|
Name |
Accession |
Description |
Interval |
E-value |
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
3-305 |
1.47e-172 |
|
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: 479.93 E-value: 1.47e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAIqsvGGTLDAFVAgigtggtitgtgEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:COG0031 162 IWEQT---DGKVDAFVAgvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLID 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLST 305
Cdd:COG0031 239 EVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
8-308 |
2.52e-168 |
|
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: 469.15 E-value: 2.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIvPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01139 1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENP-SYFMAEQFKNKANVKIHRETTGPEIVEA 166
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnSYFMLQQFENPANPEIHRKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 167 IqsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIH 246
Cdd:TIGR01139 160 T---DGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVIT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 247 IENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01139 237 VSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
8-308 |
8.88e-160 |
|
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: 447.50 E-value: 8.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIVEAI 167
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 qsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIHI 247
Cdd:TIGR01136 161 ---DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 248 ENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLG-AGKRVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01136 238 SDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
13-304 |
2.30e-153 |
|
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: 430.78 E-value: 2.30e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 93 IVMPETMSMERRNLLRAYGAELVLTPGAE--GMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIVEAIqsv 170
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 171 GGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIHIEND 250
Cdd:cd01561 158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1011417748 251 DAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLS 304
Cdd:cd01561 238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
3-309 |
2.32e-114 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 333.37 E-value: 2.32e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:PRK10717 2 KIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGA------EGMNGAVKKAEELLKENPS-YFMAEQFKNKANVKIH 155
Cdd:PRK10717 82 VAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNgAIWANQFDNPANREAH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 156 RETTGPEIveaIQSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPI----LAG--GKPGPHKIQGIGA 229
Cdd:PRK10717 162 YETTGPEI---WEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEGIGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 230 NFIPEILDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTpLYN 309
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK-LFN 317
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
4-309 |
1.54e-112 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 328.81 E-value: 1.54e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 4 VVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTI-IEATSGNTGIGLAM 82
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:PLN02565 85 MAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAiqsVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:PLN02565 165 IWKG---TGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ-LGAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PLN02565 242 EVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-308 |
4.05e-101 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 303.24 E-value: 4.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 4 VVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTI-IEATSGNTGIGLAM 82
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGPE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAIQsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:PLN03013 273 IWDDTK---GKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMD 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ-LGAGKRVVVIVPSNGeRYLSTPLY 308
Cdd:PLN03013 350 EVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRpENAGKLIAVSLFASG-RDIYTPRC 415
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
6-309 |
1.92e-100 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 298.07 E-value: 1.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 6 NNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPG-DTIIEATSGNTGIGLAMVA 84
Cdd:PLN00011 9 NDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 85 AAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIv 164
Cdd:PLN00011 89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPEI- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 165 eaIQSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEI 244
Cdd:PLN00011 168 --WRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEI 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011417748 245 IHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ-LGAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PLN00011 246 IQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVIFPSGGERYLSTKLFE 311
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
10-309 |
1.18e-97 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 289.85 E-value: 1.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 10 ELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGY 89
Cdd:PRK11761 8 DTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 90 KSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENpSYFMAEQFKNKANVKIHRETTGPEIveaIQS 169
Cdd:PRK11761 88 RMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEG-EGKVLDQFANPDNPLAHYETTGPEI---WRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 170 VGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPA-ASPIlaggkPGphkIQGIGANFIPEILDQEIYDEIIHIE 248
Cdd:PRK11761 164 TEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEeGSSI-----PG---IRRWPEEYLPKIFDASRVDRVLDVS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011417748 249 NDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLgAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PRK11761 236 QQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLSTGVFP 295
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
3-309 |
9.30e-97 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 289.94 E-value: 9.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDT-IIEATSGNTGIGLA 81
Cdd:PLN02556 48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 82 MVAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGP 161
Cdd:PLN02556 128 FMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 162 EIVEaiqSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIY 241
Cdd:PLN02556 208 EIWE---DTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVM 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011417748 242 DEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQL-GAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PLN02556 285 EKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPeNKGKLIVTVHPSFGERYLSSVLFQ 353
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
7-304 |
1.44e-93 |
|
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: 284.77 E-value: 1.44e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 7 NVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAA 86
Cdd:TIGR01137 4 NILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 87 KGYKSVIVMPETMSMERRNLLRAYGAELVLTPGA---EGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEI 163
Cdd:TIGR01137 84 KGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAaafDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 164 VEAIQsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASpILAGGKP------GPHKIQGIGANFIPEILD 237
Cdd:TIGR01137 164 LEQCE---GKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVLD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011417748 238 QEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGA-GKRVVVIVPSNGERYLS 304
Cdd:TIGR01137 240 RKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQeGQRCVVLLPDSIRNYMT 307
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
8-308 |
9.00e-87 |
|
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: 261.77 E-value: 9.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMaEQFKNKANVKIHRETTGPEIveaI 167
Cdd:TIGR01138 82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEI---W 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 QSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGgkpgphkIQGIGANFIPEILDQEIYDEIIHI 247
Cdd:TIGR01138 158 QQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011417748 248 ENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKrVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01138 231 HQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLSTGVF 290
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
8-309 |
1.16e-84 |
|
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: 256.75 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 88 GYKSVIVMPETMSMERRNLLRAYGA--ELVLTPGAEG--MNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEI 163
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAevEKVTEPDETGgyLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 164 VEAIqsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILaGGKPGPHKIQGIGANFIPEILDQEIYDE 243
Cdd:TIGR03945 161 ARAF----PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIF-GGPPGRRHIPGLGASVVPELLDESLIDD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011417748 244 IIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTpLYN 309
Cdd:TIGR03945 236 VVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDT-VYN 300
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
15-296 |
1.17e-73 |
|
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: 226.63 E-value: 1.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLkPGDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 95 MPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHReTTGPEIVEaiQSVGGTL 174
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILE--QLGGQKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 175 DAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPaaspilaggkpgphkiqgiganfipeildqeiydEIIHIENDDAFE 254
Cdd:cd00640 155 DAVVVPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------EVVTVSDEEALE 200
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1011417748 255 TARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVP 296
Cdd:cd00640 201 AIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILT 242
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
8-296 |
2.07e-71 |
|
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: 222.96 E-value: 2.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEgklKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHrETTGPEIVEAI 167
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY-GTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 qsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGG---------KPGPHKIQGIGANFIPEILDQ 238
Cdd:pfam00291 155 ---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALAL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 239 EIY----DEIIHIENDDAFETARQVAKEEGILSGISSGAAIRA-GLQVAKQLGAGKRVVVIVP 296
Cdd:pfam00291 232 DLLdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAlKLALAGELKGGDRVVVVLT 294
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
1-304 |
9.52e-43 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 152.07 E-value: 9.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 1 MAKVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGL 80
Cdd:PLN02356 40 KKKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 81 AMVAAAKGYKSVIVMPETMSMERRNLLRAYGA----------------------------ELVLTPG-AEGMNGAVKKA- 130
Cdd:PLN02356 120 ATVAPAYGCKCHVVIPDDVAIEKSQILEALGAtvervrpvsithkdhyvniarrraleanELASKRRkGSETDGIHLEKt 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 131 ----EELLKENPSY-------FMAEQFKNKANVKIHRETTGPEIVEaiqSVGGTLDAFVAGIGTGGTITGTGEVLKESFP 199
Cdd:PLN02356 200 ngciSEEEKENSLFsssctggFFADQFENLANFRAHYEGTGPEIWE---QTQGNLDAFVAAAGTGGTLAGVSRFLQEKNP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 200 GIKIVAVEPAASPIL-------------AGGK----PGPHKIQGIGANFIPEILDQEIYDEIIHIENDDAFETARQVAKE 262
Cdd:PLN02356 277 NIKCFLIDPPGSGLFnkvtrgvmytreeAEGRrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKN 356
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1011417748 263 EGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLS 304
Cdd:PLN02356 357 DGLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
15-295 |
1.50e-19 |
|
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: 87.01 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDR---IAISIVEEAEKEGklkpgdTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRgayNALASLSEEERAR------GVVAASAGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 92 VIVMPETMSMERRNLLRAYGAELVLTPG--AEgmngAVKKAEELLKE---------NPSYFMAEQfknkanvkihrETTG 160
Cdd:COG1171 99 TIVMPETAPAVKVAATRAYGAEVVLHGDtyDD----AEAAAAELAEEegatfvhpfDDPDVIAGQ-----------GTIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 161 PEIVEAIQSV--------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVEPAASP-------------------I 213
Cdd:COG1171 164 LEILEQLPDLdavfvpvgGGGLIAGVAA------------ALKALSPDIRVIGVEPEGAAamyrslaagepvtlpgvdtI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 214 ---LAGGKPGPHkiqgigaNFipEILdQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIrAGLQVAKQLGAGKR 290
Cdd:COG1171 232 adgLAVGRPGEL-------TF--EIL-RDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL-AALLAGKERLKGKR 300
|
....*
gi 1011417748 291 VVVIV 295
Cdd:COG1171 301 VVVVL 305
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
13-299 |
6.38e-18 |
|
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: 83.33 E-value: 6.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGA----KTIVCASSGNGSAALAAYAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 93 IVMPET-MSMERRNLLRAYGAELVLTPGaegmN--GAVKKAEELLKENPSYFmaeqfknkANVkIH---RE---TTGPEI 163
Cdd:COG0498 141 VFVPEGkVSPGQLAQMLTYGAHVIAVDG----NfdDAQRLVKELAADEGLYA--------VNS-INparLEgqkTYAFEI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 164 VEAIQSV-----------GGTLDAFVAGIGTGGTItgtgevLKESFPgiKIVAVEPA-ASPIL---AGGKPGPHKIQG-- 226
Cdd:COG0498 208 AEQLGRVpdwvvvptgngGNILAGYKAFKELKELG------LIDRLP--RLIAVQATgCNPILtafETGRDEYEPERPet 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 227 ------IG--ANFiPEILDqEIYD---EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ--LGAGKRVVV 293
Cdd:COG0498 280 iapsmdIGnpSNG-ERALF-ALREsggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVV 357
|
....*.
gi 1011417748 294 IVPSNG 299
Cdd:COG0498 358 LSTGHG 363
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
15-295 |
1.10e-17 |
|
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: 81.76 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIA----ISIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAAAKGYK 90
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAynklLSLSEEERAKG-------VVAASAGNHAQGVAYAAKLLGIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 91 SVIVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKEN-----PSYF----MAEQfknkanvkihrETTGP 161
Cdd:cd01562 91 ATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEgltfiHPFDdpdvIAGQ-----------GTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 162 EIVEAIQSV--------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVEPAASPI----LAGGKPGPHKIQG--- 226
Cdd:cd01562 158 EILEQVPDLdavfvpvgGGGLIAGIAT------------AVKALSPNTKVIGVEPEGAPAmaqsLAAGKPVTLPEVDtia 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 227 -------IGANFiPEILdQEIYDEIIHIEND-------DAFETARQVAkeEGilsgiSSGAAIRAGLQVAKQLgAGKRVV 292
Cdd:cd01562 226 dglavkrPGELT-FEII-RKLVDDVVTVSEDeiaaamlLLFEREKLVA--EP-----AGALALAALLSGKLDL-KGKKVV 295
|
...
gi 1011417748 293 VIV 295
Cdd:cd01562 296 VVL 298
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
13-141 |
2.64e-16 |
|
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: 78.02 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:cd01563 21 GNTPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1011417748 92 VIVMPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYF 141
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEG--NFDDALRLVRELAEENWIYL 144
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
13-120 |
2.97e-14 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 72.05 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:PRK06381 14 GGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
|
90 100
....*....|....*....|....*....
gi 1011417748 92 VIVMPETMSMERRNLLRAYGAELVLTPGA 120
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGK 118
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
8-299 |
1.06e-11 |
|
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: 64.71 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAA 86
Cdd:TIGR00260 16 VDLGEGVTPLFRAPALAANvGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 87 KGYKSVIVMPE-TMSMERRNLLRAYGAELVltpgaeGMNG----AVKKAEELLKENPSYFMaeqfkNKANVKIHR----E 157
Cdd:TIGR00260 92 AGLKVVVLYPAgKISLGKLAQALGYNAEVV------AIDGnfddAQRLVKQLFEDKPALGL-----NSANSIPYRlegqK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 158 TTGPEIVEAIQ---------SVG--GTLDAFVAgigtggTITGTGEVLKESFPgIKIVAVEPAASPI----LAGGKPGPH 222
Cdd:TIGR00260 161 TYAFEAVEQLGweapdkvvvPVPnsGNFGAIWK------GFKEKKMLGLDSLP-VKRGIQAEGAADIvrafLEGGQWEPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 223 KIQ---------GIGANFIPEILDQEIYDEIIHIENDDA-FETARQVAKEEGILSGISSGAAIRAGL-QVAK-QLGAGKR 290
Cdd:TIGR00260 234 ETPetlstamdiGNPANWPRALEAFRRSNGYAEDLSDEEiLEAIKLLAREEGYFVEPHSAVAVAALLkLVEKgTADPAER 313
|
....*....
gi 1011417748 291 VVVIVPSNG 299
Cdd:TIGR00260 314 VVCALTGNG 322
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
1-132 |
2.05e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 63.64 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 1 MAKVVNNVTELIGGTPLVR---LNRIVpegSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKpgDTIIEATSGNTG 77
Cdd:PRK06608 10 IAAAHNRIKQYLHLTPIVHsesLNEML---GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLP--DKIVAYSTGNHG 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1011417748 78 IGLAMVAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEE 132
Cdd:PRK06608 85 QAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEE 139
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
15-295 |
6.30e-11 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 62.02 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIA----ISIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAAAKGYK 90
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnklRLLNEAQRQQG-------VITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 91 SVIVMPETMSMERRNLLRAYGAELVLTPG----AEgMNGAVKKAEELLKENPSYfmaeqfkNKANVKIHRETTGPEIVEA 166
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLYGGdalnAE-LAARRAAEQQGKVYISPY-------NDPQVIAGQGTIGMELVEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 167 IqsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPI----LAGGKPGPHKIQ---------GIGANFIP 233
Cdd:PRK06815 166 Q----PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSlytsLEAGEIVEVAEQptlsdgtagGVEPGAIT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 234 EILDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLgAGKRVVVIV 295
Cdd:PRK06815 242 FPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY-QGKKVAVVL 302
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
15-207 |
1.06e-10 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 61.68 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIA---ISIVEEAEKEgklkpgDTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKR------KGVVACSAGNHAQGVALSCALLGIDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 92 VIVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSYFMAEQfkNKANVKIHRETTGPEIVEAIQSV- 170
Cdd:PRK08638 102 KVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEEGRTFIPPY--DDPKVIAGQGTIGLEILEDLWDVd 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1011417748 171 -------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVE 207
Cdd:PRK08638 178 tvivpigGGGLIAGIAV------------ALKSINPTIHIIGVQ 209
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
13-119 |
1.33e-10 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 61.56 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDR---IAISIVEEAEKEGKLKPgdtiieaTSGNTGIGLAMVAAAKG 88
Cdd:PRK08197 78 GMTPLLPLPRLGKAlGIGRLWVKDEGLNPTGSFKARglaVGVSRAKELGVKHLAMP-------TNGNAGAAWAAYAARAG 150
|
90 100 110
....*....|....*....|....*....|.
gi 1011417748 89 YKSVIVMPETMSMERRNLLRAYGAELVLTPG 119
Cdd:PRK08197 151 IRATIFMPADAPEITRLECALAGAELYLVDG 181
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
13-299 |
4.10e-10 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 60.21 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRlNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 93 IVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSY-------FMAEQFKNKANVKIHrETTGPEIVE 165
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLNGLYnvtpeynIIGLEGQKTIAFELW-EEINPTHVI 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 166 AIQSVGGTLDAFVagigtggtiTGTGEVLK----ESFPgiKIVAVE-----PAASPILAGGK-------PGPHKIQGIGA 229
Cdd:PRK05638 217 VPTGSGSYLYSIY---------KGFKELLEigviEEIP--KLIAVQtercnPIASEILGNKTkcnetkaLGLYVKNPVMK 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 230 NFIPEILDQeiYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ--LGAGKRVVVIVPSNG 299
Cdd:PRK05638 286 EYVSEAIKE--SGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGSG 355
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
15-295 |
5.94e-10 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 59.20 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPeGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKegklkPGDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:PRK08246 24 TPVLEADGAGF-GPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 95 MPETMSMERRNLLRAYGAELVLTPG--AEGMNGAVKKAEEllkenpSYFMAEQFKNKANVKIHRETTGPEIVEAIQSV-- 170
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE------TGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVdt 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 171 ------GGTLDAFVAGIGtggtitgtgevlkesFPGIKIVAVEPAASPIL----AGGKPGPHKIQGI-----GANFIPEI 235
Cdd:PRK08246 172 vlvavgGGGLIAGIAAWF---------------EGRARVVAVEPEGAPTLhaalAAGEPVDVPVSGIaadslGARRVGEI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 236 LDQ--EIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQV-AKQLGAGKRVVVIV 295
Cdd:PRK08246 237 AFAlaRAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSgAYVPAPGERVAVVL 299
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
15-295 |
6.08e-10 |
|
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: 59.37 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKpgdTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQR---GVVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 95 MPETMSMERRNLLRAYGAELVLtpgaEGMN--GAVKKAEELLKENPSYFMaEQFkNKANVKIHRETTGPEIVEAIqsvgG 172
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVIL----HGDDydEAYAFATSLAEEEGRVFV-HPF-DDEFVMAGQGTIGLEIMEDI----P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 173 TLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAG----GKPGPHKI-----QGIGANFIPEI---LDQEI 240
Cdd:TIGR01127 148 DVDTVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYEslreGKIKAVESvrtiaDGIAVKKPGDLtfnIIKEY 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1011417748 241 YDEIIHIeNDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIV 295
Cdd:TIGR01127 228 VDDVVTV-DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVL 281
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
29-115 |
4.05e-09 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 56.93 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 29 AEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGdtIIEATSGNTGIGLAMVAAAKGYKSVIVMPETMSMERRNLLR 108
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113
|
....*..
gi 1011417748 109 AYGAELV 115
Cdd:PRK06110 114 ALGAELI 120
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
13-143 |
3.14e-08 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 54.36 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 13 GGTPLVRLNrivpegsaEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:PRK06450 57 GRTPLIKKG--------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1011417748 93 IVMPETMSMERRNLLRAYGAELVltpGAEGMNGAVKKAeellKENPSYFMA 143
Cdd:PRK06450 125 IFVPETASGGKLKQIESYGAEVV---RVRGSREDVAKA----AENSGYYYA 168
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
15-293 |
4.12e-08 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 54.08 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKpgdTIIEATSGNTGIGLAMVAAAKGYKSVI 93
Cdd:cd06446 35 TPLYRAKRLSEYlGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR---VIAETGAGQHGVATATACALFGLECEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 94 VMPETmSMERRNL----LRAYGAELVltpgaegmngAVKKAEELLKENPSYFMAEQFKNKAN-----------------V 152
Cdd:cd06446 112 YMGAV-DVERQPLnvfrMELLGAEVV----------PVPSGSGTLKDAISEAIRDWVTNVEDthyllgsvvgphpypnmV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 153 KIHRETTGPEIVEAIQSVGGTL-DAFVA-GIGTGGTITGTGEVLKEsfPGIKIVAVEPAASPI--------LAGGKPG-- 220
Cdd:cd06446 181 RDFQSVIGEEAKKQILEKEGELpDVVIAcVGGGSNAAGLFYPFIND--KDVKLIGVEAGGCGLetgghaayLFGGTAGvl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 221 -----------------PHKIQ------GIGanfiPEI--LDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAI 275
Cdd:cd06446 259 hglkmytlqdedgqivpPHSISagldypGVG----PEHayLKDSGRVEYVAVTDEEALEAFKLLARTEGIIPALESSHAI 334
|
330
....*....|....*...
gi 1011417748 276 RAGLQVAKQLGAGKRVVV 293
Cdd:cd06446 335 AYAIKLAKKLGKEKVIVV 352
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
67-137 |
1.06e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 52.57 E-value: 1.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 67 TIIEATSGNTGIGLAMVAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGaegmN--GAVKKAEELLKEN 137
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDG----NydDSVRLAAQEAQEN 186
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
15-114 |
1.50e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 49.05 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLnrivpegSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:PRK08329 65 TPTVKR-------SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100
....*....|....*....|
gi 1011417748 95 MPETMSMERRNLLRAYGAEL 114
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAEL 153
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
60-172 |
7.14e-06 |
|
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: 46.83 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 60 GKLKPGDTIIEaTSGNTGIGLAMV--AAAKGYKSVIVMPETMSMER-RNLLRAYGAELVLTpgaegmngavkkaEEllkE 136
Cdd:cd08290 142 VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT-------------EE---E 204
|
90 100 110
....*....|....*....|....*....|....*.
gi 1011417748 137 NPSYFMAEQFKNKanvkihretTGPEIVEAIQSVGG 172
Cdd:cd08290 205 LRSLLATELLKSA---------PGGRPKLALNCVGG 231
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
15-116 |
2.29e-05 |
|
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: 45.37 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDR-IAISIVEEAEKEGKLKPGdtIIEATSGNTGIGLAMVAAAKGYKSVI 93
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTI 79
|
90 100
....*....|....*....|...
gi 1011417748 94 VMPETMSMERRNLLRAYGAELVL 116
Cdd:cd06448 80 VVPESTKPRVVEKLRDEGATVVV 102
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
15-215 |
4.65e-05 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 44.79 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpGDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQL---ARGVITASAGNHAQGVALAAARLGVKAVIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 95 MPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSYFMAEQfkNKANVKIHRETTGPEIVEAIQsvgGTL 174
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPPF--DDPDVIAGQGTVAMEILRQHP---GPL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1011417748 175 DAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILA 215
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQ 228
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
15-215 |
2.76e-04 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 42.43 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVRLNRIvpegSA----EVFVKLEYQNPGSSVK-----DRIAiSIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAA 85
Cdd:PRK09224 21 TPLEKAPKL----SArlgnQVLLKREDLQPVFSFKlrgayNKMA-QLTEEQLARG-------VITASAGNHAQGVALSAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 86 AKGYKSVIVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSYFmaeqfknkanvkIH---------- 155
Cdd:PRK09224 89 RLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLH--GDSFDEAYAHAIELAEEEGLTF------------IHpfddpdviag 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011417748 156 RETTGPEIVEAIQSV---------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVEPAASPILA 215
Cdd:PRK09224 155 QGTIAMEILQQHPHPldavfvpvgGGGLIAGVAA------------YIKQLRPEIKVIGVEPEDSACLK 211
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
51-130 |
6.34e-04 |
|
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 40.89 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 51 SIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSVIVMpeTMSMERRNLLRAYGAELVLTPGAEGMNGAVKKA 130
Cdd:COG1063 148 AVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVV--DRNPERLELARELGADAVVNPREEDLVEAVREL 225
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
60-121 |
9.03e-04 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally 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. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 40.38 E-value: 9.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 60 GKLKPGDTIieATSGNTGIGLAMVAAAKGYKSVIVMPEtMSMERRNLLRAYGAELVLTPGAE 121
Cdd:cd05188 130 GVLKPGDTV--LVLGAGGVGLLAAQLAKAAGARVIVTD-RSDEKLELAKELGADHVIDYKEE 188
|
|
| Zn_ADH2 |
cd08256 |
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ... |
60-118 |
1.01e-03 |
|
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176218 [Multi-domain] Cd Length: 350 Bit Score: 40.47 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1011417748 60 GKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSVIVMpeTMSMERRNLLRAYGAELVLTP 118
Cdd:cd08256 170 ANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVL--DLKDERLALARKFGADVVLNP 226
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
15-116 |
1.26e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 40.26 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 15 TPLVR---LNRIVpegSAEVFVKLEYQNPGSSVKDRIAI----SIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAAAK 87
Cdd:PRK07334 24 TPCVHsrtLSQIT---GAEVWLKFENLQFTASFKERGALnkllLLTEEERARG-------VIAMSAGNHAQGVAYHAQRL 93
|
90 100
....*....|....*....|....*....
gi 1011417748 88 GYKSVIVMPETMSMERRNLLRAYGAELVL 116
Cdd:PRK07334 94 GIPATIVMPRFTPTVKVERTRGFGAEVVL 122
|
|
| butanediol_DH_like |
cd08233 |
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ... |
56-129 |
1.86e-03 |
|
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.
Pssm-ID: 176195 [Multi-domain] Cd Length: 351 Bit Score: 39.45 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011417748 56 AEKEGKLKPGDTIIEATSGNtgIGLAMVAAAKGYK-SVIVMPEtMSMERRNLLRAYGAELVLTPGAEGMNGAVKK 129
Cdd:cd08233 164 AVRRSGFKPGDTALVLGAGP--IGLLTILALKAAGaSKIIVSE-PSEARRELAEELGATIVLDPTEVDVVAEVRK 235
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
30-215 |
3.65e-03 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 38.75 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 30 EVFVKLEYQNPGSSVKDRIAISIVEEAEKEgKLKPGdtIIEATSGNTGIGLAMVAAAKGYKSVIVMPETMSMERRNLLRA 109
Cdd:PLN02550 125 KVLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVER 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 110 YGAELVLTpgAEGMNGAVKKAEELLKENPSYFMAEqFKNkANVKIHRETTGPEIVEAIQsvgGTLDAFVAGIGTGGTITG 189
Cdd:PLN02550 202 LGATVVLV--GDSYDEAQAYAKQRALEEGRTFIPP-FDH-PDVIAGQGTVGMEIVRQHQ---GPLHAIFVPVGGGGLIAG 274
|
170 180
....*....|....*....|....*.
gi 1011417748 190 TGEVLKESFPGIKIVAVEPAASPILA 215
Cdd:PLN02550 275 IAAYVKRVRPEVKIIGVEPSDANAMA 300
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
8-97 |
3.97e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 38.64 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 8 VTELIGGTPLVRLNRIVPE--GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKL-KPGDTIIEATSGNTGIGLAMVA 84
Cdd:PLN02569 127 VSLFEGNSNLFWAERLGKEflGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYC 206
|
90
....*....|...
gi 1011417748 85 AAKGYKSVIVMPE 97
Cdd:PLN02569 207 AAAGIPSIVFLPA 219
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
196-293 |
4.23e-03 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 38.62 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 196 ESFPGIKIVAVEPAASPILAGG----------KPGP-HKIQGIGANFIPE--------------ILDQEIYDEIIH---I 247
Cdd:PRK12391 280 EGKKDTRFIAVEPAACPTLTKGeyaydfgdtaGLTPlLKMYTLGHDFVPPpihagglryhgmapLVSLLVHEGLIEaraY 359
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1011417748 248 ENDDAFETARQVAKEEGILSGISSGAAIRAGLQVA---KQLGAGKRVVV 293
Cdd:PRK12391 360 PQTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEAlkaKEEGEEKVILF 408
|
|
| quinone_oxidoreductase_like_1 |
cd08243 |
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
61-117 |
7.50e-03 |
|
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.
Pssm-ID: 176205 [Multi-domain] Cd Length: 320 Bit Score: 37.59 E-value: 7.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1011417748 61 KLKPGDTI-IEAtsGNTGIGLAMVAAAKGYKSViVMPETMSMERRNLLRAYGAELVLT 117
Cdd:cd08243 139 GLQPGDTLlIRG--GTSSVGLAALKLAKALGAT-VTATTRSPERAALLKELGADEVVI 193
|
|
|