|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-419 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 828.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAK 80
Cdd:PRK00402 1 MGMTLAEKILARHSGR-DVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 81 MVRDFAKKHNIKWFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSM 160
Cdd:PRK00402 80 ILREFAKEQGIPNFFDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 161 KFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQR 240
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 241 AKKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVH 320
Cdd:PRK00402 240 AGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 321 PYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANP 400
Cdd:PRK00402 320 PGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLASP 399
|
410
....*....|....*....
gi 570724915 401 AVVAASAVLGRIAHPEEVV 419
Cdd:PRK00402 400 AVAAASAVTGKITDPREVL 418
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-418 |
0e+00 |
|
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: 767.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAK 80
Cdd:COG0065 1 MGMTLAEKILARHAGR-EVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 81 MVRDFAKKHNIKwFFQEGE-GIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHS 159
Cdd:COG0065 80 TLREFAKEFGIT-FFDVGDpGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 160 MKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQ 239
Cdd:COG0065 159 MRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 240 RAKKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKV 319
Cdd:COG0065 239 RPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 320 HPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLAN 399
Cdd:COG0065 319 APGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYLAS 398
|
410
....*....|....*....
gi 570724915 400 PAVVAASAVLGRIAHPEEV 418
Cdd:COG0065 399 PATAAASAIAGRITDPREL 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-416 |
0e+00 |
|
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: 718.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 4 TITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMVR 83
Cdd:TIGR01343 1 TIAEKILSKKSGK-EVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 84 DFAKKHNIKWFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFI 163
Cdd:TIGR01343 80 EFVKKQGIKYFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 164 FYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAKK 243
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 244 PWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYV 323
Cdd:TIGR01343 240 PFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 324 RCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVV 403
Cdd:TIGR01343 320 RLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEIYLASPATA 399
|
410
....*....|...
gi 570724915 404 AASAVLGRIAHPE 416
Cdd:TIGR01343 400 AASAVKGYIADPR 412
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-412 |
0e+00 |
|
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: 661.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 31 LAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMVRDFAKKHNIKWFFQEGEGIEHTILPEEG 110
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGINFFDVGRQGICHVILPEKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 111 LVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGA 190
Cdd:cd01583 81 LTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 191 LYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAKKPWKIYHSDPDAEYSEIYEWDAGKLEPL 270
Cdd:cd01583 161 TYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAYWKELKSDEDAEYDKVVEIDASELEPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 271 VAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEA 350
Cdd:cd01583 241 VAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570724915 351 GCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVVAASAVLGRI 412
Cdd:cd01583 321 GAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-416 |
4.48e-180 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 508.53 E-value: 4.48e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 3 MTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNiDKVFDPEKIALVLSHFVPAKDIKSAEQAKMV 82
Cdd:NF040615 1 MTLAEKILSKKLGK-EVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 83 RDFAKKHNIKWFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKF 162
Cdd:NF040615 79 REFVKEQGIKNFYLGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 163 IFYGKpSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAK 242
Cdd:NF040615 159 NIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 243 --------KPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKIL 314
Cdd:NF040615 238 seeeiaelKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 315 KGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSE 394
Cdd:NF040615 318 KGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNINSY 397
|
410 420
....*....|....*....|..
gi 570724915 395 AYLANPAVVAASAVLGRIAHPE 416
Cdd:NF040615 398 IYLSSPKIAAKSAVKGYITNEE 419
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-410 |
4.09e-140 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 408.35 E-value: 4.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 7 EKIIADHAGKKEvkPGDLVTVkIDLAMANDVTAPLAIKILEKYNiDKVFDPEKIALVLSHFVP------------AKDIK 74
Cdd:pfam00330 1 EKIWDAHLVEEL--DGSLLYI-PDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPtdlvidhapdalDKNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 75 SA-----EQAKMVRDFAKKHNIKwFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMAT 149
Cdd:pfam00330 77 DEisrnkEQYDFLEWNAKKFGIR-FVPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 150 GETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAP 229
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 230 DEKTLQYVSQ--RAKKP----------WKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSES----------- 286
Cdd:pfam00330 236 DETTFEYLRAtgRPEAPkgeaydkavaWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELvpdpfadavkr 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 287 ------------------THITIDQAFIGSCTNGRIEDLRIAAKILK-----GRKVHPYVRCIVIPASKKVYMQALKEGL 343
Cdd:pfam00330 316 kaaeraleymglgpgtplSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570724915 344 IDIFLEAGCVVSVSTCGPCLGGHmGILAEGERCISTSNRNFPGRMgHPKSEAYLANPAVVAASAVLG 410
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQ-GPGGRTHLASPALVAAAAIAG 460
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-419 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 828.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAK 80
Cdd:PRK00402 1 MGMTLAEKILARHSGR-DVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 81 MVRDFAKKHNIKWFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSM 160
Cdd:PRK00402 80 ILREFAKEQGIPNFFDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 161 KFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQR 240
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 241 AKKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVH 320
Cdd:PRK00402 240 AGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 321 PYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANP 400
Cdd:PRK00402 320 PGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLASP 399
|
410
....*....|....*....
gi 570724915 401 AVVAASAVLGRIAHPEEVV 419
Cdd:PRK00402 400 AVAAASAVTGKITDPREVL 418
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-418 |
0e+00 |
|
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: 767.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAK 80
Cdd:COG0065 1 MGMTLAEKILARHAGR-EVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 81 MVRDFAKKHNIKwFFQEGE-GIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHS 159
Cdd:COG0065 80 TLREFAKEFGIT-FFDVGDpGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 160 MKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQ 239
Cdd:COG0065 159 MRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 240 RAKKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKV 319
Cdd:COG0065 239 RPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 320 HPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLAN 399
Cdd:COG0065 319 APGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYLAS 398
|
410
....*....|....*....
gi 570724915 400 PAVVAASAVLGRIAHPEEV 418
Cdd:COG0065 399 PATAAASAIAGRITDPREL 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-416 |
0e+00 |
|
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: 718.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 4 TITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMVR 83
Cdd:TIGR01343 1 TIAEKILSKKSGK-EVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 84 DFAKKHNIKWFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFI 163
Cdd:TIGR01343 80 EFVKKQGIKYFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 164 FYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAKK 243
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 244 PWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYV 323
Cdd:TIGR01343 240 PFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 324 RCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVV 403
Cdd:TIGR01343 320 RLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEIYLASPATA 399
|
410
....*....|...
gi 570724915 404 AASAVLGRIAHPE 416
Cdd:TIGR01343 400 AASAVKGYIADPR 412
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
3-418 |
0e+00 |
|
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131138 Cd Length: 419 Bit Score: 661.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 3 MTITEKIIADHAGKKEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMV 82
Cdd:TIGR02083 1 MTMAEKILAQHAGLESVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 83 RDFAKKHNIKWFFQEGE-GIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMK 161
Cdd:TIGR02083 81 REFAREQGIEKFFEIGNmGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 162 FIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRA 241
Cdd:TIGR02083 161 FVLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 242 KKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSE--STHITIDQAFIGSCTNGRIEDLRIAAKILKGRKV 319
Cdd:TIGR02083 241 KREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEagKEEIKIDQVVIGSCTNGRLEDLRLAAEILKGKTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 320 HPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLAN 399
Cdd:TIGR02083 321 APDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSEVYLAS 400
|
410
....*....|....*....
gi 570724915 400 PAVVAASAVLGRIAHPEEV 418
Cdd:TIGR02083 401 PAVAAASAIKGYIASPEEV 419
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-412 |
0e+00 |
|
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: 661.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 31 LAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMVRDFAKKHNIKWFFQEGEGIEHTILPEEG 110
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGINFFDVGRQGICHVILPEKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 111 LVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGA 190
Cdd:cd01583 81 LTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 191 LYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAKKPWKIYHSDPDAEYSEIYEWDAGKLEPL 270
Cdd:cd01583 161 TYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAYWKELKSDEDAEYDKVVEIDASELEPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 271 VAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEA 350
Cdd:cd01583 241 VAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570724915 351 GCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVVAASAVLGRI 412
Cdd:cd01583 321 GAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-417 |
0e+00 |
|
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: 575.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 3 MTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMV 82
Cdd:TIGR02086 1 MTLAEKILSEKVGR-PVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTVEAAEMQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 83 RDFAKKHNIKwFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKF 162
Cdd:TIGR02086 80 REFAKRHGIK-NFDVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 163 IFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAK 242
Cdd:TIGR02086 159 VVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 243 KPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPY 322
Cdd:TIGR02086 239 LEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 323 VRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAV 402
Cdd:TIGR02086 319 VRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSPNAEIYLASPAT 398
|
410
....*....|....*
gi 570724915 403 VAASAVLGRIAHPEE 417
Cdd:TIGR02086 399 AAASAVEGYITDPED 413
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-416 |
4.48e-180 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 508.53 E-value: 4.48e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 3 MTITEKIIADHAGKkEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNiDKVFDPEKIALVLSHFVPAKDIKSAEQAKMV 82
Cdd:NF040615 1 MTLAEKILSKKLGK-EVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 83 RDFAKKHNIKWFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKF 162
Cdd:NF040615 79 REFVKEQGIKNFYLGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 163 IFYGKpSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAK 242
Cdd:NF040615 159 NIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 243 --------KPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKIL 314
Cdd:NF040615 238 seeeiaelKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 315 KGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSE 394
Cdd:NF040615 318 KGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNINSY 397
|
410 420
....*....|....*....|..
gi 570724915 395 AYLANPAVVAASAVLGRIAHPE 416
Cdd:NF040615 398 IYLSSPKIAAKSAVKGYITNEE 419
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-410 |
4.09e-140 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 408.35 E-value: 4.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 7 EKIIADHAGKKEvkPGDLVTVkIDLAMANDVTAPLAIKILEKYNiDKVFDPEKIALVLSHFVP------------AKDIK 74
Cdd:pfam00330 1 EKIWDAHLVEEL--DGSLLYI-PDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPtdlvidhapdalDKNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 75 SA-----EQAKMVRDFAKKHNIKwFFQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMAT 149
Cdd:pfam00330 77 DEisrnkEQYDFLEWNAKKFGIR-FVPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 150 GETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAP 229
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 230 DEKTLQYVSQ--RAKKP----------WKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSES----------- 286
Cdd:pfam00330 236 DETTFEYLRAtgRPEAPkgeaydkavaWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELvpdpfadavkr 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 287 ------------------THITIDQAFIGSCTNGRIEDLRIAAKILK-----GRKVHPYVRCIVIPASKKVYMQALKEGL 343
Cdd:pfam00330 316 kaaeraleymglgpgtplSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570724915 344 IDIFLEAGCVVSVSTCGPCLGGHmGILAEGERCISTSNRNFPGRMgHPKSEAYLANPAVVAASAVLG 410
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQ-GPGGRTHLASPALVAAAAIAG 460
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-415 |
4.28e-132 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 388.49 E-value: 4.28e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKKEvkPGDLVTVKIDLAMANDVTAPLAIKILEKYNIdKVFDPEKIALVLSHFVP--------AKD 72
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARL--DDGHVLLYIDRHLLNEYTSPQAFSGLRARGR-TVRRPDLTLAVVDHVVPtrpgrdrgITD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 73 IKSAEQAKMVRDFAKKHNIKWF--FQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATG 150
Cdd:PRK12466 79 PGGALQVDYLRENCADFGIRLFdvDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 151 ETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPD 230
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 231 EKTLQYVSQRAKKP-----------WKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSES------------- 286
Cdd:PRK12466 239 ETTFDYLRGRPRAPkgalwdaalayWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRvpdpaaeadparr 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 287 ------------------THITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFL 348
Cdd:PRK12466 319 aameraldymgltpgtplAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570724915 349 EAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGhPKSEAYLANPAVVAASAVLGRIAHP 415
Cdd:PRK12466 399 AAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQG-PGARTHLMSPAMVAAAAVAGHITDV 464
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-419 |
1.01e-119 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 356.74 E-value: 1.01e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKKEvkPGDLVTVKIDLAMANDVTAPLAIKILEKYNIdKVFDPEKIALVLSHFVPAKDIK------ 74
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEE--EDGPDLLYIDRHLVHEVTSPQAFEGLRLAGR-KVRRPDLTFATMDHNVPTTDRDlpiadp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 75 -SAEQAKMVRDFAKKHNIKwFFQEG---EGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATG 150
Cdd:PRK05478 78 vSRIQVETLEKNCKEFGIT-LFDLGdprQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 151 ETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPD 230
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 231 EKTLQYVSQR-----------AKKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSES------------- 286
Cdd:PRK05478 237 ETTFEYLKGRpfapkgedwdkAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKvpdpedfadpvkr 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 287 ------------------THITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFL 348
Cdd:PRK05478 317 asaeralaymglkpgtpiTDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 570724915 349 EAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGhPKSEAYLANPAVVAASAVLGRIAHPEEVV 419
Cdd:PRK05478 397 EAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQG-KGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-412 |
1.70e-111 |
|
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: 332.92 E-value: 1.70e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 31 LAMANDVTAPLAIKILEKY-NIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMVRDFAKKHNIKwFFQEGEGIEHTILPEE 109
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILaALGKVADPSQIACVHDHAVQLEKPVNNEGHKFLSFFAALQGIA-FYRPGVGIIHQIMVEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 110 gLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDG 189
Cdd:cd01351 80 -LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 190 ALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYV--SQRAKKPWKIYH------SDPDAEYSEIYE 261
Cdd:cd01351 159 VLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLeaTGRPLLKNLWLAfpeellADEGAEYDQVIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 262 WDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKE 341
Cdd:cd01351 239 IDLSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSRE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 570724915 342 GLIDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVVAASAVLGRI 412
Cdd:cd01351 319 GYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-415 |
1.04e-105 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 326.33 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKKEVKPGDLVTVKIDLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVlSHFVPAKDIKSAEQAK 80
Cdd:PRK07229 1 MGLTLTEKILYAHLVEGELEPGEEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYV-DHNLLQADFENADDHR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 81 MVRDFAKKHNIkWFFQEGEGIEH-TILpeEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHS 159
Cdd:PRK07229 80 FLQSVAAKYGI-YFSKPGNGICHqVHL--ERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 160 MKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYV-S 238
Cdd:PRK07229 157 VGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLkA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 239 QRAKKPWKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRK 318
Cdd:PRK07229 237 QGREDDWVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVDQVLIGSCTNSSYEDLMRAASILKGKK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 319 VHPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGghMGIlAEGERCIS--TSNRNFPGRMGHPKSEAY 396
Cdd:PRK07229 317 VHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIG--MGQ-APATGNVSlrTFNRNFPGRSGTKDAQVY 393
|
410
....*....|....*....
gi 570724915 397 LANPAVVAASAVLGRIAHP 415
Cdd:PRK07229 394 LASPETAAASALTGVITDP 412
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-413 |
1.38e-103 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 315.26 E-value: 1.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 1 MGMTITEKIIADHAGKKEVKPGDLVTvkIDLAMANDVTAPLAIKILEKYNiDKVFDPEKIALVLSHFVP-------AKDI 73
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLY--IDRHLIHEVTSPQAFEGLRQAG-RKVRRPQKTFATMDHNIPtqnrdfnIKDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 74 KSAEQAKMVRDFAKKHNIKWF--FQEGEGIEHTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGE 151
Cdd:TIGR00170 78 VAKIQVTELEKNCKEFGVRLFdlHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 152 TWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDE 231
Cdd:TIGR00170 158 LKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 232 KTLQYVSQRAKKP-----------WKIYHSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSES-------------- 286
Cdd:TIGR00170 238 TTFEYCKGRPHAPkgkefdkavayWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEvpdpesfadpvdka 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 287 -----------------THITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLE 349
Cdd:TIGR00170 318 saeralaymglepgtplKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 570724915 350 AGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHpKSEAYLANPAVVAASAVLGRIA 413
Cdd:TIGR00170 398 AGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAIHGHFV 460
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
30-412 |
2.44e-90 |
|
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: 278.56 E-value: 2.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 30 DLAMANDVTAPLAIKILEKYNIDKVFDPEKIALVlSHFVPAKDIKSAEQAKMVRDFAKKHNIkWFFQEGEGIEHTiLPEE 109
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVSYV-DHNTLQTDFENADDHRFLQTVAARYGI-YFSRPGNGICHQ-VHLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 110 GLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDG 189
Cdd:cd01585 78 RFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 190 ALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYV-SQRAKKPWKIYHSDPDAEYSEIYEWDAGKLE 268
Cdd:cd01585 158 GVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLaAQGREDDWVELAADADAEYDEEIEIDLSELE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 269 PLVAWPYLPSNVHPVSESTHITIDQAFIGSCTNGRIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFL 348
Cdd:cd01585 238 PLIARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 570724915 349 EAGCVVSVSTCGPCLGghMG-ILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVVAASAVLGRI 412
Cdd:cd01585 318 AAGARILESACGPCIG--MGqAPPTGGVSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
33-412 |
4.63e-79 |
|
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: 249.07 E-value: 4.63e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 33 MANDVTAPLAIKILeKYNIDKVFDPEKIALVLSHFVPAKDIKSAEQAKMVRDFAKKHNIKwFFQEGEGIEHTILPEEGLV 112
Cdd:cd01582 3 MTHDNSWPVALKFM-SIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGID-FYPAGRGIGHQIMIEEGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 113 VPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALY 192
Cdd:cd01582 81 FPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 193 KAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYvsqrakkpwkiyhsdpdaeyseiyewDAGKLEPLVA 272
Cdd:cd01582 161 HAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLIL--------------------------DLSTLSPYVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 273 WPYLPSNVHPVSE--STHITIDQAFIGSCTNGRIEDLRIAAKILKGRK-------VHPYVRCIVIPASKKVYMQALKEGL 343
Cdd:cd01582 215 GPNSVKVSTPLKEleAQNIKINKAYLVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKNGD 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 570724915 344 IDIFLEAGCVVSVSTCGPCLGGHMGILAEGERCISTSNRNFPGRMGHPKSEAYLANPAVVAASAVLGRI 412
Cdd:cd01582 295 WQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
36-412 |
1.71e-46 |
|
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: 165.31 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 36 DVTAPLAIKILEKYNIDKVFDPEKIA---LVLSHFVPAKDIKSA-EQAKMVRDF----AKKHNIKwFFQEGEGIEHTILP 107
Cdd:cd01584 6 DATAQMALLQFMSSGLPKVAVPSTIHcdhLIEAQVGGEKDLKRAkDINKEVYDFlasaGAKYGIG-FWKPGSGIIHQIVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 108 EEgLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMAtGETW-LRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIG 186
Cdd:cd01584 85 EN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGKLSGWTSPKDVILKVAGILT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 187 VDGALYKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQY--------VSQRAKK-PWKIYHSDPDAEYS 257
Cdd:cd01584 163 VKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYlkatgraeIADLADEfKDDLLVADEGAEYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 258 EIYEWDAGKLEPLVAWPYLPSNVHPVSESTHIT--------IDQAFIGSCTNGRIEDLRIAAKILKGRKVH---PYVRCI 326
Cdd:cd01584 243 QLIEINLSELEPHINGPFTPDLATPVSKFKEVAekngwpldLRVGLIGSCTNSSYEDMGRAASIAKQALAHglkCKSIFT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 327 VIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLG--GHMGILAEGERCISTS-NRNFPGRM-GHPKSEAYLANPAV 402
Cdd:cd01584 323 ITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGqwDRKDIKKGEKNTIVTSyNRNFTGRNdANPATHAFVASPEI 402
|
410
....*....|
gi 570724915 403 VAASAVLGRI 412
Cdd:cd01584 403 VTAMAIAGTL 412
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
98-417 |
1.37e-43 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 163.04 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 98 GEGIEHTILPEegLVVPGDLVVGADSHTctygalgAFSTGM----GSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVM 173
Cdd:PRK09238 464 GDGVIHSWLNR--MLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGIT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 174 GKDLIlHTI-------GQIGVDGALYK------AMEFEGeaIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTL-QY--- 236
Cdd:PRK09238 535 LRDLV-HAIpyyaikqGLLTVEKKGKKnifsgrILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKEPIiEYlrs 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 237 ------------------VSQRAKK--PW----KIYHSDPDAEYSEIYEWDAGKL-EPLVAWPYLPSNVHPVSESTHITI 291
Cdd:PRK09238 612 nivllkwmiaegygdartLERRIAAmeEWlanpELLEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLSEVAGTKI 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 292 DQAFIGSC-TNgrIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGIl 370
Cdd:PRK09238 692 DEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARV- 768
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 570724915 371 AEGERCISTSNRNFPGRMGhPKSEAYLANPAVVAASAVLGRIAHPEE 417
Cdd:PRK09238 769 ADGATVFSTSTRNFPNRLG-KGANVYLGSAELAAVCALLGRIPTVEE 814
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
7-412 |
5.99e-42 |
|
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: 153.42 E-value: 5.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 7 EKIIADHAGKKEVKPGDLVTVKIDLAMANDVTAPLAIKILE-----KYNIDKVFD--------PEKIALVLSHFVPAkdi 73
Cdd:cd01581 3 QKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKelaclGFSADLVMQsfchtaayPKPVDVKTHRTLPD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 74 ksaeqakMVRDFAKKHnikwfFQEGEGIEHTILPEegLVVPGDLVVGADSHT-----CTYGAlgafstgmGSTDIAYAMA 148
Cdd:cd01581 80 -------FISNRGGVA-----LRPGDGVIHSWLNR--MLLPDTVGTGGDSHTrfpigISFPA--------GSGLVAFAAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 149 TGETWLRVPHSMKFIFYGKPSPWVMGKDLI-----------LHTIGQIGVDGALY-KAMEFEGeaIRHLSMDQRFTITNM 216
Cdd:cd01581 138 TGVMPLDMPESVLVRFKGKMQPGITLRDLVnaipyyaiqqgLLTVEKKGKKNVFNgRILEIEG--LPDLKVEQAFELTDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 217 AVEAGAKNGIIAPDEKTL-QYVSQ-----------------------RAKKPW----KIYHSDPDAEYSEIYEWDAGKL- 267
Cdd:cd01581 216 SAERSAAACTVRLDKEPViEYLESnvvlmkimiangyddartllrriIAMEEWlanpPLLEPDADAEYAAVIEIDLDDIk 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 268 EPLVAWPYLPSNVHPVSESTHITIDQAFIGSC-TNgrIEDLRIAAKILKGRKVHPyVRCIVIPASKKVYMQALKEGLIDI 346
Cdd:cd01581 296 EPILACPNDPDDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSI 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 570724915 347 FLEAGCVVSVSTCGPCLGGHMGIlAEGERCISTSNRNFPGRMGHpKSEAYLANPAVVAASAVLGRI 412
Cdd:cd01581 373 FGDAGARTEMPGCSLCMGNQARV-ADGATVFSTSTRNFDNRVGK-GAEVYLGSAELAAVCALLGRI 436
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
56-412 |
1.21e-33 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 133.98 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 56 DPEKIA------LVLSHFVPAKDIKSAEQAK------MVRDFAKKHNIKWFFQE---------GEGIEH---------TI 105
Cdd:PTZ00092 120 DPAKINplvpvdLVIDHSVQVDFSRSPDALElnqeieFERNLERFEFLKWGSKAfknllivppGSGIVHqvnleylarVV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 106 LPEEGLVVPgDLVVGADSHTCTYGALGAFSTGMGSTDiAYAMATGETWLRV-PHSMKFIFYGKPSPWVMGKDLILhTIGQ 184
Cdd:PTZ00092 200 FNKDGLLYP-DSVVGTDSHTTMINGLGVLGWGVGGIE-AEAVMLGQPISMVlPEVVGFKLTGKLSEHVTATDLVL-TVTS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 185 I----GVDGalyKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQ---------------RAKKPW 245
Cdd:PTZ00092 277 MlrkrGVVG---KFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQtgrseekveliekylKANGLF 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 246 KIYHSDPdaEYSEIYEWDAGKLEPLVAWPYLP------SNVH---------PVS------------------------ES 286
Cdd:PTZ00092 354 RTYAEQI--EYSDVLELDLSTVVPSVAGPKRPhdrvplSDLKkdftaclsaPVGfkgfgipeekhekkvkftykgkeyTL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 287 THITIDQAFIGSCTNGRIEDLRIAAKIL------KGRKVHPYVRCIVIPASKKV--YMQalKEGLIDiFLEA-GCVVSVS 357
Cdd:PTZ00092 432 THGSVVIAAITSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVtkYLE--ASGLLK-YLEKlGFYTAGY 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 570724915 358 TCGPCLGGHMGILAEGERCIS----------TSNRNFPGRMgHPKSEA-YLANPAVVAASAVLGRI 412
Cdd:PTZ00092 509 GCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAGRV 573
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
98-427 |
1.61e-31 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 127.73 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 98 GEGIEHTILPEegLVVPGDLVVGADSHTctygalgAFSTGM----GSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVM 173
Cdd:PLN00094 538 GDGVIHSWLNR--MLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGIT 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 174 GKDLIlHTIGQIGV-DGALYKAME-----FEG-----EAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTL-QYVSQR- 240
Cdd:PLN00094 609 LRDLV-HAIPYTAIqDGLLTVEKKgkknvFSGrileiEGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIiEYLNSNv 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 241 ----------------------AKKPW----KIYHSDPDAEYSEIYEWDAGKL-EPLVAWPYLPSNVHPVSESTHITIDQ 293
Cdd:PLN00094 688 vmlkwmiaegygdrrtlerriaRMQQWladpELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGDKIDE 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 294 AFIGSC-TNgrIEDLRIAAKILKGRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGHMGIlAE 372
Cdd:PLN00094 768 VFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARV-AE 844
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 570724915 373 GERCISTSNRNFPGRMGHpKSEAYLANPAVVAASAVLGRIAHPEEVVSLKEVEEA 427
Cdd:PLN00094 845 KSTVVSTSTRNFPNRLGK-GANVYLASAELAAVAAILGRLPTVEEYLSYMEKLDA 898
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
103-412 |
3.71e-31 |
|
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: 126.37 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 103 HTILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMAtGETW-LRVPHSMKFIFYGKPSPWVMGKDLILhT 181
Cdd:COG1048 191 WTREEDGETVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAML-GQPVsMLIPEVVGVKLTGKLPEGVTATDLVL-T 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 182 IGQI----GVDGalyKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQ---------------RAK 242
Cdd:COG1048 269 VTEMlrkkGVVG---KFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLtgrseeqielveayaKAQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 243 KPWKIYhSDPDAEYSEIYEWDAGKLEPLVAWPYLPSNVHPVSE-------------------STHITIDQ---------- 293
Cdd:COG1048 346 GLWRDP-DAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDlkeafraalaapvgeeldkPVRVEVDGeefelghgav 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 294 --AFIGSCTNGRIEDLRIAAKIL------KGRKVHPYVRCIVIPASKKVYMQALKEGLIDiFLEA--------GCvvsvS 357
Cdd:COG1048 425 viAAITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLLP-YLEAlgfnvvgyGC----T 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570724915 358 TC----GPCLGGHMGILAEGER--CISTS-NRNFPGRMGHPKSEAYLANPAVVAASAVLGRI 412
Cdd:COG1048 500 TCignsGPLPPEISEAIEENDLvvAAVLSgNRNFEGRIHPDVKANFLASPPLVVAYALAGTV 561
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
115-389 |
1.70e-29 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 121.27 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 115 GDLVVGADSHTcTYGALGAFSTGMGSTDIAYAMaTGETW-LRVPHSMKFIFYGKPSPWVMGKDLILHTIGQIGVDGALY- 192
Cdd:PRK11413 142 GKMILGSDSHT-RYGALGTMAVGEGGGELVKQL-LNDTYdIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVKn 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 193 KAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQRAKKP-WKIYHSDPDAEYSEIYEWDAGKLEPLV 271
Cdd:PRK11413 220 KVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQdYCELNPQPMAYYDGCISVDLSAIKPMI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 272 AWPYLPSNVHPVSE---------------------------------STHITIDQAFIGSCTNGRIEDLRIAAKILKGRK 318
Cdd:PRK11413 300 ALPFHPSNVYEIDElnqnltdilreveieservahgkaklslldkieNGRLKVQQGIIAGCSGGNYENVIAAANALRGQS 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570724915 319 V-HPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTCGPCLGGhmG-ILAEGERCISTSNRNFPGRMG 389
Cdd:PRK11413 380 CgNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGA--GdTPANNGLSIRHTTRNFPNREG 450
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
56-412 |
3.25e-28 |
|
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: 115.09 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 56 DPEKIA------LVLSHFVPAKDIKSAEQAK--MVRDFAKKHN----IKW---FFQE------GEGIEH----------- 103
Cdd:cd01586 29 DPEKINplipvdLVIDHSVQVDFYGTADALAknMKLEFERNREryefLKWgqkAFKNlrvvppGTGIIHqvnleylarvv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 104 -TILPEEGLVVPGDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILhTI 182
Cdd:cd01586 109 fTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVL-TV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 183 GQI----GVDGalyKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDektlqyvsqrakkpwkiyhsdpdaeySE 258
Cdd:cd01586 188 TQMlrkvGVVG---KFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD--------------------------TQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 259 IYEWDAGKLEPLVAWPYLPSNVHPVSESTHItidqAFIGSCTNGRIEDLRIAAKIL------KGRKVHPYVRCIVIPASK 332
Cdd:cd01586 239 VVELDLSTVEPSVSGPKRPQDRVPLHGSVVI----AAITSCTNTSNPSVMLAAGLLakkaveLGLKVKPYVKTSLAPGSR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 333 KVYMQALKEGLIDiFLEA--------GCvvsvSTCgpclGGHMGILAEG-ERCIS----------TSNRNFPGRMgHPKS 393
Cdd:cd01586 315 VVTKYLEASGLLP-YLEKlgfhvvgyGC----TTC----IGNSGPLPEEvEEAIKendlvvaavlSGNRNFEGRI-HPLV 384
|
410 420
....*....|....*....|
gi 570724915 394 EA-YLANPAVVAASAVLGRI 412
Cdd:cd01586 385 RAnYLASPPLVVAYALAGTV 404
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
98-413 |
1.28e-26 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 112.72 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 98 GEGIEHTILPE-------------EGLVVPgDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIF 164
Cdd:PRK12881 176 GTGIMHQVNLEylarvvhtkeddgDTVAYP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVEL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 165 YGKPSPWVMGKDLIL---HTIGQIGVDGalyKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQ-- 239
Cdd:PRK12881 255 TGKLREGVTATDLVLtvtEMLRKEGVVG---KFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLtg 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 240 -------------RAKKPWKiyhsDPDAE--YSEIYEWDAGKLEPLVAWPYLPSNVHPVSESTHITIDQ----------- 293
Cdd:PRK12881 332 rteaqialveayaKAQGLWG----DPKAEprYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLfskpvaengfa 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 294 ------------------AFIGSCTNGRIEDLRIAAKIL------KGRKVHPYVRCIVIPASKKV--YMQalKEGLIDiF 347
Cdd:PRK12881 408 kkaqtsngvdlpdgavaiAAITSCTNTSNPSVLIAAGLLakkaveRGLTVKPWVKTSLAPGSKVVteYLE--RAGLLP-Y 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 348 LEA--------GCvvsvSTC----GPCLGG-HMGILAEGERCIS--TSNRNFPGRMgHPKSEA-YLANPAVVAASAVLGR 411
Cdd:PRK12881 485 LEKlgfgivgyGC----TTCignsGPLTPEiEQAITKNDLVAAAvlSGNRNFEGRI-HPNIKAnFLASPPLVVAYALAGT 559
|
..
gi 570724915 412 IA 413
Cdd:PRK12881 560 VR 561
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
56-412 |
9.71e-25 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 107.20 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 56 DPEKIA------LVLSHFVPAKDIKS--AEQAKMVRDFAKKHN----IKW---FFQE------GEGIEHTILPE------ 108
Cdd:PLN00070 152 DPNKINplvpvdLVIDHSVQVDVARSenAVQANMELEFQRNKErfafLKWgstAFQNmlvvppGSGIVHQVNLEylgrvv 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 109 ---EGLVVPgDLVVGADSHTCTYGALGAFSTGMGSTDIAYAMATGETWLRVPHSMKFIFYGKPSPWVMGKDLILhTIGQI 185
Cdd:PLN00070 232 fntDGILYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVL-TVTQM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 186 ----GVDGalyKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQYVSQ---------------RAKKPWk 246
Cdd:PLN00070 310 lrkhGVVG---KFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLtgrsdetvamieaylRANKMF- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 247 IYHSDPDAE--YSEIYEWDAGKLEPLVAWPYLPSNVHPV---------------------------------------SE 285
Cdd:PLN00070 386 VDYNEPQQErvYSSYLELDLEDVEPCISGPKRPHDRVPLkemkadwhscldnkvgfkgfavpkeaqskvakfsfhgqpAE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 286 STHITIDQAFIGSCTNGRIEDLRIAAKILK------GRKVHPYVRCIVIPASKKVYMQALKEGLIDIFLEAGCVVSVSTC 359
Cdd:PLN00070 466 LRHGSVVIAAITSCTNTSNPSVMLGAGLVAkkacelGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGC 545
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 570724915 360 GPCLGGHMGILAEGERCIS----------TSNRNFPGRMgHPKSEA-YLANPAVVAASAVLGRI 412
Cdd:PLN00070 546 TTCIGNSGELDESVASAITendivaaavlSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAGTV 608
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
116-412 |
1.37e-21 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 97.50 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 116 DLVVGADSHTCTYGALGAFSTGMGSTDIAYAMaTGE-TWLRVPHSMKFIFYGKPSPWVMGKDLILhTIGQI----GVDGa 190
Cdd:PRK09277 206 DTLVGTDSHTTMINGLGVLGWGVGGIEAEAAM-LGQpSSMLIPEVVGVKLTGKLPEGVTATDLVL-TVTEMlrkkGVVG- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 191 lyKAMEFEGEAIRHLSMDQRFTITNMAVEAGAKNGIIAPDEKTLQY-------------VSQRAKKP--WkiYHSDPDAE 255
Cdd:PRK09277 283 --KFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYlrltgrdeeqvalVEAYAKAQglW--RDPLEEPV 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 256 YSEIYEWDAGKLEPLVAWPYLP------SNVH-----------------PVSESTHITIDQ-----AFIGSCTNGRIEDL 307
Cdd:PRK09277 359 YTDVLELDLSTVEPSLAGPKRPqdriplSDVKeafaksaelgvqgfgldEAEEGEDYELPDgavviAAITSCTNTSNPSV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570724915 308 RIAAKIL------KGRKVHPYVRCIVIPASKKV--YmqaLKE-GLIDiFLEA--------GCvvsvSTCgpclGGHMGIL 370
Cdd:PRK09277 439 MIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVtdY---LEKaGLLP-YLEAlgfnlvgyGC----TTC----IGNSGPL 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 570724915 371 AEG-ERCI------STS----NRNFPGRMgHPKSEA-YLANPAVVAASAVLGRI 412
Cdd:PRK09277 507 PPEiEKAIndndlvVTAvlsgNRNFEGRI-HPLVKAnYLASPPLVVAYALAGTV 559
|
|
| |
