|
Name |
Accession |
Description |
Interval |
E-value |
| cysM |
PRK11761 |
cysteine synthase CysM; |
1-294 |
0e+00 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 638.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 1 MSTLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIA 80
Cdd:PRK11761 3 YPTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 81 ALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQ 160
Cdd:PRK11761 83 AIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEIWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 161 QTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTEYLPGIFNASLVDEVLDIHQRDAENT 240
Cdd:PRK11761 163 QTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDVSQQEAENT 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16130347 241 MRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIICDRGDRYLSTGVFGE 294
Cdd:PRK11761 243 MRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAIICDRGDRYLSTGVFPA 296
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
3-292 |
0e+00 |
|
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: 554.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 3 TLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 82
Cdd:TIGR01138 1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 83 KGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 163 GGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTEYLPGIFNASLVDEVLDIHQRDAENTMR 242
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPGIRRWPTEYLPGIFDASLVDRVLDIHQRDAENTMR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16130347 243 ELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIICDRGDRYLSTGVF 292
Cdd:TIGR01138 241 ELAVREGIFCGVSSGGAVAAALRLARELPDAVVVAIICDRGDRYLSTGVF 290
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
4-292 |
1.63e-175 |
|
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: 486.79 E-value: 1.63e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 83
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANR-GEGKLLDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 163 GGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPG-------IRRWPTEYLPGIFNASLVDEVLDIHQR 235
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGgepgphkIQGIGAGFIPKILDLSLIDEVITVSDE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130347 236 DAENTMRELAVREGIFCGVSSGGAVAGALRVAK--ANPDAVVVAIICDRGDRYLSTGVF 292
Cdd:TIGR01136 241 DAIETARRLAREEGILVGISSGAAVAAALKLAKrlENADKVIVAILPDTGERYLSTGLF 299
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-289 |
3.19e-167 |
|
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: 466.06 E-value: 3.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 1 MSTLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIA 80
Cdd:COG0031 4 YDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 81 ALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEG-KLLDQFNNPDNPYAHYTTTGPEIW 159
Cdd:COG0031 84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGaFWPNQFENPANPEAHYETTGPEIW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 160 QQTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPG-------IRRWPTEYLPGIFNASLVDEVLDI 232
Cdd:COG0031 164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGgepgphkIEGIGAGFVPKILDPSLIDEVITV 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130347 233 HQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAK-ANPDAVVVAIICDRGDRYLST 289
Cdd:COG0031 244 SDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKrLGPGKTIVTILPDSGERYLST 301
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
9-288 |
5.45e-146 |
|
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: 411.91 E-value: 5.45e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMK 88
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 89 LLMPDNMSQERRAAMRAYGAELILVTKEQ--GMEGARDLALEMANRGEG-KLLDQFNNPDNPYAHYTTTGPEIWQQTGGR 165
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNaFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 166 ITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEE----------GSSIPGIRRWpteYLPGIFNASLVDEVLDIHQR 235
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGsvlfsggppgPHKIEGIGAG---FIPENLDRSLIDEVVRVSDE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16130347 236 DAENTMRELAVREGIFCGVSSGGAVAGALRVAKAN-PDAVVVAIICDRGDRYLS 288
Cdd:cd01561 238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTILPDSGERYLS 291
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
5-292 |
1.31e-123 |
|
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: 355.52 E-value: 1.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 5 EQTIGNTPLVKLQRMGPDNGsEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKG 84
Cdd:TIGR01139 2 SELIGNTPLVRLNRIEGCNA-NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 85 YRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGK--LLDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01139 81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyfMLQQFENPANPEIHRKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 163 GGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPG-------IRRWPTEYLPGIFNASLVDEVLDIHQR 235
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGgkpgphkIQGIGAGFIPKNLNRSVIDEVITVSDE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130347 236 DAENTMRELAVREGIFCGVSSGGAVAGALRVAK-ANPDAVVVAIICDRGDRYLSTGVF 292
Cdd:TIGR01139 241 EAIETARRLAAEEGILVGISSGAAVAAALKLAKrPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
6-289 |
3.73e-101 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 299.47 E-value: 3.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 6 QTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGY 85
Cdd:PRK10717 9 DTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 86 RMKLLMPDNMSQERRAAMRAYGAELILV------TKEQGMEGARDLALEMANRGEGK--LLDQFNNPDNPYAHYTTTGPE 157
Cdd:PRK10717 89 KTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPNGaiWANQFDNPANREAHYETTGPE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 158 IWQQTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPE---------------EGSSIP---GIRRwpteyLPG 219
Cdd:PRK10717 169 IWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTgsalysyyktgelkaEGSSITegiGQGR-----ITA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130347 220 IFNASLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKAN-PDAVVVAIICDRGDRYLST 289
Cdd:PRK10717 244 NLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELgPGHTIVTILCDSGERYQSK 314
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
8-292 |
4.73e-88 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 266.02 E-value: 4.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 8 IGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGD-VLIEATSGNTGIALAMIAALKGYR 86
Cdd:PLN02565 13 IGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGEsVLIEPTSGNTGIGLAFMAAAKGYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 87 MKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEM-ANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQTGGR 165
Cdd:PLN02565 93 LIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEIlAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 166 ITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTE-------YLPGIFNASLVDEVLDIHQRDAE 238
Cdd:PLN02565 173 VDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKiqgigagFIPGVLDVDLLDEVVQVSSDEAI 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130347 239 NTMRELAVREGIFCGVSSGGAVAGALRVAK--ANPDAVVVAIICDRGDRYLSTGVF 292
Cdd:PLN02565 253 ETAKLLALKEGLLVGISSGAAAAAAIKIAKrpENAGKLIVVIFPSFGERYLSSVLF 308
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
8-288 |
1.24e-86 |
|
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: 266.67 E-value: 1.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 8 IGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:TIGR01137 9 IGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 88 KLLMPDNMSQERRAAMRAYGAELILVTKEQGMEG-------ARDLALEMANrgeGKLLDQFNNPDNPYAHYTTTGPEIWQ 160
Cdd:TIGR01137 89 IIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSpeshigvAKRLVREIPG---AHILDQYRNPSNPLAHYDTTGPEILE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 161 QTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPE-----EGSSIPGIRRWPTE-------YLPGIFNASLVDE 228
Cdd:TIGR01137 166 QCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEgsilaQPEELNQTGRTPYKvegigydFIPTVLDRKVVDE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130347 229 VLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKA--NPDAVVVAIICDRGDRYLS 288
Cdd:TIGR01137 246 WIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDelQEGQRCVVLLPDSIRNYMT 307
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
4-289 |
1.60e-86 |
|
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: 261.37 E-value: 1.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 83
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVTK--EQG-MEGAR-DLALEMANRGEGKL-LDQFNNPDNPYAHYTTTGPEI 158
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEpdETGgYLGTRiARVRELLASIPDAYwPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 159 WQQTgGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQpEEGSSI----PGIRRWP---TEYLPGIFNASLVDEVLD 231
Cdd:TIGR03945 161 ARAF-PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVD-AVGSVIfggpPGRRHIPglgASVVPELLDESLIDDVVH 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130347 232 IHQRDAENTMRELAVREGIFCGVSSGGAVAGALRV-AKANPDAVVVAIICDRGDRYLST 289
Cdd:TIGR03945 239 VPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLlPRIPEGSTVVAILPDRGERYLDT 297
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
11-282 |
1.57e-82 |
|
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: 248.97 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIkPGDVLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 91 MPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMANRGEG-KLLDQFNNPDNPYAHYtTTGPEIWQQTGG-RITH 168
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLV--PGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 169 FVSSMGTTGTITGVSRFMREQSKPVTIVGLQPeegssipgirrwpteylpgifnaslvdEVLDIHQRDAENTMRELAVRE 248
Cdd:cd00640 157 VVVPVGGGGNIAGIARALKELLPNVKVIGVEP---------------------------EVVTVSDEEALEAIRLLAREE 209
|
250 260 270
....*....|....*....|....*....|....*
gi 16130347 249 GIFCGVSSGGAVAGALRVA-KANPDAVVVAIICDR 282
Cdd:cd00640 210 GILVEPSSAAALAAALKLAkKLGKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
4-281 |
2.77e-79 |
|
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: 242.60 E-value: 2.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIvEAEKRGEikPGDVLIEATSGNTGIALAMIAALK 83
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGE--GGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMANRGEGK-LLDQFNNPDNPYAhYTTTGPEIWQQT 162
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV--GGDYDEAVAAARELAAEGPGAyYINQYDNPLNIEG-YGTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 163 GGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIP---------------------GIRRWPTEYLPGIF 221
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALArslaagrpvpvpvadtiadglGVGDEPGALALDLL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130347 222 NAsLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKA--NPDAVVVAIICD 281
Cdd:pfam00291 235 DE-YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGelKGGDRVVVVLTG 295
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
6-294 |
1.68e-77 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 240.63 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 6 QTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGD-VLIEATSGNTGIALAMIAALKG 84
Cdd:PLN02556 55 QLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKtTLIEPTSGNMGISLAFMAAMKG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 85 YRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEM-ANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQTG 163
Cdd:PLN02556 135 YKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELlESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 164 GRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTE-------YLPGIFNASLVDEVLDIHQRD 236
Cdd:PLN02556 215 GQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHitgngvgFKPDILDMDVMEKVLEVSSED 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 237 AENTMRELAVREGIFCGVSSGGAVAGALRVAK--ANPDAVVVAIICDRGDRYLSTGVFGE 294
Cdd:PLN02556 295 AVNMARELALKEGLMVGISSGANTVAALRLAKmpENKGKLIVTVHPSFGERYLSSVLFQE 354
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
6-292 |
3.55e-76 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 235.67 E-value: 3.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 6 QTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPG-DVLIEATSGNTGIALAMIAALKG 84
Cdd:PLN00011 13 ELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAARG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 85 YRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGK-LLDQFNNPDNPYAHYTTTGPEIWQQTG 163
Cdd:PLN00011 93 YKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGyIPQQFENPANPEIHYRTTGPEIWRDSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 164 GRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWP-------TEYLPGIFNASLVDEVLDIHQRD 236
Cdd:PLN00011 173 GKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPhliqgigSGIIPFNLDLTIVDEIIQVTGEE 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130347 237 AENTMRELAVREGIFCGVSSGGAVAGALRVAK--ANPDAVVVAIICDRGDRYLSTGVF 292
Cdd:PLN00011 253 AIETAKLLALKEGLLVGISSGAAAAAALKVAKrpENAGKLIVVIFPSGGERYLSTKLF 310
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
4-292 |
5.34e-76 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 238.52 E-value: 5.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPG-DVLIEATSGNTGIALAMIAAL 82
Cdd:PLN03013 117 VSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGkSVLVEPTSGNTGIGLAFIAAS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 83 KGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALE-MANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQ 161
Cdd:PLN03013 197 RGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEiLKNTPDAYMLQQFDNPANPKIHYETTGPEIWDD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 162 TGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTE-------YLPGIFNASLVDEVLDIHQ 234
Cdd:PLN03013 277 TKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKiqgigagFIPKNLDQKIMDEVIAISS 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130347 235 RDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDA-VVVAIICDRGDRYLSTGVF 292
Cdd:PLN03013 357 EEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAgKLIAVSLFASGRDIYTPRC 415
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
4-288 |
4.90e-42 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 149.76 E-value: 4.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 83
Cdd:PLN02356 47 LIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVT------KEQGMEGARDLALEmANRGEGKL-------------------- 137
Cdd:PLN02356 127 GCKCHVVIPDDVAIEKSQILEALGATVERVRpvsithKDHYVNIARRRALE-ANELASKRrkgsetdgihlektngcise 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 138 -----------------LDQFNNPDNPYAHYTTTGPEIWQQTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQP 200
Cdd:PLN02356 206 eekenslfsssctggffADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 201 -------------------EEGSSIP----------GIRRwpteyLPGIFNASLVDEVLDIHQRDAENTMRELAVREGIF 251
Cdd:PLN02356 286 pgsglfnkvtrgvmytreeAEGRRLKnpfdtitegiGINR-----LTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLF 360
|
330 340 350
....*....|....*....|....*....|....*...
gi 16130347 252 CGVSSGGAVAGALRVAKA-NPDAVVVAIICDRGDRYLS 288
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSlGPGHTIVTILCDSGMRHLS 398
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
9-279 |
7.30e-32 |
|
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: 121.85 E-value: 7.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIkpgdVLIEATSGNTGIALAMIAALKGYRMK 88
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 89 LLMP-DNMSQERRAAMRAYGAELILVtkeqgmEGARDLALEMANRgegkLLDQFN----NPDNPYAH--YTTTGPEIWQQ 161
Cdd:COG0498 141 VFVPeGKVSPGQLAQMLTYGAHVIAV------DGNFDDAQRLVKE----LAADEGlyavNSINPARLegQKTYAFEIAEQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 162 TGGRITHFVSSMGTTGTITGVSRFMRE-------QSKPvTIVGLQPE----------EGSSIPGIRRWPTeYLPG--IFN 222
Cdd:COG0498 211 LGRVPDWVVVPTGNGGNILAGYKAFKElkelgliDRLP-RLIAVQATgcnpiltafeTGRDEYEPERPET-IAPSmdIGN 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130347 223 ASLVDEVLDIHQR---------DAE--NTMRELAVREGIFCGVSSGGAVAGALRVAKA---NPDAVVVAII 279
Cdd:COG0498 289 PSNGERALFALREsggtavavsDEEilEAIRLLARREGIFVEPATAVAVAGLRKLREEgeiDPDEPVVVLS 359
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
9-280 |
2.38e-26 |
|
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: 105.75 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPD-NGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEikpgDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:cd01563 21 GNTPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 88 KLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMANRGEGKLldqfNNPDNPYAH--YTTTGPEIWQQTGGR 165
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAV--EGNFDDALRLVRELAEENWIYL----SNSLNPYRLegQKTIAFEIAEQLGWE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 166 I-THFVSSMGTTGTITGVSRFMREQ------SKPVTIVGLQPEEGSSI-PGIRRWPTEYLPG-----------IFNASLV 226
Cdd:cd01563 171 VpDYVVVPVGNGGNITAIWKGFKELkelgliDRLPRMVGVQAEGAAPIvRAFKEGKDDIEPVenpetiatairIGNPASG 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130347 227 DEVLDIHQR---------DAENT--MRELAVREGIFCGVSSGGAVAGALRVAKA---NPDAVVVAIIC 280
Cdd:cd01563 251 PKALRAVREsggtavavsDEEILeaQKLLARTEGIFVEPASAASLAGLKKLREEgiiDKGERVVVVLT 318
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
4-280 |
2.86e-20 |
|
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: 88.70 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIV----EAEKRGeikpgdvLIEATSGNTGIALAMI 79
Cdd:cd01562 11 IKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLslseEERAKG-------VVAASAGNHAQGVAYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 80 AALKGYRMKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMANRGEGKLLDQFNNPDnpyahyT-----TT 154
Cdd:cd01562 84 AKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLTFIHPFDDPD------ViagqgTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 155 GPEIWQQTGGRITHFVS-SMGttGTITGVSRFMREQSKPVTIVGLQPE----------EGSSIP---------GIR-RWP 213
Cdd:cd01562 156 GLEILEQVPDLDAVFVPvGGG--GLIAGIATAVKALSPNTKVIGVEPEgapamaqslaAGKPVTlpevdtiadGLAvKRP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130347 214 TEYLPGIFNAsLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIIC 280
Cdd:cd01562 234 GELTFEIIRK-LVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLS 299
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
11-280 |
5.50e-20 |
|
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: 88.17 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIV----EAEKRGeikpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslseEERARG-------VVAASAGNHAQGVAYAARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 87 MKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMANRgEGKLLDQfnnpdnPYAH------YTTTGPEIWQ 160
Cdd:COG1171 98 ATIVMPETAPAVKVAATRAYGAEVVLH--GDTYDDAEAAAAELAEE-EGATFVH------PFDDpdviagQGTIALEILE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 161 QTGGrITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSI--------------------------PGIRRWPt 214
Cdd:COG1171 169 QLPD-LDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMyrslaagepvtlpgvdtiadglavgrPGELTFE- 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130347 215 eylpgiFNASLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIIC 280
Cdd:COG1171 247 ------ILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLS 306
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
11-282 |
2.73e-19 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 86.29 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIV----EAEKRGeikpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRllneAQRQQG-------VITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 87 MKLLMPDNMSQERRAAMRAYGAELILVtkeqgmeGARDLALEMANRGEGKL-----LDQFNNPDnPYAHYTTTGPEIWQQ 161
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLY-------GGDALNAELAARRAAEQqgkvyISPYNDPQ-VIAGQGTIGMELVEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 162 TGGRITHFVsSMGTTGTITGVSRFMREQSKPVTIVGLQPEEG----SSIPGIRRWPTEYLPGIFNAS------------- 224
Cdd:PRK06815 166 QPDLDAVFV-AVGGGGLISGIATYLKTLSPKTEIIGCWPANSpslyTSLEAGEIVEVAEQPTLSDGTaggvepgaitfpl 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130347 225 ---LVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIICDR 282
Cdd:PRK06815 245 cqqLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGK 305
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
9-279 |
1.68e-16 |
|
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: 78.58 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPDNGS-EVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEikpgDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:TIGR00260 21 GVTPLFRAPALAANVGIkNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 88 KLLMP-DNMSQERRAAMRAYGAELILVTKEqgMEGARDLALEMANRGEGKLLDQFNNPdnPY--AHYTTTGPEIWQQTGG 164
Cdd:TIGR00260 97 VVLYPaGKISLGKLAQALGYNAEVVAIDGN--FDDAQRLVKQLFEDKPALGLNSANSI--PYrlEGQKTYAFEAVEQLGW 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 165 RI-THFVSSMGTTGTITGVSRFMRE------QSKPVTIvGLQPEEGSSIpgIRRW-----------PTEYLPG--IFNAS 224
Cdd:TIGR00260 173 EApDKVVVPVPNSGNFGAIWKGFKEkkmlglDSLPVKR-GIQAEGAADI--VRAFleggqwepietPETLSTAmdIGNPA 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130347 225 LVDEVLDIHQR---------DAE--NTMRELAVREGIFCGVSSGGAVAGALRVAK---ANPDAVVVAII 279
Cdd:TIGR00260 250 NWPRALEAFRRsngyaedlsDEEilEAIKLLAREEGYFVEPHSAVAVAALLKLVEkgtADPAERVVCAL 318
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
9-163 |
4.46e-14 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 71.28 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPDNG-SEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEikpgDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:PRK06381 14 GGTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 88 KLLMPDNMSQERRAAMRAYGAELILV--TKEQGMEGARDLALEM----ANRGEgklldqfNNPDNPYAHYTTTGPEIWQQ 161
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVdgKYEEAVERSRKFAKENgiydANPGS-------VNSVVDIEAYSAIAYEIYEA 162
|
..
gi 16130347 162 TG 163
Cdd:PRK06381 163 LG 164
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
11-201 |
1.09e-13 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 69.98 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDnGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKrgeikPGDVLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:PRK08246 24 TPVLEADGAGFG-PAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 91 MPDNMSQERRAAMRAYGAELILVTKE--QGMEGARDLAlemANRGeGKLLDQFNNPDNpYAHYTTTGPEIWQQTGGRITH 168
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAEyaDALEAAQAFA---AETG-ALLCHAYDQPEV-LAGAGTLGLEIEEQAPGVDTV 172
|
170 180 190
....*....|....*....|....*....|...
gi 16130347 169 FVsSMGTTGTITGVSRFMREQSKpvtIVGLQPE 201
Cdd:PRK08246 173 LV-AVGGGGLIAGIAAWFEGRAR---VVAVEPE 201
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
9-275 |
1.93e-13 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 69.76 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKlqrmgpdnGSEVWLKLEGNNPAGSVKDRAALSMIVE-AEKR-GEIKpgdvliEATSGNTGIALAMIAALKGYR 86
Cdd:PRK06450 57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYlAEKGiKQIS------EDSSGNAGASIAAYGAAAGIE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 87 MKLLMPDNMSQERRAAMRAYGAELILVtkeqgmEGARDlALEMANRGEGK------LLDQFNNPDNPYAHytttgpEIWQ 160
Cdd:PRK06450 123 VKIFVPETASGGKLKQIESYGAEVVRV------RGSRE-DVAKAAENSGYyyashvLQPQFRDGIRTLAY------EIAK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 161 QTGGRITHFV---SSMGT--TGTITGVSRFMR--EQSKPVTIVGLQPEEGS----SIPGIRRWPTEYLPGIFNA------ 223
Cdd:PRK06450 190 DLDWKIPNYVfipVSAGTllLGVYSGFKHLLDsgVISEMPKIVAVQTEQVSplcaKFKGISYTPPDKVTSIADAlvstrp 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130347 224 SLVDEVLDIHQRDAE----------NTMRELAvREGIFCGVSSGGAVAgALRVAKANPDAVV 275
Cdd:PRK06450 270 FLLDYMVKALSEYGEcivvsdneivEAWKELA-KKGLLVEYSSATVYA-AYKKYSVNDSVLV 329
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
4-275 |
4.15e-13 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 68.88 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGpdngseVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPgdvLIEATSGNTGIALAMIAALK 83
Cdd:PRK08813 33 LRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 84 GYRMKLLMPDNMSQERRAAMRAYGAELilvtKEQG--MEGARDLALEMANRGEGKLLDQFNNPDnPYAHYTTTGPEIWQQ 161
Cdd:PRK08813 104 GVQAITVMPHGAPQTKIAGVAHWGATV----RQHGnsYDEAYAFARELADQNGYRFLSAFDDPD-VIAGQGTVGIELAAH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 162 TGGRIthfVSSMGTTGTITGVSRFMREQSkpVTIVGLQPE--------------EGSSIPGIRRWPTEYLPGIFN----A 223
Cdd:PRK08813 179 APDVV---IVPIGGGGLASGVALALKSQG--VRVVGAQVEgvdsmarairgdlrEIAPVATLADGVKVKIPGFLTrrlcS 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16130347 224 SLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVV 275
Cdd:PRK08813 254 SLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAGRRVSGKRKCAVV 305
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
24-132 |
5.18e-13 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 68.10 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 24 GSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGdvLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAM 103
Cdd:PRK06110 35 GCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAM 112
|
90 100 110
....*....|....*....|....*....|.
gi 16130347 104 RAYGAELIlvtkEQG--MEGARDLALEMANR 132
Cdd:PRK06110 113 RALGAELI----EHGedFQAAREEAARLAAE 139
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
4-200 |
4.94e-12 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 65.56 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGeiKPGDVLIEATSGNTGIALAMIAALK 83
Cdd:PRK06608 17 IKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEmanrgEGKLLDQFNNPDNPYAHYTTTGPEIWQQTG 163
Cdd:PRK06608 95 GIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEE-----QGFYYIHPSDSDSTIAGAGTLCYEALQQLG 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 16130347 164 GRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQP 200
Cdd:PRK06608 170 FSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEP 206
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
9-113 |
6.01e-12 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 65.41 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPDNG-SEVWLKLEGNNPAGSVKDR---AALSMIVEAEKRGEIKPgdvlieaTSGNTGIALAMIAALKG 84
Cdd:PRK08197 78 GMTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARglaVGVSRAKELGVKHLAMP-------TNGNAGAAWAAYAARAG 150
|
90 100
....*....|....*....|....*....
gi 16130347 85 YRMKLLMPDNMSQERRAAMRAYGAELILV 113
Cdd:PRK08197 151 IRATIFMPADAPEITRLECALAGAELYLV 179
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
9-267 |
3.95e-11 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 63.29 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKlQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEikpgDVLIEATSGNTGIALAMIAALKGYRMK 88
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 89 LLMPDNMSQERRAAMRAYGAELIlVTKE---QGMEGARDLAlemanRGEGklLDQFNNPDNPYA--HYTTTGPEIWQQTG 163
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKII-RYGEsvdEAIEYAEELA-----RLNG--LYNVTPEYNIIGleGQKTIAFELWEEIN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 164 GriTHFVSSMGTTGTITGVSRFMREQSKPVTI------VGLQPEE----GSSIPGIRRWPTEY-LPGIF-----NASLVD 227
Cdd:PRK05638 212 P--THVIVPTGSGSYLYSIYKGFKELLEIGVIeeipklIAVQTERcnpiASEILGNKTKCNETkALGLYvknpvMKEYVS 289
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16130347 228 EVLDIHQRDA-----ENTMR--ELAVREGIFCGVSSGGAVAGALRVA 267
Cdd:PRK05638 290 EAIKESGGTAvvvneEEIMAgeKLLAKEGIFAELSSAVVMPALLKLG 336
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
2-267 |
9.16e-11 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 61.68 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 2 STLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAA---LSMIVEAEKRGEIkpgdvlIEATSGNTGIALAM 78
Cdd:PRK08638 19 QRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKGV------VACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 79 IAALKGYRMKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMAnRGEGK-LLDQFNNPDnPYAHYTTTGPE 157
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVL--HGDNFNDTIAKVEEIV-EEEGRtFIPPYDDPK-VIAGQGTIGLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 158 IWQQTGGRITHFVsSMGTTGTITGVSRFMREQSKPVTIVGLQPE---------EGSSIPGIRRWPT------EYLPGIFN 222
Cdd:PRK08638 169 ILEDLWDVDTVIV-PIGGGGLIAGIAVALKSINPTIHIIGVQSEnvhgmaasfYAGEITTHRTTGTladgcdVSRPGNLT 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16130347 223 ----ASLVDEVLDIHQRDAENTMRELAVREGIfcgVSSGgavAGALRVA 267
Cdd:PRK08638 248 yeivRELVDDIVLVSEDEIRNAMKDLIQRNKV---VTEG---AGALATA 290
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
11-202 |
1.26e-10 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 61.74 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIV----EAEKRGeikpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMArlpaEQLARG-------VITASAGNHAQGVALAAARLGVK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 87 MKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMANRGEGKLLDQFNNPDnPYAHYTTTGPEIWQQTGGRI 166
Cdd:PRK12483 111 AVIVMPRTTPQLKVDGVRAHGGEVVL--HGESFPDALAHALKLAEEEGLTFVPPFDDPD-VIAGQGTVAMEILRQHPGPL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 16130347 167 THFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEE 202
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDD 223
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
11-163 |
8.69e-09 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 55.99 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLqrmgpdnGSEVWLKLEGNNPAGSVKDRAALsmiVEAEKRGEIKPGDVLIEaTSGNTGIALAMIAALKGYRMKLL 90
Cdd:PRK08329 65 TPTVKR-------SIKVYFKLDYLQPTGSFKDRGTY---VTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 91 MPDNMSQERRAAMRAYGAELILVtkeqgmEGAR----DLALEMANRGEGKLLDQFNNPdnpyahYTTTGP-----EIWQQ 161
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFV------EGDRmevhEEAVKFSKRNNIPYVSHWLNP------YFLEGTktiayEIYEQ 201
|
..
gi 16130347 162 TG 163
Cdd:PRK08329 202 IG 203
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
24-203 |
1.77e-08 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 54.64 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 24 GSEVWLKLEGNNPAGSVKDRA---ALSMIVEAEKRGEIkpgdvlIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERR 100
Cdd:PRK07048 38 GAQVFFKCENFQRMGAFKFRGaynALSQFSPEQRRAGV------VTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 101 AAMRAYGAELILV--TKEQGMEGARDLALEmanRGEgKLLDQFNNPDnPYAHYTTTGPEIWQQTGGRITHFVsSMGTTGT 178
Cdd:PRK07048 112 AATRGYGGEVVTYdrYTEDREEIGRRLAEE---RGL-TLIPPYDHPH-VIAGQGTAAKELFEEVGPLDALFV-CLGGGGL 185
|
170 180
....*....|....*....|....*
gi 16130347 179 ITGVSRFMREQSKPVTIVGLQPEEG 203
Cdd:PRK07048 186 LSGCALAARALSPGCKVYGVEPEAG 210
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
11-117 |
3.36e-08 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 53.82 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAA----LSMIVEAEKRGeikpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGAtnalLSLSAQERARG-------VVTASTGNHGRALAYAARALGIR 92
|
90 100 110
....*....|....*....|....*....|....*
gi 16130347 87 ----MKLLMPDNmsqeRRAAMRAYGAELILVTKEQ 117
Cdd:PRK07476 93 aticMSRLVPAN----KVDAIRALGAEVRIVGRSQ 123
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
11-206 |
1.02e-07 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 53.00 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRgEIKPGdvLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 91 MPDNMSQERRAAMRAYGAELILV--TKEQGMEGARDLALEmanrgEGK-LLDQFNNPDnPYAHYTTTGPEIWQQTGGRIT 167
Cdd:PLN02550 187 MPVTTPEIKWQSVERLGATVVLVgdSYDEAQAYAKQRALE-----EGRtFIPPFDHPD-VIAGQGTVGMEIVRQHQGPLH 260
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130347 168 HFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSI 206
Cdd:PLN02550 261 AIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAM 299
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
9-108 |
1.92e-06 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 49.04 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 9 GNTPLVKLQRMGPDNG--SEVWLKLEGNNPAGSVKDR---AALSMIVEAEKRGeiKPGDVLIEATSGNTGIALAMIAALK 83
Cdd:PLN02569 132 GNSNLFWAERLGKEFLgmNDLWVKHCGISHTGSFKDLgmtVLVSQVNRLRKMA--KPVVGVGCASTGDTSAALSAYCAAA 209
|
90 100
....*....|....*....|....*.
gi 16130347 84 GYRMKLLMP-DNMSQERRAAMRAYGA 108
Cdd:PLN02569 210 GIPSIVFLPaDKISIAQLVQPIANGA 235
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
52-132 |
6.49e-06 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 47.18 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 52 AEKRGEIkpgdVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILVtkeqgmEGARDLALEMAN 131
Cdd:PRK08206 111 REKLGDI----TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT------DGNYDDSVRLAA 180
|
.
gi 16130347 132 R 132
Cdd:PRK08206 181 Q 181
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
10-201 |
2.12e-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: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 10 NTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVlIEATSGNTGIALAMIAALKGYRMKL 89
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHV-VCSSGGNAGLAAAYAARKLGVPCTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 90 LMPDNMSQERRAAMRAYGAELILVTKEQGmEGARDLALEMANRGEGKL-LDQFNNPDNPYAHyTTTGPEIWQQ--TGGRI 166
Cdd:cd06448 80 VVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAENDPGPVyVHPFDDPLIWEGH-SSMVDEIAQQlqSQEKV 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 16130347 167 THFVSSMGTTGTITGVSRFMRE-QSKPVTIVGLQPE 201
Cdd:cd06448 158 DAIVCSVGGGGLLNGIVQGLERnGWGDIPVVAVETE 193
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
1-205 |
5.66e-05 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 44.41 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 1 MSTLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRgEIKPGDVLieATSGNTGIALAMIA 80
Cdd:PRK08639 16 AKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDE-ELAAGVVC--ASAGNHAQGVAYAC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 81 ALKGYRMKLLMPDNMSQERRAAMRAYGA---ELILV--TKEQGMEGARDLALEmanrgEGK-LLDQFNNPDNpYAHYTTT 154
Cdd:PRK08639 93 RHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVgdTFDDSAAAAQEYAEE-----TGAtFIPPFDDPDV-IAGQGTV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130347 155 GPEIWQQTG--GRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSS 205
Cdd:PRK08639 167 AVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAAS 219
|
|
| MDR2 |
cd08268 |
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
45-139 |
6.92e-05 |
|
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. 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.
Pssm-ID: 176229 [Multi-domain] Cd Length: 328 Bit Score: 43.74 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 45 ALSMIVEAekrGEIKPGD-VLIEATSGNTGIALAMIAALKGYRMKLLmpdNMSQERRAAMRAYGAELILVTKEQgmegar 123
Cdd:cd08268 132 AYGALVEL---AGLRPGDsVLITAASSSVGLAAIQIANAAGATVIAT---TRTSEKRDALLALGAAHVIVTDEE------ 199
|
90
....*....|....*.
gi 16130347 124 DLALEMANRGEGKLLD 139
Cdd:cd08268 200 DLVAEVLRITGGKGVD 215
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
24-289 |
1.32e-04 |
|
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: 42.91 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 24 GSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKpgdVLIEATSGNTGIALAMIAALKGYRMKLLM--PDNMSQE-RR 100
Cdd:cd06446 49 GAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR---VIAETGAGQHGVATATACALFGLECEIYMgaVDVERQPlNV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 101 AAMRAYGAELILVTKEQGMEG-ARDLALEmanrgegkllDQFNNPDN------------PYA-----HYTTTGPEIWQQ- 161
Cdd:cd06446 126 FRMELLGAEVVPVPSGSGTLKdAISEAIR----------DWVTNVEDthyllgsvvgphPYPnmvrdFQSVIGEEAKKQi 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 162 --------------------TGGRITHFVS-------------------------SMGTTGTITGVSRFMreqskpvtiv 196
Cdd:cd06446 196 lekegelpdvviacvgggsnAAGLFYPFINdkdvkligveaggcgletgghaaylFGGTAGVLHGLKMYT---------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 197 gLQPEEGSSIP------GIRrwpteYlPGI--FNASLVD----EVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGAL 264
Cdd:cd06446 266 -LQDEDGQIVPphsisaGLD-----Y-PGVgpEHAYLKDsgrvEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAI 338
|
330 340
....*....|....*....|....*.
gi 16130347 265 RVA-KANPDAVVVAIICDRGDRYLST 289
Cdd:cd06446 339 KLAkKLGKEKVIVVNLSGRGDKDLQT 364
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
3-201 |
1.50e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 42.96 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 3 TLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAA---LSMIVEAEK-RGeikpgdvLIEATSGNTGIALAM 78
Cdd:PRK07334 16 RLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGAlnkLLLLTEEERaRG-------VIAMSAGNHAQGVAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 79 IAALKGYRMKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMANRGEGKLLDQFNNPDnPYAHYTTTGPEI 158
Cdd:PRK07334 89 HAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVL--HGETLDEARAHARELAEEEGLTFVHPYDDPA-VIAGQGTVALEM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130347 159 WQQTGGrITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPE 201
Cdd:PRK07334 166 LEDAPD-LDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
11-114 |
3.24e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 42.11 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 11 TPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKpgdVLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTR---IIAETGAGQHGVATATACALFGLKCTIF 348
|
90 100
....*....|....*....|....*..
gi 16130347 91 M--PDNMSQERRAA-MRAYGAELILVT 114
Cdd:PRK13803 349 MgeEDIKRQALNVErMKLLGANVIPVL 375
|
|
| Zn_ADH2 |
cd08256 |
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ... |
52-125 |
1.13e-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: 40.08 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130347 52 AEKRGEIKPGDVLIEATSGNTGiaLAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELIL-VTKEQGMEGARDL 125
Cdd:cd08256 166 AVDRANIKFDDVVVLAGAGPLG--LGMIGAARLKNPKKLIVLDLKDERLALARKFGADVVLnPPEVDVVEKIKEL 238
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
4-197 |
3.92e-03 |
|
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: 38.24 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 4 LEQTIGNTPLVKLQRMGPDNGSEVWLKLE--------GNnpagsvKDRAALSMIVEAEKRGEikpgDVLIeaTSG----N 71
Cdd:COG2515 5 LPLAFLPTPLQPLPRLSAALGVELWIKRDdltgpaigGN------KTRKLEYLLADALAQGA----DTLV--TFGgaqsN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130347 72 TGIALAMIAALKGYRMKLLMPDNMSQERR---AAMRAYGAELILVTKEQGmegaRDLALEMANRGEgKLLDQFNNP---- 144
Cdd:COG2515 73 HARATAAAAAKLGLKCVLVLRGEEPTPLNgnlLLDRLLGAELHFVSRGEY----RDRDEAMEAVAA-ELRARGGKPyvip 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130347 145 ---DNPYAH--YTTTGPEIWQQ---TGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVG 197
Cdd:COG2515 148 eggSNPLGAlgYVEAAAELAAQlaeLGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIG 208
|
|
| |
