|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
2-277 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 588.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:PRK09277 243 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAASAELELN 161
Cdd:PRK09277 323 TLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 162 TAQRDRQPVdytmnGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLAQ 241
Cdd:PRK09277 403 GFGLDEAEE-----GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEK 477
|
250 260 270
....*....|....*....|....*....|....*.
gi 435304079 242 AKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:PRK09277 478 AGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKA 513
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
2-277 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 564.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:COG1048 241 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGD-EPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAASaeLEL 160
Cdd:COG1048 321 TLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDApEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA--LAA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 NTAQRDRQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLA 240
Cdd:COG1048 399 PVGEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 435304079 241 QAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:COG1048 479 RAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEA 515
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
1-277 |
1.39e-174 |
|
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes. [Energy metabolism, TCA cycle]
Pssm-ID: 273562 [Multi-domain] Cd Length: 876 Bit Score: 504.34 E-value: 1.39e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDA 80
Cdd:TIGR01341 225 YYMNVPEVIGVKLTGKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 ITLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFaaSAELEL 160
Cdd:TIGR01341 305 VTLQYLRLTGRDGDHVELVEKYARAQGLFYDDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKF--SKELEK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 NTAQRD----RQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVS 236
Cdd:TIGR01341 383 NGGDKGftlrKEPLKKKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVT 462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 435304079 237 DYLAQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:TIGR01341 463 DYLAESGLLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEA 503
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
2-272 |
2.85e-133 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 384.85 E-value: 2.85e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:pfam00330 159 EMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDET 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVelVEAYAKAQGMWRNPGDE-PVFTSTLELDMGDVEASLAGPKRPQDRVAL-GDVPKAFAASAEle 159
Cdd:pfam00330 239 TFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPgAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLsELVPDPFADAVK-- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 160 lntAQRDRQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLaKKAVTLGLKRQPWVKASLAPGSKVVSDYL 239
Cdd:pfam00330 315 ---RKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASVVPGSEVVRAYA 390
|
250 260 270
....*....|....*....|....*....|...
gi 435304079 240 AQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPE 272
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP 423
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
1-277 |
2.49e-128 |
|
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: 370.10 E-value: 2.49e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDa 80
Cdd:cd01586 158 ISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 itleymrlsgrsddlvelveayakaqgmwrnpgdepvfTSTLELDMGDVEASLAGPKRPQDRVALgdvpkafaasaelel 160
Cdd:cd01586 237 --------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 ntaqrdrqpvdytmngqpyqlpDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLA 240
Cdd:cd01586 264 ----------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLE 321
|
250 260 270
....*....|....*....|....*....|....*..
gi 435304079 241 QAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:cd01586 322 ASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEA 358
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
2-277 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 588.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:PRK09277 243 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAASAELELN 161
Cdd:PRK09277 323 TLDYLRLTGRDEEQVALVEAYAKAQGLWRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 162 TAQRDRQPVdytmnGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLAQ 241
Cdd:PRK09277 403 GFGLDEAEE-----GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEK 477
|
250 260 270
....*....|....*....|....*....|....*.
gi 435304079 242 AKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:PRK09277 478 AGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKA 513
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
2-277 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 564.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:COG1048 241 SMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGD-EPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAASaeLEL 160
Cdd:COG1048 321 TLDYLRLTGRSEEQIELVEAYAKAQGLWRDPDApEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA--LAA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 NTAQRDRQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLA 240
Cdd:COG1048 399 PVGEELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 478
|
250 260 270
....*....|....*....|....*....|....*..
gi 435304079 241 QAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:COG1048 479 RAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEA 515
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
1-277 |
1.39e-174 |
|
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes. [Energy metabolism, TCA cycle]
Pssm-ID: 273562 [Multi-domain] Cd Length: 876 Bit Score: 504.34 E-value: 1.39e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDA 80
Cdd:TIGR01341 225 YYMNVPEVIGVKLTGKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 ITLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFaaSAELEL 160
Cdd:TIGR01341 305 VTLQYLRLTGRDGDHVELVEKYARAQGLFYDDSEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKF--SKELEK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 NTAQRD----RQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVS 236
Cdd:TIGR01341 383 NGGDKGftlrKEPLKKKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVT 462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 435304079 237 DYLAQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:TIGR01341 463 DYLAESGLLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEA 503
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
2-277 |
5.23e-173 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 500.61 E-value: 5.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:PRK12881 243 YMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAAsaeleln 161
Cdd:PRK12881 323 TLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSD------- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 162 TAQRDRQPVDYTMNGQP---YQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDY 238
Cdd:PRK12881 396 LFSKPVAENGFAKKAQTsngVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEY 475
|
250 260 270
....*....|....*....|....*....|....*....
gi 435304079 239 LAQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:PRK12881 476 LERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQA 514
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
1-277 |
7.26e-144 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 425.97 E-value: 7.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDA 80
Cdd:PTZ00092 245 ISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 ITLEYMRLSGRSDDLVELVEAYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAASAELEL 160
Cdd:PTZ00092 325 KTLDYLKQTGRSEEKVELIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 N------TAQRDRQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKV 234
Cdd:PTZ00092 405 GfkgfgiPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKV 484
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 435304079 235 VSDYLAQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:PTZ00092 485 VTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEA 527
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
1-277 |
1.52e-135 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 405.34 E-value: 1.52e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDA 80
Cdd:PLN00070 277 MSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDH 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 ITLEYMRLSGRSDDLVELVEAYAKAQGM---WRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVP-------- 149
Cdd:PLN00070 357 VTLQYLKLTGRSDETVAMIEAYLRANKMfvdYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKadwhscld 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 150 -----KAFAASAELELNTAQrdrqpvdYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWV 224
Cdd:PLN00070 437 nkvgfKGFAVPKEAQSKVAK-------FSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWI 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 435304079 225 KASLAPGSKVVSDYLAQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:PLN00070 510 KTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASA 562
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
2-272 |
2.85e-133 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 384.85 E-value: 2.85e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAI 81
Cdd:pfam00330 159 EMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDET 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 82 TLEYMRLSGRSDDLVelVEAYAKAQGMWRNPGDE-PVFTSTLELDMGDVEASLAGPKRPQDRVAL-GDVPKAFAASAEle 159
Cdd:pfam00330 239 TFEYLRATGRPEAPK--GEAYDKAVAWKTLASDPgAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLsELVPDPFADAVK-- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 160 lntAQRDRQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLaKKAVTLGLKRQPWVKASLAPGSKVVSDYL 239
Cdd:pfam00330 315 ---RKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASVVPGSEVVRAYA 390
|
250 260 270
....*....|....*....|....*....|...
gi 435304079 240 AQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPE 272
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP 423
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
1-277 |
2.49e-128 |
|
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: 370.10 E-value: 2.49e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDa 80
Cdd:cd01586 158 ISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 itleymrlsgrsddlvelveayakaqgmwrnpgdepvfTSTLELDMGDVEASLAGPKRPQDRVALgdvpkafaasaelel 160
Cdd:cd01586 237 --------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL--------------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 ntaqrdrqpvdytmngqpyqlpDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLA 240
Cdd:cd01586 264 ----------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLE 321
|
250 260 270
....*....|....*....|....*....|....*..
gi 435304079 241 QAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETA 277
Cdd:cd01586 322 ASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEA 358
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
1-276 |
7.56e-47 |
|
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: 160.74 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 1 MSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDA 80
Cdd:cd01351 121 AWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 81 ITLEYMRLSGRSDdLVELVEAYAKAQgmwrNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKafaasaelel 160
Cdd:cd01351 201 TTLKWLEATGRPL-LKNLWLAFPEEL----LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG---------- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 161 ntaqrdrqpvdytmngqpyqlpdGAVVIAAITSCTNtSNPSVLMAAGLLAKKAvtlglKRQPWVKASLAPGSKVVSDYLA 240
Cdd:cd01351 266 -----------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGA-----KVAPGVRLIVTPGSRMVYATLS 316
|
250 260 270
....*....|....*....|....*....|....*.
gi 435304079 241 QAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIET 276
Cdd:cd01351 317 REGYYEILVDSGARILPPGCGPCMGNGARLVADGEV 352
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
6-265 |
7.58e-33 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 126.41 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 6 PDVVGFKLTGKLREGITATDLVLTvtqMLRKHGV---VGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAIT 82
Cdd:PRK07229 154 PKVVGVKLTGKLPPWVSAKDVILE---LLRRLTVkggVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 83 LEYMRLSGRSDDLVELVeayakaqgmwrnPGDEPVFTSTLELDMGDVEASLAGPKRPqDRValgdVPkafaaSAELElnt 162
Cdd:PRK07229 231 REFLKAQGREDDWVELL------------ADPDAEYDEVIEIDLSELEPLIAGPHSP-DNV----VP-----VSEVA--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 163 aqrdRQPVDYtmngqpyqlpdgavviAAITSCTNTSNPSVLMAAGLLAKKAVTlglkrqpwVKASL--APGSKVVSDYLA 240
Cdd:PRK07229 286 ----GIKVDQ----------------VLIGSCTNSSYEDLMRAASILKGKKVH--------PKVSLviNPGSRQVLEMLA 337
|
250 260
....*....|....*....|....*
gi 435304079 241 QAKLTPYLDELGFNLVGYGCTTCIG 265
Cdd:PRK07229 338 RDGALADLIAAGARILENACGPCIG 362
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
3-265 |
1.82e-32 |
|
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: 122.56 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 3 MLIPDVVGFKLTGKLREGITATDLVLtvtQMLRKHGV---VGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPID 79
Cdd:cd01585 122 IPMPKVVGVRLTGELPPWVTAKDVIL---ELLRRLTVkggVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 80 AITLEYMRLSGRSDDLVELVeayakaqgmwrnPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVpkafaasaele 159
Cdd:cd01585 199 ERTREFLAAQGREDDWVELA------------ADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREV----------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 160 lntaqrDRQPVDYTmngqpyqlpdgavviaAITSCTNTSNPSVLMAAGLLAKKAVtlglkrQPWVKASLAPGSKVVSDYL 239
Cdd:cd01585 256 ------AGIKVDQV----------------AIGSCTNSSYEDLMTVAAILKGRRV------HPHVSMVVAPGSKQVLEML 307
|
250 260
....*....|....*....|....*.
gi 435304079 240 AQAKLTPYLDELGFNLVGYGCTTCIG 265
Cdd:cd01585 308 ARNGALADLLAAGARILESACGPCIG 333
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
6-272 |
6.53e-26 |
|
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: 105.11 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 6 PDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAITLEY 85
Cdd:COG0065 156 PETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEY 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 86 MRlsGRsddlvelveAYAKAQGMWRNPGdePVFTSTLELDMGDVEASLAGPKRPQDRVALGDVpkafaasaelelntaqr 165
Cdd:COG0065 236 LK--GR---------PFAPWRTLKSDED--AVYDKEVEIDASDLEPQVAWPHSPDNVVPVSEL----------------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 166 DRQPVDYtmngqpyqlpdgavviAAITSCTNtsnpSVL----MAAGLLAkkavtlGLKRQPWVKASLAPGSKVVsdyLAQ 241
Cdd:COG0065 286 EGIKIDQ----------------VFIGSCTN----GRIedlrAAAEILK------GRKVAPGVRAIVVPGSQEV---YRQ 336
|
250 260 270
....*....|....*....|....*....|....*
gi 435304079 242 AKLTPYLDEL---GFNLVGYGCTTCIG-NSGPLPE 272
Cdd:COG0065 337 AEAEGLDEIFieaGAEWREPGCGMCLGmNMGVLAP 371
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
6-265 |
1.56e-22 |
|
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: 95.97 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 6 PDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAITLEY 85
Cdd:cd01584 133 PKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKY 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 86 MRLSGRSdDLVELVEAYAKAQgmwRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKafaasaelelnTAQR 165
Cdd:cd01584 213 LKATGRA-EIADLADEFKDDL---LVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKE-----------VAEK 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 166 DRQPVDytmngqpyqlpdgaVVIAAITSCTNTSNPSVLMAAGlLAKKAVTLGLKrqPWVKASLAPGSKVVSDYLAQAKLT 245
Cdd:cd01584 278 NGWPLD--------------LRVGLIGSCTNSSYEDMGRAAS-IAKQALAHGLK--CKSIFTITPGSEQIRATIERDGLL 340
|
250 260
....*....|....*....|
gi 435304079 246 PYLDELGFNLVGYGCTTCIG 265
Cdd:cd01584 341 QTFRDAGGIVLANACGPCIG 360
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
13-265 |
1.32e-19 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 88.04 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 13 LTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAITLEYMRlsGRS 92
Cdd:PRK12466 172 VDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLR--GRP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 93 DDLVElvEAYAKAQGMWRN-PGDE-PVFTSTLELDMGDVEASLAGPKRPQDRVALGD-VPKAFAASAELELNTAQRdrqP 169
Cdd:PRK12466 250 RAPKG--ALWDAALAYWRTlRSDAdAVFDREVEIDAADIAPQVTWGTSPDQAVPITGrVPDPAAEADPARRAAMER---A 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 170 VDYtMNGQPYQLPDGAVVIAA-ITSCTNtSNPSVLMAAGllakkAVTLGLKRQPWVKASLAPGSKVVSDYLAQAKLTPYL 248
Cdd:PRK12466 325 LDY-MGLTPGTPLAGIPIDRVfIGSCTN-GRIEDLRAAA-----AVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIF 397
|
250
....*....|....*..
gi 435304079 249 DELGFNLVGYGCTTCIG 265
Cdd:PRK12466 398 IAAGFEWREPGCSMCLA 414
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
5-139 |
3.78e-19 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 86.38 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 5 IPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAITLE 84
Cdd:PRK00402 155 VPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 435304079 85 YmrLSGRSDDLVELVEAYAKAqgmwrnpgdepVFTSTLELDMGDVEASLAGPKRP 139
Cdd:PRK00402 235 Y--LKERAGRDYKPWKSDEDA-----------EYEEVYEIDLSKLEPQVAAPHLP 276
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
2-265 |
7.05e-16 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 77.08 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 2 SMLIpdvvgfKLTGKLREGITATDLVLTVtqmLRKHGV---VGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPI 78
Cdd:PRK05478 165 TMKI------EVDGKLPPGVTAKDIILAI---IGKIGTaggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 79 DAITLEYMRlsGRsdDLVELVEAYAKAQGMWRN-PGDE-PVFTSTLELDMGDVEASLAGPKRPQDRVAL-GDVPkafaaS 155
Cdd:PRK05478 236 DETTFEYLK--GR--PFAPKGEDWDKAVAYWKTlKSDEdAVFDKVVTLDAADIEPQVTWGTNPGQVISIdGKVP-----D 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 156 AELELNTAQRD--RQPVDYtMNGQPYQ-LPDGAVVIAAITSCTNtSNPSVLMAAGLLAKkavtlGLKRQPWVKASLAPGS 232
Cdd:PRK05478 307 PEDFADPVKRAsaERALAY-MGLKPGTpITDIKIDKVFIGSCTN-SRIEDLRAAAAVVK-----GRKVAPGVRALVVPGS 379
|
250 260 270
....*....|....*....|....*....|....*.
gi 435304079 233 KVVSdylAQAK---LTPYLDELGFNLVGYGCTTCIG 265
Cdd:PRK05478 380 GLVK---AQAEaegLDKIFIEAGFEWREPGCSMCLA 412
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
5-80 |
1.16e-14 |
|
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: 73.03 E-value: 1.16e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 435304079 5 IPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDA 80
Cdd:cd01582 124 IPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA 199
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
6-139 |
4.71e-07 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 50.78 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435304079 6 PDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVV-GKFVEFYGDGLDSLPLADRATIANMSPEygATC--GFFPIDAIT 82
Cdd:PRK11413 183 PGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTE--TTClsSIWQTDEEV 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 435304079 83 LEYMRLSGRSDDLVELveayakaqgmwrNPGDEPVFTSTLELDMGDVEASLAGPKRP 139
Cdd:PRK11413 261 HNWLALHGRGQDYCEL------------NPQPMAYYDGCISVDLSAIKPMIALPFHP 305
|
|
| |
