|
Name |
Accession |
Description |
Interval |
E-value |
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
3-302 |
3.20e-161 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 451.04 E-value: 3.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 3 RLANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAM 82
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 83 IAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAEH-GYFLPQQFTNPANAVIHRLTTGPE 161
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETpGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 162 IVEAFDGlTLDAFVagvgtggtitgaGAV------------LKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFV 229
Cdd:COG0031 162 IWEQTDG-KVDAFV------------AGVgtggtitgvgryLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFV 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126589967 230 PTVLDTEIYSSVFPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIVPSNGERYLST 302
Cdd:COG0031 229 PKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
8-305 |
1.72e-158 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 444.12 E-value: 1.72e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 8 IAELVGKTPIVKLNHATsENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMIAAAK 87
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIE-GCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 88 GYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAEHG--YFLPQQFTNPANAVIHRLTTGPEIVEA 165
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnsYFMLQQFENPANPEIHRKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 166 FDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIYSSVFPVE 245
Cdd:TIGR01139 160 TDG-KLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 246 NEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIVPSNGERYLSTPLY 305
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
8-305 |
6.58e-148 |
|
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273463 Cd Length: 299 Bit Score: 417.07 E-value: 6.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 8 IAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMIAAAK 87
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 88 GYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAE-HGYFLPQQFTNPANAVIHRLTTGPEIVEAF 166
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 167 DGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIYSSVFPVEN 246
Cdd:TIGR01136 161 DG-RIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 247 EVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLG-KGSNVLAIVPSNGERYLSTPLY 305
Cdd:TIGR01136 240 EDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
13-301 |
2.35e-143 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 405.36 E-value: 2.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 13 GKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMIAAAKGYKAI 92
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 93 LVMPETMSLERRNLLRAYGAELVLTPGPA--GMKGAIAKAEELSAEH-GYFLPQQFTNPANAVIHRLTTGPEIVEAFDGl 169
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETpNAFWLNQFENPANPEAHYETTAPEIWEQLDG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 170 TLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIYSSVFPVENEVA 249
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 126589967 250 FEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIVPSNGERYLS 301
Cdd:cd01561 240 FAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
2-306 |
7.09e-102 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 301.46 E-value: 7.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 2 SRLANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTI-IEPTSGNTGIGL 80
Cdd:PLN02565 3 SSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 81 AMIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAE--HGYFLpQQFTNPANAVIHRLTT 158
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKtpNSYIL-QQFENPANPKIHYETT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 159 GPEIVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIY 238
Cdd:PLN02565 162 GPEIWKGTGG-KVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126589967 239 SSVFPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKR-LGKGSNVLAIVPSNGERYLSTPLYQ 306
Cdd:PLN02565 241 DEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
2-302 |
6.23e-99 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 294.08 E-value: 6.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 2 SRLANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLA 81
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 82 MIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPA------GMKGAIAKAEEL--SAEHGYFLPQQFTNPANAVI 153
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPyanpnnYVKGAGRLAEELvaSEPNGAIWANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 154 HRLTTGPEIVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLS---GGQ---PGPHKIQGIGAG 227
Cdd:PRK10717 161 HYETTGPEIWEQTDG-KVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyykTGElkaEGSSITEGIGQG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126589967 228 FVPTVLDTEIYSSVFPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIVPSNGERYLST 302
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK 314
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-306 |
2.10e-90 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 273.76 E-value: 2.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 2 SRLANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGT-IIEPTSGNTGIGL 80
Cdd:PLN02556 47 TKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 81 AMIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAEH-GYFLPQQFTNPANAVIHRLTTG 159
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTpDAFMLQQFSNPANTQVHFETTG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 160 PEIVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIYS 239
Cdd:PLN02556 207 PEIWEDTLG-QVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVME 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126589967 240 SVFPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRL-GKGSNVLAIVPSNGERYLSTPLYQ 306
Cdd:PLN02556 286 KVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPeNKGKLIVTVHPSFGERYLSSVLFQ 353
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
4-306 |
2.05e-89 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 269.57 E-value: 2.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 4 LANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPG-GTIIEPTSGNTGIGLAM 82
Cdd:PLN00011 7 IKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 83 IAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEE-LSAEHGYFLPQQFTNPANAVIHRLTTGPE 161
Cdd:PLN00011 87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEiLSKTPGGYIPQQFENPANPEIHYRTTGPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 162 IVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIYSSV 241
Cdd:PLN00011 167 IWRDSAG-KVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEI 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126589967 242 FPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKR-LGKGSNVLAIVPSNGERYLSTPLYQ 306
Cdd:PLN00011 246 IQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVIFPSGGERYLSTKLFE 311
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
6-305 |
4.67e-89 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 267.89 E-value: 4.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 6 NSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMIAA 85
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 86 AKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAEHGYFLPQQFTNPANAVIHRLTTGPEIVEA 165
Cdd:PRK11761 84 IKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEIWRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 166 FDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDspvlsGGQpgphkIQGI---GAGFVPTVLDTEIYSSVF 242
Cdd:PRK11761 164 TEG-RITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEE-----GSS-----IPGIrrwPEEYLPKIFDASRVDRVL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126589967 243 PVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLgKGSNVLAIVPSNGERYLSTPLY 305
Cdd:PRK11761 233 DVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLSTGVF 294
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-306 |
3.78e-87 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 267.41 E-value: 3.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 4 LANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTI-IEPTSGNTGIGLAM 82
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 83 IAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEEL--SAEHGYFLpQQFTNPANAVIHRLTTGP 160
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEIlkNTPDAYML-QQFDNPANPKIHYETTGP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 161 EIVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGGQPGPHKIQGIGAGFVPTVLDTEIYSS 240
Cdd:PLN03013 272 EIWDDTKG-KVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126589967 241 VFPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIV-PSNGeRYLSTPLYQ 306
Cdd:PLN03013 351 VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSlFASG-RDIYTPRCS 416
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
4-301 |
8.73e-87 |
|
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 267.44 E-value: 8.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 4 LANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMI 83
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 84 AAAKGYKAILVMPETMSLERRNLLRAYGAELVLTP---GPAGMKGAIAKAEELSAE-HGYFLPQQFTNPANAVIHRLTTG 159
Cdd:TIGR01137 81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPtaaAFDSPESHIGVAKRLVREiPGAHILDQYRNPSNPLAHYDTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 160 PEIVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSpVLSGGQP------GPHKIQGIGAGFVPTVL 233
Cdd:TIGR01137 161 PEILEQCEG-KLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126589967 234 DTEIYSSVFPVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGK-GSNVLAIVPSNGERYLS 301
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQeGQRCVVLLPDSIRNYMT 307
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
8-302 |
1.85e-76 |
|
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274872 [Multi-domain] Cd Length: 304 Bit Score: 235.94 E-value: 1.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 8 IAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMIAAAK 87
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 88 GYKAILVMPETMSLERRNLLRAYGA--ELVLTPGPAG--MKGAIAKAEELSAE-HGYFLPQQFTNPANAVIHRLTTGPEI 162
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAevEKVTEPDETGgyLGTRIARVRELLASiPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 163 VEAFDglTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSpVLSGGQPGPHKIQGIGAGFVPTVLDTEIYSSVF 242
Cdd:TIGR03945 161 ARAFP--TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGS-VIFGGPPGRRHIPGLGASVVPELLDESLIDDVV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 243 PVENEVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIVPSNGERYLST 302
Cdd:TIGR03945 238 HVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDT 297
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
7-305 |
7.33e-75 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 231.34 E-value: 7.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 7 SIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGLAMIAAA 86
Cdd:TIGR01138 1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 87 KGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKAEELSAEHGYFLPQQFTNPANAVIHRLTTGPEIVEAF 166
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 167 DGlTLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGgqpgphkIQGIGAGFVPTVLDTEIYSSVFPVEN 246
Cdd:TIGR01138 161 GG-RITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 126589967 247 EVAFEVARKVAREEGILCGISSGAAIYAAIEAAKRLGKGSnVLAIVPSNGERYLSTPLY 305
Cdd:TIGR01138 233 RDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLSTGVF 290
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-293 |
3.17e-68 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 212.76 E-value: 3.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 15 TPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLqPGGTIIEPTSGNTGIGLAMIAAAKGYKAILV 94
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 95 MPETMSLERRNLLRAYGAELVLTPGpaGMKGAIAKAEELSAE-HGYFLPQQFTNPANAVIHRlTTGPEIVEAFDGLTLDA 173
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGQKPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 174 FVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKdspvlsggqpgphkiqgigagfvptvldteiyssVFPVENEVAFEVA 253
Cdd:cd00640 157 VVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------VVTVSDEEALEAI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 126589967 254 RKVAREEGILCGISSGAAIYAAIEAAKRLGKGSNVLAIVP 293
Cdd:cd00640 203 RLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILT 242
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
8-293 |
6.52e-62 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 198.30 E-value: 6.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 8 IAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKdgtLQPGGTIIEPTSGNTGIGLAMIAAAK 87
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 88 GYKAILVMPETMSLERRNLLRAYGAELVLTPGpaGMKGAIAKAEELSAE-HGYFLPQQFTNPANAVIHRlTTGPEIVEAF 166
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 167 DGLtLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSPVLSGG---------QPGPHKIQGIGAGFVPTVLDTEI 237
Cdd:pfam00291 155 GGD-PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126589967 238 Y----SSVFPVENEVAFEVARKVAREEGILCGISSGAA-IYAAIEAAKRLGKGSNVLAIVP 293
Cdd:pfam00291 234 LdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAlAALKLALAGELKGGDRVVVVLT 294
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-301 |
2.34e-28 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 113.16 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 1 MSRLANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGGTIIEPTSGNTGIGL 80
Cdd:PLN02356 40 KKKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 81 AMIAAAKGYKAILVMPETMSLERRNLLRAYGAElVLTPGPAGMKGA-----IAK-----AEELSAEH------------- 137
Cdd:PLN02356 120 ATVAPAYGCKCHVVIPDDVAIEKSQILEALGAT-VERVRPVSITHKdhyvnIARrraleANELASKRrkgsetdgihlek 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 138 --------------------GYFLPQQFTNPANAVIHRLTTGPEIVEAFDGlTLDAFVAGVGTGGTITGAGAVLKEKYPN 197
Cdd:PLN02356 199 tngciseeekenslfsssctGGFFADQFENLANFRAHYEGTGPEIWEQTQG-NLDAFVAAAGTGGTLAGVSRFLQEKNPN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 198 VEIIAVEPKDSPVLSG-----------------GQPGPHKIQGIGAGFVPTVLDTEIYSSVFPVENEVAFEVARKVAREE 260
Cdd:PLN02356 278 IKCFLIDPPGSGLFNKvtrgvmytreeaegrrlKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKND 357
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 126589967 261 GILCGISSGAAIYAAIEAAKRLGKGSNVLAIVPSNGERYLS 301
Cdd:PLN02356 358 GLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
5-209 |
4.61e-16 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 77.14 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 5 ANSIAELVGKTPIVKlNHATSENEGT-VYVKLEYFNPGSSVKDRLALAMIEAAEKDGtlQPGGtIIEPTSGNTGIGLAMI 83
Cdd:cd01562 8 AARIKPVVRRTPLLT-SPTLSELLGAeVYLKCENLQKTGSFKIRGAYNKLLSLSEEE--RAKG-VVAASAGNHAQGVAYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 84 AAAKGYKAILVMPETMSLERRNLLRAYGAELVLTpgPAGMKGAIAKAEELSAEHGYFLPQQFTNPanAVIHRL-TTGPEI 162
Cdd:cd01562 84 AKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLTFIHPFDDP--DVIAGQgTIGLEI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126589967 163 VEAFDGltLDAFVAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSP 209
Cdd:cd01562 160 LEQVPD--LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAP 204
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
12-175 |
1.30e-15 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 76.39 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 12 VGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLqpggTIIEPTSGNTGIGLAMIAAAKGYKA 91
Cdd:COG0498 64 EGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 92 ILVMPET-MSLERRNLLRAYGAELVLTPGPAGmkGAIAKAEELSAEHGYFLpqqftnpANAV-IHRL----TTGPEIVEA 165
Cdd:COG0498 140 FVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFD--DAQRLVKELAADEGLYA-------VNSInPARLegqkTYAFEIAEQ 210
|
170
....*....|
gi 126589967 166 FDGLtLDAFV 175
Cdd:COG0498 211 LGRV-PDWVV 219
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
13-175 |
3.96e-14 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 71.47 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 13 GKTPIVKL-NHATSENEGTVYVKLEYFNPGSSVKDR-LALAMIEAAEKDGTlqpggTIIEPTSGNTGIGLAMIAAAKGYK 90
Cdd:cd01563 21 GNTPLVRApRLGERLGGKNLYVKDEGLNPTGSFKDRgMTVAVSKAKELGVK-----AVACASTGNTSASLAAYAARAGIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 91 AILVMPETMSLERRNLLRAYGAELVLTPGpaGMKGAIAKAEELSAEHGYFLpQQFTNPanaviHRL----TTGPEIVEAF 166
Cdd:cd01563 96 CVVFLPAGKALGKLAQALAYGATVLAVEG--NFDDALRLVRELAEENWIYL-SNSLNP-----YRLegqkTIAFEIAEQL 167
|
....*....
gi 126589967 167 DGLTLDAFV 175
Cdd:cd01563 168 GWEVPDYVV 176
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
8-209 |
4.34e-14 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 71.61 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 8 IAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDgtlQPGGTIIEPTSGNTGIGLAMIAAAK 87
Cdd:COG1171 18 IAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEE---ERARGVVAASAGNHAQGVAYAARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 88 GYKAILVMPETMSLERRNLLRAYGAELVLTPGpaGMKGAIAKAEELSAEHGYFLPQQFTNPanAVIH-RLTTGPEIVEAF 166
Cdd:COG1171 95 GIPATIVMPETAPAVKVAATRAYGAEVVLHGD--TYDDAEAAAAELAEEEGATFVHPFDDP--DVIAgQGTIALEILEQL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126589967 167 DGltLDAFVagvgtggtitgagaV--------------LKEKYPNVEIIAVEPKDSP 209
Cdd:COG1171 171 PD--LDAVF--------------VpvggggliagvaaaLKALSPDIRVIGVEPEGAA 211
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
15-209 |
1.59e-11 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 64.38 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 15 TPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTlQPGgtIIEPTSGNTGIGLAMIAAAKGYKAILV 94
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQR-QRG--VVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 95 MPETMSLERRNLLRAYGAELVLTpgPAGMKGAIAKAEELSAEHGYFLPQQFTNPaNAVIHRLTTGPEIVEafDGLTLDAF 174
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILH--GDDYDEAYAFATSLAEEEGRVFVHPFDDE-FVMAGQGTIGLEIME--DIPDVDTV 152
|
170 180 190
....*....|....*....|....*....|....*
gi 126589967 175 VAGVGTGGTITGAGAVLKEKYPNVEIIAVEPKDSP 209
Cdd:TIGR01127 153 IVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAP 187
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
31-211 |
1.97e-11 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 63.56 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 31 VYVKLEYFNPGSSVKDRLA----LAMIEAAEKDGtlqpggtIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRNL 106
Cdd:PRK06815 37 VYLKCEHLQHTGSFKFRGAsnklRLLNEAQRQQG-------VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 107 LRAYGAELVLTPGPagMKGAIAKAEELSAEHGyfLPqqFTNPAN--AVIH-RLTTGPEIVEAFDGLtlDAFVAGVGTGGT 183
Cdd:PRK06815 110 IRALGAEVRLYGGD--ALNAELAARRAAEQQG--KV--YISPYNdpQVIAgQGTIGMELVEQQPDL--DAVFVAVGGGGL 181
|
170 180
....*....|....*....|....*...
gi 126589967 184 ITGAGAVLKEKYPNVEIIAVEPKDSPVL 211
Cdd:PRK06815 182 ISGIATYLKTLSPKTEIIGCWPANSPSL 209
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
13-140 |
2.22e-10 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 60.52 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 13 GKTPIVKlnhatsenEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTlqpgGTIIEPTSGNTGIGLAMIAAAKGYKAI 92
Cdd:PRK06450 57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 126589967 93 LVMPETMSLERRNLLRAYGAELVLTpgpAGMKGAIAKAEElsaEHGYF 140
Cdd:PRK06450 125 IFVPETASGGKLKQIESYGAEVVRV---RGSREDVAKAAE---NSGYY 166
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
1-140 |
2.61e-10 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 60.49 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 1 MSRLANSIAELVGKTPIVKLNHATSE-NEGTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTlqpgGTIIEPTSGNTGIG 79
Cdd:PRK06381 2 EEELSSSEEKPPGGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGAS 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126589967 80 LAMIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPagMKGAIAKAEELSAEHGYF 140
Cdd:PRK06381 78 IAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGK--YEEAVERSRKFAKENGIY 136
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
2-137 |
1.39e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 58.04 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 2 SRLANSIAELVGKTPIVKLNhATSENEGTVYVKLEYFNPGSSVKDRLALAMIEAAEkdgtlQPGGTIIEPTSGNTGIGLA 81
Cdd:PRK08246 11 RAAAQRIAPHIRRTPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 126589967 82 MIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPgpagmkGAIAKAEELSAEH 137
Cdd:PRK08246 85 YAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVG------AEYADALEAAQAF 134
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
7-138 |
6.86e-09 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 56.28 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 7 SIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDRLA---LAMIEAAEKdgtlQPGgtIIEPTSGNTGIGLAMI 83
Cdd:PRK08638 20 RLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEK----RKG--VVACSAGNHAQGVALS 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 126589967 84 AAAKGYKAILVMPETMSLERRNLLRAYGAELVLTpgPAGMKGAIAKAEELSAEHG 138
Cdd:PRK08638 94 CALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEEG 146
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
6-142 |
4.58e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 53.62 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 6 NSIAELVGKTPIVklnHATSENEGT---VYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPggTIIEPTSGNTGIGLAM 82
Cdd:PRK06608 15 NRIKQYLHLTPIV---HSESLNEMLgheIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAY 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 83 IAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAgmkGAIAKAEELSAEHGYFLP 142
Cdd:PRK06608 90 ASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQ---EAEEKAKEDEEQGFYYIH 146
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
31-208 |
1.14e-07 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 52.88 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 31 VYVKLEYFNPGSSVKDRLA---LAMIEAAEkdgtLQPGgtIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRNLL 107
Cdd:PRK12483 54 VLLKREDLQPVFSFKIRGAynkMARLPAEQ----LARG--VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 108 RAYGAELVLTpgPAGMKGAIAKAEELSAEHGYFLPQQFTNPaNAVIHRLTTGPEIVEAFDGlTLDAFVAGVGTGGTITGA 187
Cdd:PRK12483 128 RAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPPFDDP-DVIAGQGTVAMEILRQHPG-PLDAIFVPVGGGGLIAGI 203
|
170 180
....*....|....*....|.
gi 126589967 188 GAVLKEKYPNVEIIAVEPKDS 208
Cdd:PRK12483 204 AAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
13-140 |
1.22e-07 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 52.70 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 13 GKTPIVKL-NHATSENEGTVYVKLEYFNPGSSVKDR-LALAMIEAAEKDGTlqpggTIIEPTSGNTGIGLAMIAAAKGYK 90
Cdd:PRK08197 78 GMTPLLPLpRLGKALGIGRLWVKDEGLNPTGSFKARgLAVGVSRAKELGVK-----HLAMPTNGNAGAAWAAYAARAGIR 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 126589967 91 AILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKaeELSAEHGYF 140
Cdd:PRK08197 153 ATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVA--EAVAEYGWF 200
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
30-211 |
4.63e-07 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 50.91 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 30 TVYVKLEYFNPGSSVKDRLALAMI----EAAEKDGtlqpggtIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRN 105
Cdd:PRK09224 36 QVLLKREDLQPVFSFKLRGAYNKMaqltEEQLARG-------VITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 106 LLRAYGAELVLtpgpagmKG-----AIAKAEELSAEHGY-FLPQqFTNPAnaVIH-RLTTGPEIVEAFDGLtLDA-FVAg 177
Cdd:PRK09224 109 AVRAFGGEVVL-------HGdsfdeAYAHAIELAEEEGLtFIHP-FDDPD--VIAgQGTIAMEILQQHPHP-LDAvFVP- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126589967 178 vgtggtitgagaV------------LKEKYPNVEIIAVEPKDSPVL 211
Cdd:PRK09224 177 ------------VggggliagvaayIKQLRPEIKVIGVEPEDSACL 210
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
15-114 |
5.68e-07 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 50.21 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 15 TPIVKLNHatsenegTVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQpggtIIEPTSGNTGIGLAMIAAAKGYKAILV 94
Cdd:PRK08329 65 TPTVKRSI-------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINE----VVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100
....*....|....*....|
gi 126589967 95 MPETMSLERRNLLRAYGAEL 114
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAEL 153
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
30-115 |
7.77e-07 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 49.99 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 30 TVYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPGgtIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRNLLRA 109
Cdd:PRK06110 37 EVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRA 114
|
....*.
gi 126589967 110 YGAELV 115
Cdd:PRK06110 115 LGAELI 120
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
13-165 |
2.29e-06 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 48.53 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 13 GKTPIVKlNHATSENEGT--VYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLqpggTIIEPTSGNTGIGLAMIAAAKGYK 90
Cdd:TIGR00260 21 GVTPLFR-APALAANVGIknLYVKELGHNPTLSFKDRGMAVALTKALELGND----TVLCASTGNTGAAAAAYAGKAGLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 91 AILVMPE-TMSLERRNLLRAYGAELVltpgpaGMKGAIAKAEELSAEHGYFLPQQFTNPANAVIHRL----TTGPEIVEA 165
Cdd:TIGR00260 96 VVVLYPAgKISLGKLAQALGYNAEVV------AIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLegqkTYAFEAVEQ 169
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
54-143 |
1.82e-05 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 45.64 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 54 EAAEKDGTLqpggTIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGpaGMKGAIAKAEEL 133
Cdd:PRK08206 109 EVREKLGDI----TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDG--NYDDSVRLAAQE 182
|
90
....*....|
gi 126589967 134 SAEHGYFLPQ 143
Cdd:PRK08206 183 AQENGWVVVQ 192
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
13-140 |
2.88e-05 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 45.19 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 13 GKTPIVKLNHATSENEgTVYVKLEYFNPGSSVKDRLALAMIEaaekDGTLQPGGTIIEPTSGNTGIGLAMIAAAKGYKAI 92
Cdd:PRK05638 65 GGTPLIRARISEKLGE-NVYIKDETRNPTGSFRDRLATVAVS----YGLPYAANGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 126589967 93 LVMPETMSLERRNLLRAYGAELVLTpgPAGMKGAIAKAEELSAEHGYF 140
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLNGLY 185
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
31-208 |
1.48e-04 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 43.37 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 31 VYVKLEYFNPGSSVKDRLALAMIEAAEKDgTLQPGgtIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRNLLRAY 110
Cdd:PLN02550 126 VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 111 GAELVLTPGpaGMKGAIAKAEELSAEHGYFLPQQFTNPaNAVIHRLTTGPEIVEAFDGlTLDAFVAGVGTGGTITGAGAV 190
Cdd:PLN02550 203 GATVVLVGD--SYDEAQAYAKQRALEEGRTFIPPFDHP-DVIAGQGTVGMEIVRQHQG-PLHAIFVPVGGGGLIAGIAAY 278
|
170
....*....|....*...
gi 126589967 191 LKEKYPNVEIIAVEPKDS 208
Cdd:PLN02550 279 VKRVRPEVKIIGVEPSDA 296
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
60-117 |
8.81e-04 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 40.28 E-value: 8.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126589967 60 GTLQPGGTIIEpTSGNTGIGLAMI--AAAKGYKAILVMPETMSLER-RNLLRAYGAELVLT 117
Cdd:cd08290 142 VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
14-135 |
1.72e-03 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 39.59 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 14 KTPIVKlNHATSENEGT-VYVKLEYFNPGSSVKDR-LALAMIEAAEKDGTLQPGgtIIEPTSGNTGIGLAMIAAAKGYKA 91
Cdd:cd06448 1 KTPLIE-STALSKTAGCnVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 126589967 92 ILVMPETMSLERRNLLRAYGAELVLTpGPAGMKGAIAKAEELSA 135
Cdd:cd06448 78 TIVVPESTKPRVVEKLRDEGATVVVH-GKVWWEADNYLREELAE 120
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
31-162 |
4.87e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 38.07 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 31 VYVKLEYFNPGSSVKDRLALAMIEAAEKDGTLQPggtIIEPTSGNTGIGLAMIAAAKGYKAILVMPETMSLERRNLLRAY 110
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHW 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 126589967 111 GAElVLTPGPAgMKGAIAKAEELSAEHGYFLPQQFTNPaNAVIHRLTTGPEI 162
Cdd:PRK08813 127 GAT-VRQHGNS-YDEAYAFARELADQNGYRFLSAFDDP-DVIAGQGTVGIEL 175
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
5-138 |
7.14e-03 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 37.69 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126589967 5 ANSIAELVGKTPIVKLNHATSENEGTVYVKLEYFNPGSSVKDR---LALAMIEAAEKdgtlQPGgtIIEPTSGNTGIGLA 81
Cdd:PRK07048 15 AARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIA 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 126589967 82 MIAAAKGYKAILVMPETMSLERRNLLRAYGAELVLTPGPAGMKGAIAKaeELSAEHG 138
Cdd:PRK07048 89 LSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGR--RLAEERG 143
|
|
| |
