|
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: 638.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 1 MNTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIA 80
Cdd:PRK11761 3 YPTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 81 ALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRGEGKLLDQFNNPDNPYAHYTTTGPEIWQ 160
Cdd:PRK11761 83 AIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEIWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 161 QTAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRRWPAEYMPGIFNASLVDAVLDIHQQDAENT 240
Cdd:PRK11761 163 QTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDVSQQEAENT 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 647263415 241 MRQLAVREGIFCGVSSGGAVAGALRIARENPGAVVVAIVCDRGDRYLSTGVFGE 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: 540.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 3 TLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAAL 82
Cdd:TIGR01138 1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 83 KGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01138 81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 163 AGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRRWPAEYMPGIFNASLVDAVLDIHQQDAENTMR 242
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPGIRRWPTEYLPGIFDASLVDRVLDIHQRDAENTMR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 647263415 243 QLAVREGIFCGVSSGGAVAGALRIARENPGAVVVAIVCDRGDRYLSTGVF 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 |
4.19e-174 |
|
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: 483.32 E-value: 4.19e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 4 LEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAALK 83
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQR-GEGKLLDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 163 AGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPG-------IRRWPAEYMPGIFNASLVDAVLDIHQQ 235
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGgepgphkIQGIGAGFIPKILDLSLIDEVITVSDE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 647263415 236 DAENTMRQLAVREGIFCGVSSGGAVAGALRIAR--ENPGAVVVAIVCDRGDRYLSTGVF 292
Cdd:TIGR01136 241 DAIETARRLAREEGILVGISSGAAVAAALKLAKrlENADKVIVAILPDTGERYLSTGLF 299
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-289 |
3.89e-168 |
|
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: 468.37 E-value: 3.89e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 1 MNTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIA 80
Cdd:COG0031 4 YDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 81 ALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRGEG-KLLDQFNNPDNPYAHYTTTGPEIW 159
Cdd:COG0031 84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGaFWPNQFENPANPEAHYETTGPEIW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 160 QQTAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPG-------IRRWPAEYMPGIFNASLVDAVLDI 232
Cdd:COG0031 164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGgepgphkIEGIGAGFVPKILDPSLIDEVITV 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 647263415 233 HQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARE-NPGAVVVAIVCDRGDRYLST 289
Cdd:COG0031 244 SDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRlGPGKTIVTILPDSGERYLST 301
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
9-288 |
9.56e-147 |
|
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: 413.83 E-value: 9.56e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAALKGYRMK 88
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 89 LLMPDNMSQERRAAMRAYGAELILVTKEQ--GMEGARDLALEMAQRGEG-KLLDQFNNPDNPYAHYTTTGPEIWQQTAGR 165
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNaFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 166 ITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEE----------GSSIPGIRrwpAEYMPGIFNASLVDAVLDIHQQ 235
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGsvlfsggppgPHKIEGIG---AGFIPENLDRSLIDEVVRVSDE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 647263415 236 DAENTMRQLAVREGIFCGVSSGGAVAGALRIAREN-PGAVVVAIVCDRGDRYLS 288
Cdd:cd01561 238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTILPDSGERYLS 291
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
5-292 |
2.80e-122 |
|
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: 352.05 E-value: 2.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 5 EQTIGNTPLVKLQRLGPDNGsEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAALKG 84
Cdd:TIGR01139 2 SELIGNTPLVRLNRIEGCNA-NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 85 YRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRGEGK--LLDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01139 81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyfMLQQFENPANPEIHRKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 163 AGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPG-------IRRWPAEYMPGIFNASLVDAVLDIHQQ 235
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGgkpgphkIQGIGAGFIPKNLNRSVIDEVITVSDE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 647263415 236 DAENTMRQLAVREGIFCGVSSGGAVAGALRIA-RENPGAVVVAIVCDRGDRYLSTGVF 292
Cdd:TIGR01139 241 EAIETARRLAAEEGILVGISSGAAVAAALKLAkRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
2-289 |
4.83e-103 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 304.48 E-value: 4.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 2 NTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAA 81
Cdd:PRK10717 5 EDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 82 LKGYRMKLLMPDNMSQERRAAMRAYGAELILV------TKEQGMEGARDLALEMAQRGEGK--LLDQFNNPDNPYAHYTT 153
Cdd:PRK10717 85 ARGYKTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPNGaiWANQFDNPANREAHYET 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 154 TGPEIWQQTAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPE---------------EGSSIP---GIRRwpae 215
Cdd:PRK10717 165 TGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTgsalysyyktgelkaEGSSITegiGQGR---- 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263415 216 yMPGIFNASLVDAVLDIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIAREN-PGAVVVAIVCDRGDRYLST 289
Cdd:PRK10717 241 -ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELgPGHTIVTILCDSGERYQSK 314
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
8-292 |
2.62e-90 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 271.80 E-value: 2.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 8 IGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGD-VLIEATSGNTGIALAMIAALKGYR 86
Cdd:PLN02565 13 IGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGEsVLIEPTSGNTGIGLAFMAAAKGYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 87 MKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEM-AQRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQTAGR 165
Cdd:PLN02565 93 LIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEIlAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 166 ITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRRWP-------AEYMPGIFNASLVDAVLDIHQQDAE 238
Cdd:PLN02565 173 VDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPhkiqgigAGFIPGVLDVDLLDEVVQVSSDEAI 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 647263415 239 NTMRQLAVREGIFCGVSSGGAVAGALRIAR--ENPGAVVVAIVCDRGDRYLSTGVF 292
Cdd:PLN02565 253 ETAKLLALKEGLLVGISSGAAAAAAIKIAKrpENAGKLIVVIFPSFGERYLSSVLF 308
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
4-289 |
2.15e-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: 260.98 E-value: 2.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 4 LEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAALK 83
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVTK--EQG-MEGARdlaLEMAQRgegkLLD---------QFNNPDNPYAHY 151
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEpdETGgYLGTR---IARVRE----LLAsipdaywpnQYANPDNPRAHY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 152 TTTGPEIWQQTaGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQpEEGSSI----PGIRRWP---AEYMPGIFNAS 224
Cdd:TIGR03945 154 HGTGREIARAF-PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVD-AVGSVIfggpPGRRHIPglgASVVPELLDES 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263415 225 LVDAVldIHQQDAENTM--RQLAVREGIFCGVSSGGAVAGALRIARENP-GAVVVAIVCDRGDRYLST 289
Cdd:TIGR03945 232 LIDDV--VHVPEYDTVAgcRRLARREGILAGGSSGTVVAAIKRLLPRIPeGSTVVAILPDRGERYLDT 297
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
8-288 |
3.60e-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: 265.51 E-value: 3.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 8 IGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:TIGR01137 9 IGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 88 KLLMPDNMSQERRAAMRAYGAElILVTKEQGMEGARDLALEMAQRGEGKL-----LDQFNNPDNPYAHYTTTGPEIWQQT 162
Cdd:TIGR01137 89 IIVLPEKMSSEKVDVLRALGAE-IVRTPTAAAFDSPESHIGVAKRLVREIpgahiLDQYRNPSNPLAHYDTTGPEILEQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 163 AGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPE-----EGSSIPGIRRWPAE-------YMPGIFNASLVDAVL 230
Cdd:TIGR01137 168 EGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEgsilaQPEELNQTGRTPYKvegigydFIPTVLDRKVVDEWI 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 231 DIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARE--NPGAVVVAIVCDRGDRYLS 288
Cdd:TIGR01137 248 KTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDelQEGQRCVVLLPDSIRNYMT 307
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
11-282 |
4.38e-83 |
|
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: 250.51 E-value: 4.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIqPGDVLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 91 MPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMAQRGEG-KLLDQFNNPDNPYAHYtTTGPEIWQQTAG-RITH 168
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLV--PGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 169 FVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEegssipgirrwpaeympgifnaslvdaVLDIHQQDAENTMRQLAVRE 248
Cdd:cd00640 157 VVVPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------VVTVSDEEALEAIRLLAREE 209
|
250 260 270
....*....|....*....|....*....|....*
gi 647263415 249 GIFCGVSSGGAVAGALRIARE-NPGAVVVAIVCDR 282
Cdd:cd00640 210 GILVEPSSAAALAAALKLAKKlGKGKTVVVILTGG 244
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
6-294 |
1.12e-81 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 251.42 E-value: 1.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 6 QTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGD-VLIEATSGNTGIALAMIAALKG 84
Cdd:PLN02556 55 QLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKtTLIEPTSGNMGISLAFMAAMKG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 85 YRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRGEGK-LLDQFNNPDNPYAHYTTTGPEIWQQTA 163
Cdd:PLN02556 135 YKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAfMLQQFSNPANTQVHFETTGPEIWEDTL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 164 GRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRRWPAE-------YMPGIFNASLVDAVLDIHQQD 236
Cdd:PLN02556 215 GQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHitgngvgFKPDILDMDVMEKVLEVSSED 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 237 AENTMRQLAVREGIFCGVSSGGAVAGALRIAR--ENPGAVVVAIVCDRGDRYLSTGVFGE 294
Cdd:PLN02556 295 AVNMARELALKEGLMVGISSGANTVAALRLAKmpENKGKLIVTVHPSFGERYLSSVLFQE 354
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
2-292 |
4.83e-79 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 242.99 E-value: 4.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 2 NTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPG-DVLIEATSGNTGIALAMIA 80
Cdd:PLN00011 9 NDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 81 ALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRGEGK-LLDQFNNPDNPYAHYTTTGPEIW 159
Cdd:PLN00011 89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGyIPQQFENPANPEIHYRTTGPEIW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 160 QQTAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRRWP-------AEYMPGIFNASLVDAVLDI 232
Cdd:PLN00011 169 RDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPhliqgigSGIIPFNLDLTIVDEIIQV 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263415 233 HQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIAR--ENPGAVVVAIVCDRGDRYLSTGVF 292
Cdd:PLN00011 249 TGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKrpENAGKLIVVIFPSGGERYLSTKLF 310
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
4-281 |
5.60e-78 |
|
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: 239.13 E-value: 5.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 4 LEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEkrgEIQPGDVLIEATSGNTGIALAMIAALK 83
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 84 GYRMKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMAQRGEGK-LLDQFNNPDNPYAhYTTTGPEIWQQT 162
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV--GGDYDEAVAAARELAAEGPGAyYINQYDNPLNIEG-YGTIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 163 AGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRR--------WPAEYMPGI---FNAS------- 224
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAagrpvpvpVADTIADGLgvgDEPGalaldll 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263415 225 --LVDAVLDIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARE--NPGAVVVAIVCD 281
Cdd:pfam00291 235 deYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGelKGGDRVVVVLTG 295
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
2-292 |
1.76e-76 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 240.06 E-value: 1.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 2 NTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPG-DVLIEATSGNTGIALAMIA 80
Cdd:PLN03013 115 DNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGkSVLVEPTSGNTGIGLAFIA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 81 ALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMAQRG-EGKLLDQFNNPDNPYAHYTTTGPEIW 159
Cdd:PLN03013 195 ASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTpDAYMLQQFDNPANPKIHYETTGPEIW 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 160 QQTAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSIPGIRRWP-------AEYMPGIFNASLVDAVLDI 232
Cdd:PLN03013 275 DDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPhkiqgigAGFIPKNLDQKIMDEVIAI 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263415 233 HQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIAR--ENPGAvVVAIVCDRGDRYLSTGVF 292
Cdd:PLN03013 355 SSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKrpENAGK-LIAVSLFASGRDIYTPRC 415
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
2-288 |
2.20e-43 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 153.61 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 2 NTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVLIEATSGNTGIALAMIAA 81
Cdd:PLN02356 45 NGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 82 LKGYRMKLLMPDNMSQERRAAMRAYGAELILVT------KEQGMEGARDLALE----MAQRGE----------------- 134
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVRpvsithKDHYVNIARRRALEanelASKRRKgsetdgihlektngcis 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 135 ---------------GKLLDQFNNPDNPYAHYTTTGPEIWQQTAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQ 199
Cdd:PLN02356 205 eeekenslfsssctgGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLID 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 200 P-------------------EEGSSIP----------GIRRWPAEympgiFNASLVDAVLDIHQQDAENTMRQLAVREGI 250
Cdd:PLN02356 285 PpgsglfnkvtrgvmytreeAEGRRLKnpfdtitegiGINRLTQN-----FLMAKLDGAFRGTDKEAVEMSRYLLKNDGL 359
|
330 340 350
....*....|....*....|....*....|....*....
gi 647263415 251 FCGVSSGGAVAGALRIARE-NPGAVVVAIVCDRGDRYLS 288
Cdd:PLN02356 360 FVGSSSAMNCVGAVRVAQSlGPGHTIVTILCDSGMRHLS 398
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
9-279 |
5.10e-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: 122.23 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIqpgdVLIEATSGNTGIALAMIAALKGYRMK 88
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 89 LLMP-DNMSQERRAAMRAYGAELILVtkeqgmEGARDLALEMAQRgegkLLDQFN----NPDNPYAH--YTTTGPEIWQQ 161
Cdd:COG0498 141 VFVPeGKVSPGQLAQMLTYGAHVIAV------DGNFDDAQRLVKE----LAADEGlyavNSINPARLegQKTYAFEIAEQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 162 TAGRITHFVSSMGTTGTITGVSRFLRE-------QSKPvAIVGLQPE----------EGSSIPGIRRwPAEYMPGIFN-- 222
Cdd:COG0498 211 LGRVPDWVVVPTGNGGNILAGYKAFKElkelgliDRLP-RLIAVQATgcnpiltafeTGRDEYEPER-PETIAPSMDIgn 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263415 223 -ASLVDAVLDIHQ----------QDAENTMRQLAVREGIFCGVSSGGAVAGALRIARE---NPGAVVVAIV 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 |
3.28e-27 |
|
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: 108.06 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPD-NGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEiqpgDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:cd01563 21 GNTPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 88 KLLMPDNMSQERRAAMRAYGAELILVtkeqgmEGARDLALEMAQRGEGKLLDQFNNPDNPYAH--YTTTGPEIWQQTAGR 165
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAV------EGNFDDALRLVRELAEENWIYLSNSLNPYRLegQKTIAFEIAEQLGWE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 166 I-THFVSSMGTTGTITGVSRFLREQ------SKPVAIVGLQPEEGSSI-PGIRRWPAEYMP---------GIFNASLVDA 228
Cdd:cd01563 171 VpDYVVVPVGNGGNITAIWKGFKELkelgliDRLPRMVGVQAEGAAPIvRAFKEGKDDIEPvenpetiatAIRIGNPASG 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263415 229 --VLDIHQQ---------DAENT--MRQLAVREGIFCGVSSGGAVAGALRIARE---NPGAVVVAIVC 280
Cdd:cd01563 251 pkALRAVREsggtavavsDEEILeaQKLLARTEGIFVEPASAASLAGLKKLREEgiiDKGERVVVVLT 318
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
11-280 |
6.00e-21 |
|
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: 90.87 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIV----EAEKRGeiqpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslseEERARG-------VVAASAGNHAQGVAYAARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 87 MKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMAQRGEGKLLDQFNNPDnPYAHYTTTGPEIWQQtAGRI 166
Cdd:COG1171 98 ATIVMPETAPAVKVAATRAYGAEVVLH--GDTYDDAEAAAAELAEEEGATFVHPFDDPD-VIAGQGTIALEILEQ-LPDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 167 THFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSI--------------------------PGIRRWPAeympgi 220
Cdd:COG1171 174 DAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMyrslaagepvtlpgvdtiadglavgrPGELTFEI------ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 221 fNASLVDAVLDIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARENPGAVVVAIVC 280
Cdd:COG1171 248 -LRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLS 306
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
4-280 |
9.05e-21 |
|
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: 90.24 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 4 LEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIV----EAEKRGeiqpgdvLIEATSGNTGIALAMI 79
Cdd:cd01562 11 IKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLslseEERAKG-------VVAASAGNHAQGVAYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 80 AALKGYRMKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMAQRGEGKLLDQFNNPDnpyahyT-----TT 154
Cdd:cd01562 84 AKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLTFIHPFDDPD------ViagqgTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 155 GPEIWQQTAGRITHFVS-SMGttGTITGVSRFLREQSKPVAIVGLQPE----------EGSSIP---------GIR-RWP 213
Cdd:cd01562 156 GLEILEQVPDLDAVFVPvGGG--GLIAGIATAVKALSPNTKVIGVEPEgapamaqslaAGKPVTlpevdtiadGLAvKRP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647263415 214 AEYMPGIFNAsLVDAVLDIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARENPGAVVVAIVC 280
Cdd:cd01562 234 GELTFEIIRK-LVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLS 299
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
11-282 |
3.40e-19 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 85.90 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIV----EAEKRGeiqpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRllneAQRQQG-------VITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 87 MKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMAQRGEGKLLDQFNNPDnPYAHYTTTGPEIWQQTAGRI 166
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLY--GGDALNAELAARRAAEQQGKVYISPYNDPQ-VIAGQGTIGMELVEQQPDLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 167 THFVsSMGTTGTITGVSRFLREQSKPVAIVGLQPEEG----SSIPGIRRWPAEYMPGIFNAS----------------LV 226
Cdd:PRK06815 171 AVFV-AVGGGGLISGIATYLKTLSPKTEIIGCWPANSpslyTSLEAGEIVEVAEQPTLSDGTaggvepgaitfplcqqLI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 647263415 227 DAVLDIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARENPGAVVVAIVCDR 282
Cdd:PRK06815 250 DQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGK 305
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
9-279 |
3.37e-15 |
|
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: 74.73 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPDNGS-EVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEiqpgDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:TIGR00260 21 GVTPLFRAPALAANVGIkNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 88 KLLMP-DNMSQERRAAMRAYGAELILVTKEqgMEGARDLALEMAQRGEGKLLDQFNNPdnPY--AHYTTTGPEIWQQTAG 164
Cdd:TIGR00260 97 VVLYPaGKISLGKLAQALGYNAEVVAIDGN--FDDAQRLVKQLFEDKPALGLNSANSI--PYrlEGQKTYAFEAVEQLGW 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 165 RI-THFVSSMGTTGTITGVSRFLRE------QSKPVAIvGLQPEEGSSIpgIRRW-----------PAEYMPG--IFNAS 224
Cdd:TIGR00260 173 EApDKVVVPVPNSGNFGAIWKGFKEkkmlglDSLPVKR-GIQAEGAADI--VRAFleggqwepietPETLSTAmdIGNPA 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647263415 225 LVDAVLDIHQQ---------DAE--NTMRQLAVREGIFCGVSSGGAVAGALRIARE---NPGAVVVAIV 279
Cdd:TIGR00260 250 NWPRALEAFRRsngyaedlsDEEilEAIKLLAREEGYFVEPHSAVAVAALLKLVEKgtaDPAERVVCAL 318
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
9-129 |
2.51e-14 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 72.05 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPDNG-SEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEiqpgDVLIEATSGNTGIALAMIAALKGYRM 87
Cdd:PRK06381 14 GGTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 647263415 88 KLLMPDNMSQERRAAMRAYGAELILV--TKEQGMEGARDLALEM 129
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVdgKYEEAVERSRKFAKEN 133
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
17-132 |
9.95e-14 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 70.41 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 17 QRLGpdngSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGdvLIEATSGNTGIALAMIAALKGYRMKLLMPDNMS 96
Cdd:PRK06110 32 ERLG----CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNS 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 647263415 97 QERRAAMRAYGAELIlvtkEQG--MEGARDLALEMAQR 132
Cdd:PRK06110 106 VEKNAAMRALGAELI----EHGedFQAAREEAARLAAE 139
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
4-275 |
7.99e-13 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 68.11 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 4 LEQTIGNTPLVKLQRLGpdngseVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPgdvLIEATSGNTGIALAMIAALK 83
Cdd:PRK08813 33 LRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 84 GYRMKLLMPDNMSQERRAAMRAYGAELilvtKEQG--MEGARDLALEMAQRGEGKLLDQFNNPDnPYAHYTTTGPEIwqq 161
Cdd:PRK08813 104 GVQAITVMPHGAPQTKIAGVAHWGATV----RQHGnsYDEAYAFARELADQNGYRFLSAFDDPD-VIAGQGTVGIEL--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 162 TAGRITHFVSSMGTTGTITGVSRFLREQSkpVAIVGLQPE--------------EGSSIPGIRRWPAEYMPGIFN----A 223
Cdd:PRK08813 176 AAHAPDVVIVPIGGGGLASGVALALKSQG--VRVVGAQVEgvdsmarairgdlrEIAPVATLADGVKVKIPGFLTrrlcS 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 647263415 224 SLVDAVLDIHQQDAENTMRQLAVREGIFCGVSSGGAVAGALRIARENPGAVV 275
Cdd:PRK08813 254 SLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAGRRVSGKRKCAVV 305
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
9-113 |
8.46e-13 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 68.10 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPDNG-SEVWVKLEGNNPAGSVKDR---AALSMIVEAEKRGEIQPgdvlieaTSGNTGIALAMIAALKG 84
Cdd:PRK08197 78 GMTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARglaVGVSRAKELGVKHLAMP-------TNGNAGAAWAAYAARAG 150
|
90 100
....*....|....*....|....*....
gi 647263415 85 YRMKLLMPDNMSQERRAAMRAYGAELILV 113
Cdd:PRK08197 151 IRATIFMPADAPEITRLECALAGAELYLV 179
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
9-300 |
2.76e-12 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 66.76 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKlQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEiqpgDVLIEATSGNTGIALAMIAALKGYRMK 88
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 89 LLMPDNMSQERRAAMRAYGAELIlVTKE---QGMEGARDLAlemaqRGEGklLDQFNNPDNPYA--HYTTTGPEIWQQTA 163
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKII-RYGEsvdEAIEYAEELA-----RLNG--LYNVTPEYNIIGleGQKTIAFELWEEIN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 164 GriTHFVSSMGTTGTITGVSRFLREQSKPVAI------VGLQPEE----GSSIPGIR-RWPAEYMPGIF-----NASLVD 227
Cdd:PRK05638 212 P--THVIVPTGSGSYLYSIYKGFKELLEIGVIeeipklIAVQTERcnpiASEILGNKtKCNETKALGLYvknpvMKEYVS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 228 AVLDIHQQDA-----ENTMR--QLAVREGIFCGVSSGGAVAGALRIARE---NPGAVVVAIVCDRGDRylSTGVFGEEHF 297
Cdd:PRK05638 290 EAIKESGGTAvvvneEEIMAgeKLLAKEGIFAELSSAVVMPALLKLGEEgyiEKGDKVVLVVTGSGLK--GYGEGGREKF 367
|
...
gi 647263415 298 SQG 300
Cdd:PRK05638 368 TIG 370
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
11-201 |
4.46e-12 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 65.36 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDnGSEVWVKLEGNNPAGSVKDRAALSMIVEAEkrgeiQPGDVLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:PRK08246 24 TPVLEADGAGFG-PAPVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 91 MPDNMSQERRAAMRAYGAELILVTKE--QGMEGARDLAlemAQRGeGKLLDQFNNPDNpYAHYTTTGPEIWQQTAGRITH 168
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAEyaDALEAAQAFA---AETG-ALLCHAYDQPEV-LAGAGTLGLEIEEQAPGVDTV 172
|
170 180 190
....*....|....*....|....*....|...
gi 647263415 169 FVsSMGTTGTITGVSRFLREQSKpvaIVGLQPE 201
Cdd:PRK08246 173 LV-AVGGGGLIAGIAAWFEGRAR---VVAVEPE 201
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
2-181 |
1.61e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 64.02 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 2 NTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGeiQPGDVLIEATSGNTGIALAMIAA 81
Cdd:PRK06608 15 NRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 82 LKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEmaqrgEGKLLDQFNNPDNPYAHYTTTGPEIWQQ 161
Cdd:PRK06608 93 LFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEE-----QGFYYIHPSDSDSTIAGAGTLCYEALQQ 167
|
170 180
....*....|....*....|
gi 647263415 162 TAGRITHFVSSMGTTGTITG 181
Cdd:PRK06608 168 LGFSPDAIFASCGGGGLISG 187
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
9-271 |
2.23e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 63.60 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKlqrlgpdnGSEVWVKLEGNNPAGSVKDRAALSMIVE-AEKR-GEIQpgdvliEATSGNTGIALAMIAALKGYR 86
Cdd:PRK06450 57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYlAEKGiKQIS------EDSSGNAGASIAAYGAAAGIE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 87 MKLLMPDNMSQERRAAMRAYGAELILVtkeqgmEGARDLALEMAQRGEGK-----LLDQFNNPDNPYAHytttgpEIWQQ 161
Cdd:PRK06450 123 VKIFVPETASGGKLKQIESYGAEVVRV------RGSREDVAKAAENSGYYyashvLQPQFRDGIRTLAY------EIAKD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 162 TAGRITHFV---SSMGT--TGTITGVSRFLR--EQSKPVAIVGLQPEEGS----SIPGIRRWPAEYMPGIFNA------S 224
Cdd:PRK06450 191 LDWKIPNYVfipVSAGTllLGVYSGFKHLLDsgVISEMPKIVAVQTEQVSplcaKFKGISYTPPDKVTSIADAlvstrpF 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 647263415 225 LVDAVLDIHQQDAE----------NTMRQLAvREGIFCGVSSGGAVAGALRIARENP 271
Cdd:PRK06450 271 LLDYMVKALSEYGEcivvsdneivEAWKELA-KKGLLVEYSSATVYAAYKKYSVNDS 326
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
3-201 |
1.08e-10 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 61.29 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 3 TLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAA---LSMIVEAEKRGEIqpgdvlIEATSGNTGIALAMI 79
Cdd:PRK08638 20 RLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKGV------VACSAGNHAQGVALS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 80 AALKGYRMKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMAQRgEGK-LLDQFNNPDnPYAHYTTTGPEI 158
Cdd:PRK08638 94 CALLGIDGKVVMPKGAPKSKVAATCGYGAEVVL--HGDNFNDTIAKVEEIVEE-EGRtFIPPYDDPK-VIAGQGTIGLEI 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 647263415 159 WQQTAGRITHFVsSMGTTGTITGVSRFLREQSKPVAIVGLQPE 201
Cdd:PRK08638 170 LEDLWDVDTVIV-PIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
11-202 |
1.15e-10 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 62.12 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIV----EAEKRGeiqpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMArlpaEQLARG-------VITASAGNHAQGVALAAARLGVK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 87 MKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMAQRGEGKLLDQFNNPDnPYAHYTTTGPEIWQQTAGRI 166
Cdd:PRK12483 111 AVIVMPRTTPQLKVDGVRAHGGEVVL--HGESFPDALAHALKLAEEEGLTFVPPFDDPD-VIAGQGTVAMEILRQHPGPL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 647263415 167 THFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEE 202
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDD 223
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
24-203 |
2.82e-08 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 54.25 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 24 GSEVWVKLEGNNPAGSVKDRA---ALSMIVEAEKRGEIqpgdvlIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERR 100
Cdd:PRK07048 38 GAQVFFKCENFQRMGAFKFRGaynALSQFSPEQRRAGV------VTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 101 AAMRAYGAELILVTKEQgmEGARDLALEMAQRGEGKLLDQFNNPDnPYAHYTTTGPEIWQQTaGRITHFVSSMGTTGTIT 180
Cdd:PRK07048 112 AATRGYGGEVVTYDRYT--EDREEIGRRLAEERGLTLIPPYDHPH-VIAGQGTAAKELFEEV-GPLDALFVCLGGGGLLS 187
|
170 180
....*....|....*....|...
gi 647263415 181 GVSRFLREQSKPVAIVGLQPEEG 203
Cdd:PRK07048 188 GCALAARALSPGCKVYGVEPEAG 210
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
11-144 |
4.60e-08 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 53.68 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLqrlgpdnGSEVWVKLEGNNPAGSVKDRAALsmiVEAEKRGEIQPGDVLIEaTSGNTGIALAMIAALKGYRMKLL 90
Cdd:PRK08329 65 TPTVKR-------SIKVYFKLDYLQPTGSFKDRGTY---VTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVF 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 647263415 91 MPDNMSQERRAAMRAYGAELILVtkeqgmEGAR----DLALEMAQRGEGKLLDQFNNP 144
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFV------EGDRmevhEEAVKFSKRNNIPYVSHWLNP 185
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
11-117 |
8.46e-08 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 52.66 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAA----LSMIVEAEKRGeiqpgdvLIEATSGNTGIALAMIAALKGYR 86
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGAtnalLSLSAQERARG-------VVTASTGNHGRALAYAARALGIR 92
|
90 100 110
....*....|....*....|....*....|....*
gi 647263415 87 ----MKLLMPDNmsqeRRAAMRAYGAELILVTKEQ 117
Cdd:PRK07476 93 aticMSRLVPAN----KVDAIRALGAEVRIVGRSQ 123
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
11-206 |
2.21e-07 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 51.85 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRgEIQPGdvLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 91 MPDNMSQERRAAMRAYGAELILV--TKEQGMEGARDLALEmaqrgEGK-LLDQFNNPDnPYAHYTTTGPEIWQQTAGRIT 167
Cdd:PLN02550 187 MPVTTPEIKWQSVERLGATVVLVgdSYDEAQAYAKQRALE-----EGRtFIPPFDHPD-VIAGQGTVGMEIVRQHQGPLH 260
|
170 180 190
....*....|....*....|....*....|....*....
gi 647263415 168 HFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSSI 206
Cdd:PLN02550 261 AIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAM 299
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
9-108 |
5.05e-07 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 50.58 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 9 GNTPLVKLQRLGPDNG--SEVWVKLEGNNPAGSVKDR---AALSMIVEAEKRGeiQPGDVLIEATSGNTGIALAMIAALK 83
Cdd:PLN02569 132 GNSNLFWAERLGKEFLgmNDLWVKHCGISHTGSFKDLgmtVLVSQVNRLRKMA--KPVVGVGCASTGDTSAALSAYCAAA 209
|
90 100
....*....|....*....|....*.
gi 647263415 84 GYRMKLLMP-DNMSQERRAAMRAYGA 108
Cdd:PLN02569 210 GIPSIVFLPaDKISIAQLVQPIANGA 235
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
3-205 |
6.27e-06 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 47.11 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 3 TLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRgEIQPGDVLieATSGNTGIALAMIAAL 82
Cdd:PRK08639 18 RLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDE-ELAAGVVC--ASAGNHAQGVAYACRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 83 KGYRMKLLMPDNMSQERRAAMRAYGA---ELILV--TKEQGMEGARdlalEMAQRGEGKLLDQFNNPDNpYAHYTTTGPE 157
Cdd:PRK08639 95 LGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVgdTFDDSAAAAQ----EYAEETGATFIPPFDDPDV-IAGQGTVAVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 647263415 158 IWQQ--TAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPEEGSS 205
Cdd:PRK08639 170 ILEQleKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAAS 219
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
52-113 |
2.16e-05 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 45.64 E-value: 2.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263415 52 AEKRGEIqpgdVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILV 113
Cdd:PRK08206 111 REKLGDI----TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT 168
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
10-196 |
2.26e-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: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 10 NTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQPGDVlIEATSGNTGIALAMIAALKGYRMKL 89
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVHV-VCSSGGNAGLAAAYAARKLGVPCTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 90 LMPDNMSQERRAAMRAYGAELILVTKEQGmEGARDLALEMAQrgegklldqfNNPDNPYAHyTTTGPEIWQqtagrithf 169
Cdd:cd06448 80 VVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAE----------NDPGPVYVH-PFDDPLIWE--------- 138
|
170 180
....*....|....*....|....*..
gi 647263415 170 vssmGTTGTITGVSRFLREQSKPVAIV 196
Cdd:cd06448 139 ----GHSSMVDEIAQQLQSQEKVDAIV 161
|
|
| MDR2 |
cd08268 |
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
45-139 |
5.19e-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: 44.13 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 45 ALSMIVEAekrGEIQPGD-VLIEATSGNTGIALAMIAALKGYRMKLLmpdNMSQERRAAMRAYGAELILVTKEQgmegar 123
Cdd:cd08268 132 AYGALVEL---AGLRPGDsVLITAASSSVGLAAIQIANAAGATVIAT---TRTSEKRDALLALGAAHVIVTDEE------ 199
|
90
....*....|....*.
gi 647263415 124 DLALEMAQRGEGKLLD 139
Cdd:cd08268 200 DLVAEVLRITGGKGVD 215
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
3-201 |
5.70e-05 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 44.11 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 3 TLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAA---LSMIVEAEK-RGeiqpgdvLIEATSGNTGIALAM 78
Cdd:PRK07334 16 RLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGAlnkLLLLTEEERaRG-------VIAMSAGNHAQGVAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 79 IAALKGYRMKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMAQRGEGKLLDQFNNPDnPYAHYTTTGPEI 158
Cdd:PRK07334 89 HAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVL--HGETLDEARAHARELAEEEGLTFVHPYDDPA-VIAGQGTVALEM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 647263415 159 WQQtAGRITHFVSSMGTTGTITGVSRFLREQSKPVAIVGLQPE 201
Cdd:PRK07334 166 LED-APDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
11-289 |
6.77e-05 |
|
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: 44.06 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPD-NGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQpgdVLIEATSGNTGIALAMIAALKGYRMKL 89
Cdd:cd06446 35 TPLYRAKRLSEYlGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR---VIAETGAGQHGVATATACALFGLECEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 90 LM--PDNMSQE-RRAAMRAYGAELILVTKEQGMEG-ARDLALEmaqrgegkllDQFNNPDN------------PYA---- 149
Cdd:cd06446 112 YMgaVDVERQPlNVFRMELLGAEVVPVPSGSGTLKdAISEAIR----------DWVTNVEDthyllgsvvgphPYPnmvr 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 150 -HYTTTGPEIWQQ---------------------TAGRITHFVS-------------------------SMGTTGTITGV 182
Cdd:cd06446 182 dFQSVIGEEAKKQilekegelpdvviacvgggsnAAGLFYPFINdkdvkligveaggcgletgghaaylFGGTAGVLHGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 183 SRFLreqskpvaivgLQPEEGSSIP------GIRrwpaeYmPGI-------FNASLVDAVlDIHQQDAENTMRQLAVREG 249
Cdd:cd06446 262 KMYT-----------LQDEDGQIVPphsisaGLD-----Y-PGVgpehaylKDSGRVEYV-AVTDEEALEAFKLLARTEG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 647263415 250 IFCGVSSGGAVAGALRIARE-NPGAVVVAIVCDRGDRYLST 289
Cdd:cd06446 324 IIPALESSHAIAYAIKLAKKlGKEKVIVVNLSGRGDKDLQT 364
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
11-202 |
2.77e-04 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 42.05 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIV----EAEKRGeiqpgdvLIEATSGN--TGIALAmiAALKG 84
Cdd:PRK09224 21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAqlteEQLARG-------VITASAGNhaQGVALS--AARLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 85 YRMKLLMPDNMSQERRAAMRAYGAELILvtKEQGMEGARDLALEMAQRgEGKLldqFNNP-DNPY--AHYTTTGPEIWQQ 161
Cdd:PRK09224 92 IKAVIVMPVTTPDIKVDAVRAFGGEVVL--HGDSFDEAYAHAIELAEE-EGLT---FIHPfDDPDviAGQGTIAMEILQQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 647263415 162 TAGRITH-FVsSMGTTGTITGVSRFLREQSKPVAIVGLQPEE 202
Cdd:PRK09224 166 HPHPLDAvFV-PVGGGGLIAGVAAYIKQLRPEIKVIGVEPED 206
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
4-197 |
4.94e-04 |
|
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: 40.93 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 4 LEQTIGNTPLVKLQRLGPDNGSEVWVKLE--------GNnpagsvKDRAALSMIVEAEKRGEiqpgDVLIeaTSG----N 71
Cdd:COG2515 5 LPLAFLPTPLQPLPRLSAALGVELWIKRDdltgpaigGN------KTRKLEYLLADALAQGA----DTLV--TFGgaqsN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 72 TGIALAMIAALKGYRMKLLMPDNMSQERR---AAMRAYGAELILVTKEQGmegaRDLALEMAQRGEgKLLDQFNNP---- 144
Cdd:COG2515 73 HARATAAAAAKLGLKCVLVLRGEEPTPLNgnlLLDRLLGAELHFVSRGEY----RDRDEAMEAVAA-ELRARGGKPyvip 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263415 145 ---DNPYAH--YTTTGPEIWQQTAG---RITHFVSSMGTTGTITGVSRFLREQSKPVAIVG 197
Cdd:COG2515 148 eggSNPLGAlgYVEAAAELAAQLAElgvDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIG 208
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
11-114 |
1.05e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 40.56 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 11 TPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAALSMIVEAEKRGEIQpgdVLIEATSGNTGIALAMIAALKGYRMKLL 90
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTR---IIAETGAGQHGVATATACALFGLKCTIF 348
|
90 100
....*....|....*....|....*..
gi 647263415 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 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263415 52 AEKRGEIQPGDVLIEATSGNTGiaLAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELIL-VTKEQGMEGARDL 125
Cdd:cd08256 166 AVDRANIKFDDVVVLAGAGPLG--LGMIGAARLKNPKKLIVLDLKDERLALARKFGADVVLnPPEVDVVEKIKEL 238
|
|
| PLN02970 |
PLN02970 |
serine racemase |
2-201 |
6.38e-03 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 37.74 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 2 NTLEQTIGNTPLVKLQRLGPDNGSEVWVKLEGNNPAGSVKDRAA----LSMIVEAEKRGeiqpgdvLIEATSGNTGIALA 77
Cdd:PLN02970 19 KRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGAcnaiFSLSDDQAEKG-------VVTHSSGNHAAALA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263415 78 MIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILVtkEQGMEGARDLALEMAQRGEGKLLDQFNNPdNPYAHYTTTGPE 157
Cdd:PLN02970 92 LAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWC--EPTVESREAVAARVQQETGAVLIHPYNDG-RVISGQGTIALE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 647263415 158 IWQQTAGRITHFVSSMGtTGTITGVSRFLREQSKPVAIVGLQPE 201
Cdd:PLN02970 169 FLEQVPELDVIIVPISG-GGLISGIALAAKAIKPSIKIIAAEPK 211
|
|
| |
