|
Name |
Accession |
Description |
Interval |
E-value |
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
4-303 |
0e+00 |
|
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: 521.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 4 KPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAF 83
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 84 VCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEH-GYFEPQQFENPANPEVHELTTGPE 162
Cdd:COG0031 82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETpGAFWPNQFENPANPEAHYETTGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 163 LLQQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSI 242
Cdd:COG0031 162 IWEQTDGK-VDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDEV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304357 243 IKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLST 303
Cdd:COG0031 241 ITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
9-306 |
8.84e-179 |
|
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: 495.35 E-value: 8.84e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLrNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAK 88
Cdd:TIGR01139 1 ISELIGNTPLVRL-NRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHG--YFEPQQFENPANPEVHELTTGPELLQQ 166
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnsYFMLQQFENPANPEIHRKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 167 FEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIKVG 246
Cdd:TIGR01139 160 TDGK-LDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 247 NDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLSTPLY 306
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
9-306 |
2.63e-170 |
|
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: 474.08 E-value: 2.63e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAK 88
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEE-HGYFEPQQFENPANPEVHELTTGPELLQQF 167
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 168 EGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIKVGN 247
Cdd:TIGR01136 161 DGR-IDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 248 DTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELG-KGKTVVTVLPSNGERYLSTPLY 306
Cdd:TIGR01136 240 EDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
14-302 |
3.27e-168 |
|
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: 468.15 E-value: 3.27e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 14 GGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAKGYKAV 93
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 94 FTMPETMSQERRNLLKAYGAELVLTPGSEA--MKGAIKKAKELKEEH-GYFEPQQFENPANPEVHELTTGPELLQQFEGK 170
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEAdgMKGAIAKARELAAETpNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 171 tIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIKVGNDTA 250
Cdd:cd01561 161 -VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 579304357 251 MEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLS 302
Cdd:cd01561 240 FAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
7-303 |
2.75e-123 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 356.09 E-value: 2.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCA 86
Cdd:PRK10717 5 EDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 87 AKGYKAVFTMPETMSQERRNLLKAYGAELVLTPG------SEAMKGAIKKAKEL--KEEHGYFEPQQFENPANPEVHELT 158
Cdd:PRK10717 85 ARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAapyanpNNYVKGAGRLAEELvaSEPNGAIWANQFDNPANREAHYET 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 159 TGPELLQQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLS---GGE---PGPHKLQGLGAGFIPG 232
Cdd:PRK10717 165 TGPEIWEQTDGK-VDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyykTGElkaEGSSITEGIGQGRITA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304357 233 TLNTEIYDSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLST 303
Cdd:PRK10717 244 NLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK 314
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
1-306 |
1.52e-115 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 336.13 E-value: 1.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 1 MAQKPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTI-VEPTSGNTGI 79
Cdd:PLN02565 1 EKSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 80 GLAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKEL--KEEHGYFEpQQFENPANPEVHEL 157
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEIlaKTPNSYIL-QQFENPANPKIHYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 158 TTGPELLQQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTE 237
Cdd:PLN02565 160 TTGPEIWKGTGGK-VDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVD 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 238 IYDSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKE-LGKGKTVVTVLPSNGERYLSTPLY 306
Cdd:PLN02565 239 LLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLF 308
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
7-306 |
1.17e-106 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 313.48 E-value: 1.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPG-DTIVEPTSGNTGIGLAFVC 85
Cdd:PLN00011 9 NDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 86 AAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKE-LKEEHGYFEPQQFENPANPEVHELTTGPELL 164
Cdd:PLN00011 89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEiLSKTPGGYIPQQFENPANPEIHYRTTGPEIW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 165 QQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIK 244
Cdd:PLN00011 169 RDSAGK-VDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304357 245 VGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKE-LGKGKTVVTVLPSNGERYLSTPLY 306
Cdd:PLN00011 248 VTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVIFPSGGERYLSTKLF 310
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
7-302 |
1.25e-105 |
|
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: 315.59 E-value: 1.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCA 86
Cdd:TIGR01137 3 DNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 87 AKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGS---EAMKGAIKKAKELKEE-HGYFEPQQFENPANPEVHELTTGPE 162
Cdd:TIGR01137 83 IKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAaafDSPESHIGVAKRLVREiPGAHILDQYRNPSNPLAHYDTTGPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 163 LLQQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASpVLSGGEP------GPHKLQGLGAGFIPGTLNT 236
Cdd:TIGR01137 163 ILEQCEGK-LDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVLDR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304357 237 EIYDSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELG-KGKTVVTVLPSNGERYLS 302
Cdd:TIGR01137 241 KVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELqEGQRCVVLLPDSIRNYMT 307
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
9-307 |
1.17e-103 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 304.87 E-value: 1.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAK 88
Cdd:PRK11761 6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHGYFEPQQFENPANPEVHELTTGPELLQQFE 168
Cdd:PRK11761 86 GYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEIWRQTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 169 GKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEP-EASPVlsggePGPHKLQglgAGFIPGTLNTEIYDSIIKVGN 247
Cdd:PRK11761 166 GR-ITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSSI-----PGIRRWP---EEYLPKIFDASRVDRVLDVSQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 248 DTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELgKGKTVVTVLPSNGERYLSTPLYS 307
Cdd:PRK11761 237 QEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLSTGVFP 295
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
7-306 |
1.22e-102 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 307.09 E-value: 1.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTI-VEPTSGNTGIGLAFVC 85
Cdd:PLN03013 115 DNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 86 AAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKE-LKEEHGYFEPQQFENPANPEVHELTTGPELL 164
Cdd:PLN03013 195 ASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEiLKNTPDAYMLQQFDNPANPKIHYETTGPEIW 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 165 QQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIK 244
Cdd:PLN03013 275 DDTKGK-VDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVIA 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304357 245 VGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKE-LGKGKTVVTVLPSNGeRYLSTPLY 306
Cdd:PLN03013 354 ISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRpENAGKLIAVSLFASG-RDIYTPRC 415
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
7-306 |
2.24e-100 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 299.18 E-value: 2.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDT-IVEPTSGNTGIGLAFVC 85
Cdd:PLN02556 51 TDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 86 AAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEH-GYFEPQQFENPANPEVHELTTGPELL 164
Cdd:PLN02556 131 AMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTpDAFMLQQFSNPANTQVHFETTGPEIW 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 165 QQFEGKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIK 244
Cdd:PLN02556 211 EDTLGQ-VDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLE 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304357 245 VGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKEL-GKGKTVVTVLPSNGERYLSTPLY 306
Cdd:PLN02556 290 VSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPeNKGKLIVTVHPSFGERYLSSVLF 352
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
16-294 |
2.53e-92 |
|
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: 274.01 E-value: 2.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIkPGDTIVEPTSGNTGIGLAFVCAAKGYKAVFT 95
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 96 MPETMSQERRNLLKAYGAELVLTPGSeaMKGAIKKAKEL-KEEHGYFEPQQFENPANPEVHElTTGPELLQQFEGKTIDA 174
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPGD--FDDAIALAKELaEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGQKPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 175 FLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEaspvlsggepgphklqglgagfipgtlnteiydsIIKVGNDTAMEMS 254
Cdd:cd00640 157 VVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------VVTVSDEEALEAI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 579304357 255 RRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLP 294
Cdd:cd00640 203 RLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILT 242
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
9-307 |
4.54e-92 |
|
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: 275.62 E-value: 4.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAK 88
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKavFTM---PETMSQErRNLLKAYGAELVLT----PGSEAMKGAIKKAKELKEE-HGYFEPQQFENPANPEVHELTTG 160
Cdd:TIGR03945 81 GLR--FICvvdPNISPQN-LKLLRAYGAEVEKVtepdETGGYLGTRIARVRELLASiPDAYWPNQYANPDNPRAHYHGTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 161 PELLQQFegKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASpVLSGGEPGPHKLQGLGAGFIPGTLNTEIYD 240
Cdd:TIGR03945 158 REIARAF--PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGS-VIFGGPPGRRHIPGLGASVVPELLDESLID 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304357 241 SIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLSTpLYS 307
Cdd:TIGR03945 235 DVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDT-VYN 300
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
9-306 |
2.72e-91 |
|
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: 273.33 E-value: 2.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAK 88
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHGYFEPQQFENPANPEVHELTTGPELLQQFE 168
Cdd:TIGR01138 82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 169 GKtIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGgepgphkLQGLGAGFIPGTLNTEIYDSIIKVGND 248
Cdd:TIGR01138 162 GR-ITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDIHQR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 579304357 249 TAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGkTVVTVLPSNGERYLSTPLY 306
Cdd:TIGR01138 234 DAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDA-VVVAIICDRGDRYLSTGVF 290
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
9-294 |
7.95e-85 |
|
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: 256.85 E-value: 7.95e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREgkiKPGDTIVEPTSGNTGIGLAFVCAAK 88
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKAVFTMPETMSQERRNLLKAYGAELVLTPGSeaMKGAIKKAKELKEE-HGYFEPQQFENPANPEVHElTTGPELLQQF 167
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAARELAAEgPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 168 eGKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGG---------EPGPHKLQGLGAGFIPGTLNTEI 238
Cdd:pfam00291 155 -GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304357 239 Y----DSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAA-IQKAKELGKGKTVVTVLP 294
Cdd:pfam00291 234 LdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLT 294
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
3-302 |
3.64e-42 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 150.53 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 3 QKPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLA 82
Cdd:PLN02356 41 KKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 83 FVCAAKGYKAVFTMPETMSQERRNLLKAYGAELV-LTPGS----------------EAMKGAIKKAK------------- 132
Cdd:PLN02356 121 TVAPAYGCKCHVVIPDDVAIEKSQILEALGATVErVRPVSithkdhyvniarrralEANELASKRRKgsetdgihlektn 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 133 -----ELKEEH-------GYFEPQQFENPANPEVHELTTGPELLQQFEGkTIDAFLAGVGTGGTLSGVGKVLKKEYPNIE 200
Cdd:PLN02356 201 gciseEEKENSlfsssctGGFFADQFENLANFRAHYEGTGPEIWEQTQG-NLDAFVAAAGTGGTLAGVSRFLQEKNPNIK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 201 IVAIEPEASPVLSG-----------------GEPGPHKLQGLGAGFIPGTLNTEIYDSIIKVGNDTAMEMSRRVAKEEGI 263
Cdd:PLN02356 280 CFLIDPPGSGLFNKvtrgvmytreeaegrrlKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGL 359
|
330 340 350
....*....|....*....|....*....|....*....
gi 579304357 264 LAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLS 302
Cdd:PLN02356 360 FVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
7-293 |
4.84e-32 |
|
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: 120.67 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPgdtIVEPTSGNTGIGLAFVCA 86
Cdd:cd01562 9 ARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKG---VVAASAGNHAQGVAYAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 87 AKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSeaMKGAIKKAKELKEEHGYFepqqFENPAN-PEVHE--LTTGPEL 163
Cdd:cd01562 86 LLGIPATIVMPETAPAAKVDATRAYGAEVVLYGED--FDEAEAKARELAEEEGLT----FIHPFDdPDVIAgqGTIGLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 164 LQQFEGktIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLS----GGEPGPHKLQGL----GAGFIPGTLN 235
Cdd:cd01562 160 LEQVPD--LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAqslaAGKPVTLPEVDTiadgLAVKRPGELT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304357 236 TEIY----DSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIyAAIQKAKELGKGKTVVTVL 293
Cdd:cd01562 238 FEIIrklvDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALAL-AALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
16-293 |
4.98e-29 |
|
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: 113.21 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKpgdTIVEPTSGNTGIGLAFVCAAKGYKAVFT 95
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERAR---GVVAASAGNHAQGVAYAARLLGIPATIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 96 MPETMSQERRNLLKAYGAELVLTPGS--EAMkgaiKKAKELKEEHGYFEPQQFenpANPEVHE--LTTGPELLQQFEGkt 171
Cdd:COG1171 102 MPETAPAVKVAATRAYGAEVVLHGDTydDAE----AAAAELAEEEGATFVHPF---DDPDVIAgqGTIALEILEQLPD-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 172 IDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPV----LSGGEP----GPHKL-QGLGAGfIPGTLNTEIY--- 239
Cdd:COG1171 173 LDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAmyrsLAAGEPvtlpGVDTIaDGLAVG-RPGELTFEILrdl 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 579304357 240 -DSIIKVGND---TAMemsRRVAKEEGILAGiSSGAAIYAAIQKAKELGKGKTVVTVL 293
Cdd:COG1171 252 vDDIVTVSEDeiaAAM---RLLLERTKIVVE-PAGAAALAALLAGKERLKGKRVVVVL 305
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
14-297 |
9.38e-28 |
|
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: 109.61 E-value: 9.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 14 GGTPVVKLRNVVDD-NAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikpgDTIVEPTSGNTGIGLAFVCAAKGYKA 92
Cdd:cd01563 21 GNTPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 93 VFTMPETMSQERRNLLKAYGAELVLTPGSeaMKGAIKKAKELKEEHGYFepqqFENPANPEVHE--LTTGPELLQQFEGK 170
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEGN--FDDALRLVRELAEENWIY----LSNSLNPYRLEgqKTIAFEIAEQLGWE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 171 TIDAFLAGVGTGGTLSGVGKVLK--KEYPNIE----IVAIEPE-ASPVLSGGEPGphklqglGAGFIPGTLNTEIYDSI- 242
Cdd:cd01563 171 VPDYVVVPVGNGGNITAIWKGFKelKELGLIDrlprMVGVQAEgAAPIVRAFKEG-------KDDIEPVENPETIATAIr 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304357 243 ---------------------IKVGNDTAMEMSRRVAKEEGILAGISSGAAIyAAIQKAKELG---KGKTVVTVLPSNG 297
Cdd:cd01563 244 ignpasgpkalravresggtaVAVSDEEILEAQKLLARTEGIFVEPASAASL-AGLKKLREEGiidKGERVVVVLTGHG 321
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
5-297 |
8.22e-27 |
|
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: 108.36 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 5 PVDNITQII----GGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRiALAM-IEKAEREGKIkpgdTIVEPTSGNTGI 79
Cdd:COG0498 52 PFDDEEKAVslgeGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDR-AMQVaVSLALERGAK----TIVCASSGNGSA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 80 GLAFVCAAKGYKAVFTMPET-MSQERRNLLKAYGAELVLTPGS--EAMKGaikkAKELKEEHGYFepqqFENPANPEVHE 156
Cdd:COG0498 127 ALAAYAARAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNfdDAQRL----VKELAADEGLY----AVNSINPARLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 157 --LTTGPELLQQFeGKTIDAFLAGVGTGGTLSGVGKVlKKEYPN---IE----IVAIEPE-ASPVL---SGGEPGPHKLQ 223
Cdd:COG0498 199 gqKTYAFEIAEQL-GRVPDWVVVPTGNGGNILAGYKA-FKELKElglIDrlprLIAVQATgCNPILtafETGRDEYEPER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 224 GL---GAGFIPGTLNTE-----IYDS---IIKVGNDTAMEMSRRVAKEEGILAGISSGAAiYAAIQKAKE---LGKGKTV 289
Cdd:COG0498 277 PEtiaPSMDIGNPSNGEralfaLRESggtAVAVSDEEILEAIRLLARREGIFVEPATAVA-VAGLRKLREegeIDPDEPV 355
|
....*...
gi 579304357 290 VTVLPSNG 297
Cdd:COG0498 356 VVLSTGHG 363
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
30-293 |
4.17e-21 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 91.29 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 30 ADVYVKLEYQNPGGSVKDRIA---LAMIEKAEREgkikpgDTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRN 106
Cdd:PRK06815 35 CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQRQ------QGVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 107 LLKAYGAELVLTPGSeaMKGAIKKAKELKEEHGyfepQQFENPAN-PEV--HELTTGPELLQQFEGktIDAFLAGVGTGG 183
Cdd:PRK06815 109 AIRALGAEVRLYGGD--ALNAELAARRAAEQQG----KVYISPYNdPQViaGQGTIGMELVEQQPD--LDAVFVAVGGGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 184 TLSGVGKVLKKEYPNIEIVA------------------IEPEASPVLSGGEPGphklqGLGAGFIPGTLNTEIYDSIIKV 245
Cdd:PRK06815 181 LISGIATYLKTLSPKTEIIGcwpanspslytsleageiVEVAEQPTLSDGTAG-----GVEPGAITFPLCQQLIDQKVLV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 579304357 246 GNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELgKGKTVVTVL 293
Cdd:PRK06815 256 SEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY-QGKKVAVVL 302
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
16-293 |
1.02e-18 |
|
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: 85.57 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKpgdTIVEPTSGNTGIGLAFVCAAKGYKAVFT 95
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQR---GVVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 96 MPETMSQERRNLLKAYGAELVLTpgSEAMKGAIKKAKELKEEHGYFEPQQFEnpaNPEV--HELTTGPELLQQfeGKTID 173
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILH--GDDYDEAYAFATSLAEEEGRVFVHPFD---DEFVmaGQGTIGLEIMED--IPDVD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 174 AFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPV----LSGGEPGPHKLQGLGAGFI----PGTLNTEI----YDS 241
Cdd:TIGR01127 151 TVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSmyesLREGKIKAVESVRTIADGIavkkPGDLTFNIikeyVDD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 579304357 242 IIKVGNDTAMEMSRRVAKEEGILAGiSSGAAIYAAIQKAKELGKGKTVVTVL 293
Cdd:TIGR01127 231 VVTVDEEEIANAIYLLLERHKILAE-GAGAAGVAALLEQKVDVKGKKIAVVL 281
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
14-293 |
4.72e-18 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 82.83 E-value: 4.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 14 GGTPVVKLRNVVDD-NAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikpgDTIVEPTSGNTGIGLAFVCAAKGYKA 92
Cdd:PRK06381 14 GGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 93 VFTMPETMSQERRNLLKAYGAELVLTPGSeaMKGAIKKAKELKEEHGYFEpqqfENP--ANPEVHELTTGP---ELLQQF 167
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGK--YEEAVERSRKFAKENGIYD----ANPgsVNSVVDIEAYSAiayEIYEAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 168 eGKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIE-------IVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTE--- 237
Cdd:PRK06381 164 -GDVPDAVAVPVGNGTTLAGIYHGFRRLYDRGKtsrmprmIGVSTSGGNQIVESFKRGSSEVVDLEVDEIRETAVNEplv 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304357 238 -------------IYDS---IIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVL 293
Cdd:PRK06381 243 syrsfdgdnaleaIYDShgyAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
14-300 |
2.04e-16 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 78.89 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 14 GGTPVVKLRNVVDD-NAADVYVKLEYQNPGGSVKDRIALAMIEKAeREGKIKpgdTIVEPTSGNTGIGLAFVCAAKGYKA 92
Cdd:PRK08197 78 GMTPLLPLPRLGKAlGIGRLWVKDEGLNPTGSFKARGLAVGVSRA-KELGVK---HLAMPTNGNAGAAWAAYAARAGIRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 93 VFTMPETMSQERRNLLKAYGAELVLTPG--SEAmkGAIkkAKELKEEHGYFEPQQFENPANPEVHElTTGPELLQQFEGK 170
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYLVDGliSDA--GKI--VAEAVAEYGWFDVSTLKEPYRIEGKK-TMGLELAEQLGWR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 171 TIDAFLAGVGTGGTLSGVGKVLKK---------EYPniEIVAIEPEA-SPVLSGGEPGPHKL------QGLGAGF-IPGT 233
Cdd:PRK08197 229 LPDVILYPTGGGVGLIGIWKAFDElealgwiggKRP--RLVAVQAEGcAPIVKAWEEGKEESefwedaHTVAFGIrVPKA 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304357 234 L-NTEIYDSI-------IKVGNDTAMEMSRRVAKEEGILAGiSSGAAIYAAIQKAKE---LGKGKTVVTVLPSNGERY 300
Cdd:PRK08197 307 LgDFLVLDAVretggcaIAVSDDAILAAQRELAREEGLFAC-PEGAATFAAARQLREsgwLKGDERVVLFNTGSGLKY 383
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
16-217 |
8.04e-16 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 76.53 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRnVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEregkiKPGDTIVEPTSGNTGIGLAFVCAAKGYKAVFT 95
Cdd:PRK08246 24 TPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 96 MPETMSQERRNLLKAYGAELVLTPGS--EAMKGAIKKAKE--LKEEHGYfepqqfenpANPEV--HELTTGPELLQQFEG 169
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAEyaDALEAAQAFAAEtgALLCHAY---------DQPEVlaGAGTLGLEIEEQAPG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579304357 170 ktIDAFLAGVGTGGTLSGVGKVLKkeyPNIEIVAIEPEASPVL----SGGEP 217
Cdd:PRK08246 169 --VDTVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGAPTLhaalAAGEP 215
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
14-297 |
7.80e-15 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 74.00 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 14 GGTPVVKlrnvvddnAADVYVKLEYQNPGGSVKDRIALAMIEKAeREGKIKpgdTIVEPTSGNTGIGLAFVCAAKGYKAV 93
Cdd:PRK06450 57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYL-AEKGIK---QISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 94 FTMPETMSQERRNLLKAYGAELVLTPGSeamKGAIKKAKElkEEHGYFEPQQFEnpanPEVHE--LTTGPELLQQFEGKT 171
Cdd:PRK06450 125 IFVPETASGGKLKQIESYGAEVVRVRGS---REDVAKAAE--NSGYYYASHVLQ----PQFRDgiRTLAYEIAKDLDWKI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 172 IDAFLAGVGTGGTLSGVGKVLK--------KEYPNieIVAIEPEA-SPVLsggepgpHKLQGLgaGFIPGTLNTEIYDSI 242
Cdd:PRK06450 196 PNYVFIPVSAGTLLLGVYSGFKhlldsgviSEMPK--IVAVQTEQvSPLC-------AKFKGI--SYTPPDKVTSIADAL 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304357 243 ---------------------IKVGNDTAMEMSRRVAKeEGILAGISSgAAIYAAIQKAKElgkgKTVVTVLPSNG 297
Cdd:PRK06450 265 vstrpflldymvkalseygecIVVSDNEIVEAWKELAK-KGLLVEYSS-ATVYAAYKKYSV----NDSVLVLTGSG 334
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
30-300 |
1.07e-14 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 74.07 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 30 ADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikpGDTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLK 109
Cdd:PRK08639 40 ANVYLKREDLQPVRSYKLRGAYNAISQLSDEEL---AAGVVCASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 110 AYGA---ELVLTpGS---EAMKGAIKKAKElkeEHGYFEPQqFENPANPEvHELTTGPELLQQFE-GKTIDAFLAGVGTG 182
Cdd:PRK08639 117 FFGGefvEIVLV-GDtfdDSAAAAQEYAEE---TGATFIPP-FDDPDVIA-GQGTVAVEILEQLEkEGSPDYVFVPVGGG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 183 GTLSGVGKVLKKEYPNIEIVAIEPEASP----VLSGGEpgPHKLQGL-----GA-----GFIPGTLNTEIYDSIIKVGND 248
Cdd:PRK08639 191 GLISGVTTYLKERSPKTKIIGVEPAGAAsmkaALEAGK--PVTLEKIdkfvdGAavarvGDLTFEILKDVVDDVVLVPEG 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 249 ---TAM-EMsrrvAKEEGILAGiSSGAAIYAAIQKAKELGKGKTVVTVLpSNG----ERY 300
Cdd:PRK08639 269 avcTTIlEL----YNKEGIVAE-PAGALSIAALELYKDEIKGKTVVCVI-SGGnndiERM 322
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
31-206 |
1.31e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 73.27 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 31 DVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikPGDTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKA 110
Cdd:PRK06608 39 EIFFKVESLQKTGAFKVRGVLNHLLELKEQGK--LPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 111 YGAELVLTPGSEAmkgAIKKAKELKEEHGYFEPqqfenPANPE---VHELTTGPELLQQFeGKTIDAFLAGVGTGGTLSg 187
Cdd:PRK06608 117 YGGEVILTNTRQE---AEEKAKEDEEQGFYYIH-----PSDSDstiAGAGTLCYEALQQL-GFSPDAIFASCGGGGLIS- 186
|
170 180
....*....|....*....|.
gi 579304357 188 vGKVLKKEY--PNIEIVAIEP 206
Cdd:PRK06608 187 -GTYLAKELisPTSLLIGSEP 206
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
30-290 |
7.58e-14 |
|
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: 71.03 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 30 ADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKpgdTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPET-MSQERRN-- 106
Cdd:cd06446 50 AKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR---VIAETGAGQHGVATATACALFGLECEIYMGAVdVERQPLNvf 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 107 LLKAYGAELVLTP-GSEAMKGAIKKAKE--LKEEHGYF-------EPQQFENpanpEVHELTT--GPELLQQF---EGKT 171
Cdd:cd06446 127 RMELLGAEVVPVPsGSGTLKDAISEAIRdwVTNVEDTHyllgsvvGPHPYPN----MVRDFQSviGEEAKKQIlekEGEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 172 IDAFLAGVGTGGTLSGVGKVLKKEyPNIEIVAIEPEASPVLSGGEPGPhkLQGLGAGFIPG----TLNTEIYD----SII 243
Cdd:cd06446 203 PDVVIACVGGGSNAAGLFYPFIND-KDVKLIGVEAGGCGLETGGHAAY--LFGGTAGVLHGlkmyTLQDEDGQivppHSI 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304357 244 KVG-------------------------NDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVV 290
Cdd:cd06446 280 SAGldypgvgpehaylkdsgrveyvavtDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAKKLGKEKVIV 351
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
9-293 |
1.92e-12 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 66.68 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 9 ITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKpgdTIVEPTSGNTGIGLAFVCAAK 88
Cdd:PRK08638 21 LAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRK---GVVACSAGNHAQGVALSCALL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 89 GYKAVFTMPETMSQERRNLLKAYGAELVLTpgSEAMKGAIKKAKELKEEHGyfepQQFENPAN-PEV--HELTTGPELLQ 165
Cdd:PRK08638 98 GIDGKVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEEG----RTFIPPYDdPKViaGQGTIGLEILE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 166 QFegKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPE------ASpvLSGGEPGPHKLQG-LGAGF---IPGTLN 235
Cdd:PRK08638 172 DL--WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSEnvhgmaAS--FYAGEITTHRTTGtLADGCdvsRPGNLT 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304357 236 TEI----YDSIIKVGND---TAME--MSRRVAKEEGilAGISSGAAIYAAiqKAKELGKGKTVVTVL 293
Cdd:PRK08638 248 YEIvrelVDDIVLVSEDeirNAMKdlIQRNKVVTEG--AGALATAALLSG--KLDQYIQNKKVVAII 310
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
16-209 |
3.13e-12 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 66.74 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIA---LAMIEKAEREgkikpgDTIVEPTSGNTGIGLAFVCAAKGYKA 92
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAynkMARLPAEQLA------RGVITASAGNHAQGVALAAARLGVKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 93 VFTMPETMSQERRNLLKAYGAELVLTpgSEAMKGAIKKAKELKEEHGYFEPQQFENPaNPEVHELTTGPELLQQFEGKtI 172
Cdd:PRK12483 112 VIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPPFDDP-DVIAGQGTVAMEILRQHPGP-L 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 579304357 173 DAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEAS 209
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
14-297 |
7.87e-12 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 65.60 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 14 GGTPVVKLRNVVDDNAaDVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikpgDTIVEPTSGNTGIGLAFVCAAKGYKAV 93
Cdd:PRK05638 65 GGTPLIRARISEKLGE-NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 94 FTMPETMSQERRNLLKAYGAELVLTpgSEAMKGAIKKAKELKEEHGYFEPQQFENPANPEVHElTTGPELLQQFEGKTId 173
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQK-TIAFELWEEINPTHV- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 174 afLAGVGTGGTLSGVGKVLKK--------EYPNieIVAIEPE-ASPVLSG-----GEPGPHKLQGLgagFIPGTLNTEIY 239
Cdd:PRK05638 216 --IVPTGSGSYLYSIYKGFKElleigvieEIPK--LIAVQTErCNPIASEilgnkTKCNETKALGL---YVKNPVMKEYV 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304357 240 DSIIK-------VGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKE--LGKGKTVVTVLPSNG 297
Cdd:PRK05638 289 SEAIKesggtavVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGSG 355
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
31-212 |
3.43e-11 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 63.62 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 31 DVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKpGdtIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKA 110
Cdd:PRK09224 36 QVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLAR-G--VITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 111 YGAELVLTpgSEAMKGAIKKAKELKEEHGY-FEPqqfenpanPEVHEL------TTGPELLQQFEGKtIDAFLAGVGTGG 183
Cdd:PRK09224 113 FGGEVVLH--GDSFDEAYAHAIELAEEEGLtFIH--------PFDDPDviagqgTIAMEILQQHPHP-LDAVFVPVGGGG 181
|
170 180
....*....|....*....|....*....
gi 579304357 184 TLSGVGKVLKKEYPNIEIVAIEPEASPVL 212
Cdd:PRK09224 182 LIAGVAAYIKQLRPEIKVIGVEPEDSACL 210
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
16-293 |
4.00e-11 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 62.92 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLrnvvddnAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikpgDTIVEPTSGNTGIGLAFVCAAKGYKAVFT 95
Cdd:PRK08329 65 TPTVKR-------SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 96 MPETMSQERRNLLKAYGAELVLTPGSEaMKgAIKKAKELKEEHGYFEPQQFENPANPEVHElTTGPELLQQFegKTIDAF 175
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFVEGDR-ME-VHEEAVKFSKRNNIPYVSHWLNPYFLEGTK-TIAYEIYEQI--GVPDYA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 176 LAGVGTGGTLSGVGKVLKK--EYPNIE----IVAIEPEASPVLSGGEPGPHKL-QGLGagfIPGTLNTEIYDSIIKVGND 248
Cdd:PRK08329 209 FVPVGSGTLFLGIWKGFKElhEMGEISkmpkLVAVQAEGYESLCKRSKSENKLaDGIA---IPEPPRKEEMLRALEESNG 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 579304357 249 TAMEMSRRV---AKEEGILAGI---SSGAAIYAAIQKAKELGKGKTVVTVL 293
Cdd:PRK08329 286 FCISVGEEEtraALHWLRRMGFlvePTSAVALAAYWKLLEEGLIEGGSKVL 336
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
4-297 |
1.09e-09 |
|
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: 58.55 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 4 KPVDNITQIIGGTPVVKLRNVVDD-NAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKikpgDTIVEPTSGNTGIGLA 82
Cdd:TIGR00260 11 TEKDLVDLGEGVTPLFRAPALAANvGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 83 FVCAAKGYKAVFTMPE-TMSQERRNLLKAYGAELVLTPGS-EAMKGAIKKAKELKEEHGYfepqqfeNPANPEVHEL--- 157
Cdd:TIGR00260 87 AYAGKAGLKVVVLYPAgKISLGKLAQALGYNAEVVAIDGNfDDAQRLVKQLFEDKPALGL-------NSANSIPYRLegq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 158 -TTGPELLQQFEGKTIDAFLAGVGTGGTLSGVGK-------VLKKEYPniEIVAIEPE-ASPV----LSGGEPGPHKlqg 224
Cdd:TIGR00260 160 kTYAFEAVEQLGWEAPDKVVVPVPNSGNFGAIWKgfkekkmLGLDSLP--VKRGIQAEgAADIvrafLEGGQWEPIE--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 225 lgagfIPGTLNTEI---------------YDSIIK---VGNDTAMEMSRRVAKEEGILAGISSGAAiYAAIQKAKELGK- 285
Cdd:TIGR00260 235 -----TPETLSTAMdignpanwpraleafRRSNGYaedLSDEEILEAIKLLAREEGYFVEPHSAVA-VAALLKLVEKGTa 308
|
330
....*....|....
gi 579304357 286 --GKTVVTVLPSNG 297
Cdd:TIGR00260 309 dpAERVVCALTGNG 322
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
16-208 |
1.54e-09 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 58.11 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDR---IALAMIEKAEREGKIkpgdtiVEPTSGNTGIGLAFVCAAKGYKA 92
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRgayNALSQFSPEQRRAGV------VTFSSGNHAQAIALSARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 93 VFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIkkAKELKEEHGYFEPQQFENPanpevHEL----TTGPELLQqfE 168
Cdd:PRK07048 99 TIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEI--GRRLAEERGLTLIPPYDHP-----HVIagqgTAAKELFE--E 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579304357 169 GKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEA 208
Cdd:PRK07048 170 VGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEA 209
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
32-212 |
1.74e-09 |
|
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: 57.69 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 32 VYVKLEYQNPGGSVKDR-IALAMIEKAEREGKIKPGdtIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKA 110
Cdd:cd06448 18 VFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 111 YGAELVLTpGSEAMKGAIKKAKEL-KEEHG--YFEPqqFENPANPEVHElTTGPELLQQF-EGKTIDAFLAGVGTGGTLS 186
Cdd:cd06448 96 EGATVVVH-GKVWWEADNYLREELaENDPGpvYVHP--FDDPLIWEGHS-SMVDEIAQQLqSQEKVDAIVCSVGGGGLLN 171
|
170 180
....*....|....*....|....*..
gi 579304357 187 GVGKVLKKEYPN-IEIVAIEPEASPVL 212
Cdd:cd06448 172 GIVQGLERNGWGdIPVVAVETEGAHSL 198
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
32-206 |
3.03e-09 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 57.62 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 32 VYVKLEYQNPGGSVKDRIALAMIEKAEREgKIKPGdtIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKAY 111
Cdd:PLN02550 126 VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 112 GAELVLTPGSEAMKGAIKKAKELKEEHGYFEPqqFENPaNPEVHELTTGPELLQQFEGKtIDAFLAGVGTGGTLSGVGKV 191
Cdd:PLN02550 203 GATVVLVGDSYDEAQAYAKQRALEEGRTFIPP--FDHP-DVIAGQGTVGMEIVRQHQGP-LHAIFVPVGGGGLIAGIAAY 278
|
170
....*....|....*
gi 579304357 192 LKKEYPNIEIVAIEP 206
Cdd:PLN02550 279 VKRVRPEVKIIGVEP 293
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
16-293 |
8.89e-09 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 56.05 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIA---LAMIEKAERE-GkikpgdtIVEPTSGNTGIGLAFVCAAKGYK 91
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGAlnkLLLLTEEERArG-------VIAMSAGNHAQGVAYHAQRLGIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 92 AVFTMPETMSQERRNLLKAYGAELVLTpgSEAMKGAIKKAKELKEEHGYfepqQFENPAN-PEV--HELTTGPELLQqfE 168
Cdd:PRK07334 97 ATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAHARELAEEEGL----TFVHPYDdPAViaGQGTVALEMLE--D 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 169 GKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQG---LGAGFI---PGTLNTEIY--- 239
Cdd:PRK07334 169 APDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVALPCGgstIAEGIAvkqPGQLTLEIVrrl 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 579304357 240 -DSIIKVgNDTAME--MSRRVAKEEGILAGisSGAAIYAAIQKAKELGKGKTVVTVL 293
Cdd:PRK07334 249 vDDILLV-SEADIEqaVSLLLEIEKTVVEG--AGAAGLAALLAYPERFRGRKVGLVL 302
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
27-302 |
1.25e-07 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 52.49 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 27 DNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGkikpgdtiVEPTSGNTGIG-----LAFVCAAKGYKA-VFTMPETM 100
Cdd:PRK12391 91 GTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEG--------IKRLTTETGAGqwgsaLALACALFGLECtVFMVRVSY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 101 SQE--RRNLLKAYGAELV-----LT-------------PGSEAMkgAIKKAKELKEEHG---YfepqqfenpANPEV--- 154
Cdd:PRK12391 163 EQKpyRRSLMETYGAEVIpspsdLTeagrkilaedpdhPGSLGI--AISEAVEDAAKRPdtkY---------ALGSVlnh 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 155 ---HELTTGPELLQQFE--GKTIDAFLAGVGTGGTLSG-----VGKVLKKEyPNIEIVAIEPEASPVLSGGE-------- 216
Cdd:PRK12391 232 vllHQTVIGLEAKKQLElaGEYPDVVIGCVGGGSNFAGlafpfLGDKLEGK-KDTRFIAVEPAACPTLTKGEyaydfgdt 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 217 --PGP-HKLQGLGAGFIP--------------GTLNTEIYDSIIK---VGNDTAMEMSRRVAKEEGILAGISSGAAIYAA 276
Cdd:PRK12391 311 agLTPlLKMYTLGHDFVPppihagglryhgmaPLVSLLVHEGLIEaraYPQTEVFEAAVLFARTEGIVPAPESSHAIAAA 390
|
330 340 350
....*....|....*....|....*....|....*.
gi 579304357 277 IQ---KAKELGKGKTVVTVLPSNG-------ERYLS 302
Cdd:PRK12391 391 IDealKAKEEGEEKVILFNLSGHGlldlaayDAYLA 426
|
|
| PLN02970 |
PLN02970 |
serine racemase |
7-209 |
1.95e-07 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 51.60 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 7 DNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMI-----EKAEREgkikpgdtIVEPTSGNTGIGL 81
Cdd:PLN02970 19 KRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 82 AFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIkkAKELKEEHGyfepQQFENPAN-PEV--HELT 158
Cdd:PLN02970 91 ALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAV--AARVQQETG----AVLIHPYNdGRVisGQGT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 579304357 159 TGPELLQQFegKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEAS 209
Cdd:PLN02970 165 IALEFLEQV--PELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
16-290 |
3.94e-07 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 50.56 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNP---GGSvKDRIALAMIEKAEREGKikpgDTIVepTSGntGIG------LAFVCA 86
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDLTGpaiGGN-KTRKLEYLLADALAQGA----DTLV--TFG--GAQsnharaTAAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 87 AKGYKAV-FTMPETMSQERRNLL--KAYGAELVLTPGSE---AMKGAIKKAKELKEEHG--YFEPqqfENPANPE----V 154
Cdd:COG2515 83 KLGLKCVlVLRGEEPTPLNGNLLldRLLGAELHFVSRGEyrdRDEAMEAVAAELRARGGkpYVIP---EGGSNPLgalgY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 155 HELTTgpELLQQFE--GKTIDAFLAGVGTGGTLSG--VGKVLKKeyPNIEIVAIepeasPVLSGGEPGPHKLQGLgAGFI 230
Cdd:COG2515 160 VEAAA--ELAAQLAelGVDFDYIVVASGSGGTLAGlvAGLALLG--SDTRVIGI-----SVLKGADFLRERVAEL-ARAT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304357 231 PGTLNTEIYDSII-----------KVgNDTAMEMSRRVAKEEGILAG-ISSGAAIYAAIQ--KAKELGKGKTVV 290
Cdd:COG2515 230 AALLGLVSRADIEldddyhgggygKP-TPELIEAIRLFARTEGILLDpVYTGKAMAGLIDliRKGRFPPGSRVL 302
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
30-116 |
5.59e-07 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 50.38 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 30 ADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGdtIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLK 109
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113
|
....*..
gi 579304357 110 AYGAELV 116
Cdd:PRK06110 114 ALGAELI 120
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
16-204 |
2.59e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 48.04 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 16 TPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKpgdTIVEPTSGNTGIGLAFVCAAKGYKAVFT 95
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERAR---GVVTASTGNHGRALAYAARALGIRATIC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 96 MPETMSQERRNLLKAYGAELVLTPGS--EAMKGAIKkakeLKEEHGYFEPQQFENPAnpeV--HELTTGPELLQQF-EGK 170
Cdd:PRK07476 97 MSRLVPANKVDAIRALGAEVRIVGRSqdDAQAEVER----LVREEGLTMVPPFDDPR---IiaGQGTIGLEILEALpDVA 169
|
170 180 190
....*....|....*....|....*....|....
gi 579304357 171 TIdafLAGVGTGGTLSGVGKVLKKEYPNIEIVAI 204
Cdd:PRK07476 170 TV---LVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
55-133 |
2.76e-06 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 48.34 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 55 EKAEREGKIkpgdTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGS--EAMKGAIKKAK 132
Cdd:PRK08206 109 EVREKLGDI----TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNydDSVRLAAQEAQ 184
|
.
gi 579304357 133 E 133
Cdd:PRK08206 185 E 185
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
31-295 |
4.13e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 44.80 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 31 DVYVKLEYQNPGGSVKDRIALAMIEKAEREGKI-KPGDTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPE---TMSQERRN 106
Cdd:PLN02569 151 DLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPAdkiSIAQLVQP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 107 LlkAYGAeLVLTPGSEaMKGAIKKAKELKEEHGYFEPQQFeNPANPEVHElTTGPELLQQFEGKTIDAFLAGVGTGGTLS 186
Cdd:PLN02569 231 I--ANGA-LVLSIDTD-FDGCMRLIREVTAELPIYLANSL-NSLRLEGQK-TAAIEILQQFDWEVPDWVIVPGGNLGNIY 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 187 GVGKVLK--KEYPNIE-----IVAIEPEASPVLSGGEPG-----PHKLQGLGAGFI----PGTLNTEIY-----DSIIKV 245
Cdd:PLN02569 305 AFYKGFKmcKELGLVDrlprlVCAQAANANPLYRAYKSGweefkPVKANPTFASAIqigdPVSIDRAVYalkesNGIVEE 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 579304357 246 GNDTAMEMSRRVAKEEGILAGISSGAAiYAAIQKAKELGK-GKTVVTVLPS 295
Cdd:PLN02569 385 ATEEELMDAQAEADKTGMFLCPHTGVA-LAALKKLRASGViGPTDRTVVVS 434
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
33-131 |
1.80e-03 |
|
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: 39.35 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 33 YVKLEYQNP---GGSVKDRIAlAMIE------KAEREGKIKPGDTIVepTSGNTGIGLAFVCAAK--GYKAVFTMpeTMS 101
Cdd:COG1063 121 YVRVPAANLvkvPDGLSDEAA-ALVEplavalHAVERAGVKPGDTVL--VIGAGPIGLLAALAARlaGAARVIVV--DRN 195
|
90 100 110
....*....|....*....|....*....|
gi 579304357 102 QERRNLLKAYGAELVLTPGSEAMKGAIKKA 131
Cdd:COG1063 196 PERLELARELGADAVVNPREEDLVEAVREL 225
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
248-290 |
3.26e-03 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 38.89 E-value: 3.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 579304357 248 DTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVV 290
Cdd:PRK04346 333 DEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIV 375
|
|
| iditol_2_DH_like |
cd08235 |
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ... |
52-130 |
5.09e-03 |
|
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish 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 GroES-like catalytic domain. 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. 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.
Pssm-ID: 176197 [Multi-domain] Cd Length: 343 Bit Score: 37.96 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 52 AMIE------KAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAKGYKAVFTMpeTMSQERRNLLKAYGAELVLTPGSEAMK 125
Cdd:cd08235 146 ALVEplacciNAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVS--DLNEFRLEFAKKLGADYTIDAAEEDLV 223
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....*
gi 579304357 126 GAIKK 130
Cdd:cd08235 224 EKVRE 228
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| Zn_ADH3 |
cd08265 |
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ... |
58-119 |
6.02e-03 |
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Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. 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: 176226 [Multi-domain] Cd Length: 384 Bit Score: 37.88 E-value: 6.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304357 58 EREGKIKPGDTIVepTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTP 119
Cdd:cd08265 196 IRGGGFRPGAYVV--VYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNP 255
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| quinone_oxidoreductase_like_1 |
cd08243 |
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
62-141 |
7.36e-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: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304357 62 KIKPGDTIVePTSGNTGIGLAFVCAAKGYKAvFTMPETMSQERRNLLKAYGAELVLTPgseamKGAIkkAKELKEEHGYF 141
Cdd:cd08243 139 GLQPGDTLL-IRGGTSSVGLAALKLAKALGA-TVTATTRSPERAALLKELGADEVVID-----DGAI--AEQLRAAPGGF 209
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