRSNIALMKKmiaagY 624
Cdd:PRK12881 269 LTVTEMLRKEGVVGKFVEFfgEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLdylrlTGRTEAQIALVEA-----Y 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 625 RHADTLkkriedaekWlANPvllerDENAEYAAVIEIDLAEItEPILACPNDPDDVKLLSEVAgNKIDEIF--------- 695
Cdd:PRK12881 344 AKAQGL---------W-GDP-----KAEPRYTRTLELDLSTV-APSLAGPKRPQDRIALGNVK-SAFSDLFskpvaengf 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 696 ---------------------IGSCmTNIGHFR---AAGKIWEGA------AYPKTKIWLTP--PTLMDQMQ---LMEE- 739
Cdd:PRK12881 407 akkaqtsngvdlpdgavaiaaITSC-TNTSNPSvliAAGLLAKKAvergltVKPWVKTSLAPgsKVVTEYLEragLLPYl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 740 --------GYysiyasvgarteipGCSLCMGNQGRVQPK------------AHVLStSTRNFPNRI-GDESQVYLGSAEL 798
Cdd:PRK12881 486 eklgfgivGY--------------GCTTCIGNSGPLTPEieqaitkndlvaAAVLS-GNRNFEGRIhPNIKANFLASPPL 550
|
....*...
gi 1561167075 799 TAVTALMG 806
Cdd:PRK12881 551 VVAYALAG 558
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
218-334 |
7.54e-03 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 37.88 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 218 EGFEAGFV-----GDVV------GTGSSRKSACNSVmwkigqdipfvpnkRRGGVilGGVIAP----IFF----NTteds 278
Cdd:PRK00439 36 EDLDPEFAkkvkpGDIIvagknfGCGSSREHAPIAL--------------KAAGV--SAVIAKsfarIFYrnaiNI---- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561167075 279 gGLPII-CD--VNNIKTGDVVIVDTEKCEVRDE-AGKVIsTFKLSPATIKDEYRAGGRLN 334
Cdd:PRK00439 96 -GLPVLeCDeaVDKIEDGDEVEVDLETGVITNLtTGEEY-KFKPIPEFMLEILKAGGLIE 153
|
|
| |
