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Conserved domains on  [gi|298289240|sp|A6TXQ1|]
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RecName: Full=N-(2-amino-2-carboxyethyl)-L-glutamate synthase; Short=ACEGA synthase

Protein Classification

2,3-diaminopropionate biosynthesis protein SbnA( domain architecture ID 10800418)

2,3-diaminopropionate biosynthesis protein SbnA catalyzes the synthesis of N-((2S)-2-amino-2-carboxyethyl)-L-glutamate (ACEGA) from O-phospho-L-serine and L-glutamate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
12-314 0e+00

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: 526.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDApfRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  170 VETIKQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHV 249
Cdd:TIGR03945 161 ARAFPTL-DYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298289240  250 DDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:TIGR03945 240 PEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
 
Name Accession Description Interval E-value
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
12-314 0e+00

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: 526.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDApfRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  170 VETIKQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHV 249
Cdd:TIGR03945 161 ARAFPTL-DYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298289240  250 DDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:TIGR03945 240 PEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
17-306 8.21e-141

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: 399.58  E-value: 8.21e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  17 GQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLKLT 94
Cdd:cd01561    1 GNTPLVRLNRLSPgtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  95 CVVDPKISPTNLKIIKSYGANVEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIK 174
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEAEADG--MKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 175 QPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQVIHVDDYQ 253
Cdd:cd01561  159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 298289240 254 SALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:cd01561  239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
9-306 1.00e-130

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: 374.38  E-value: 1.00e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   9 HDSLLDSVGQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:COG0031    4 YDSILELIGNTPLVRLNRLSPgpGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYlmtrIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:COG0031   84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGA----IDKAEELAAETPGAFWPNQFENPANPEAHYETTG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:COG0031  160 PEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298289240 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:COG0031  240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLS 300
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
12-299 2.39e-75

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: 233.36  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGlitENTHLIESTSGNLGIALAMIAKIK 89
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELgvDVYLKLESLNPTGSFKDRGALNLLLRLKEGE---GGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVeepdahGGYLMTRIAKVQELLATIDDAYWINQYANELNWQShYHGAGTEI 169
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  170 VETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGD----------KPINRELPGIGASRVPEILN 239
Cdd:pfam00291 151 LEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGALA 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298289240  240 RSEINQ----VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLI-TSIEEGATIVTILPD 299
Cdd:pfam00291 231 LDLLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALaGELKGGDRVVVVLTG 295
PRK10717 PRK10717
cysteine synthase A; Provisional
9-314 1.75e-65

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 209.33  E-value: 1.75e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   9 HDSLLDSVGQTPMVQLHQL--FPKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:PRK10717   4 FEDVSDTIGNTPLIRLNRAseATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEE-PDAHGG-YLMTRIAKVQELLAT-IDDAYWINQYANELNWQSHYH 163
Cdd:PRK10717  84 AARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAaPYANPNnYVKGAGRLAEELVASePNGAIWANQFDNPANREAHYE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 164 GAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFG-------DKPINRELPGIGASRVPE 236
Cdd:PRK10717 164 TTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITEGIGQGRITA 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298289240 237 ILNRSEINQVIHVDDyQSALG-CRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:PRK10717 244 NLEGAPIDDAIRIPD-EEALStAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFL 321
 
Name Accession Description Interval E-value
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
12-314 0e+00

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: 526.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDApfRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  170 VETIKQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHV 249
Cdd:TIGR03945 161 ARAFPTL-DYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298289240  250 DDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:TIGR03945 240 PEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEWV 304
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
17-306 8.21e-141

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: 399.58  E-value: 8.21e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  17 GQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLKLT 94
Cdd:cd01561    1 GNTPLVRLNRLSPgtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  95 CVVDPKISPTNLKIIKSYGANVEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIK 174
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEAEADG--MKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 175 QPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQVIHVDDYQ 253
Cdd:cd01561  159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFsGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 298289240 254 SALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:cd01561  239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
9-306 1.00e-130

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: 374.38  E-value: 1.00e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   9 HDSLLDSVGQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:COG0031    4 YDSILELIGNTPLVRLNRLSPgpGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGYlmtrIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:COG0031   84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGA----IDKAEELAAETPGAFWPNQFENPANPEAHYETTG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIF-GDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:COG0031  160 PEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDPSLIDE 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298289240 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLD 306
Cdd:COG0031  240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLS 300
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
12-305 1.69e-86

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: 261.83  E-value: 1.69e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCdaRVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVeepDAHGGyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEI 169
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILT---PGEEG-MKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  170 VETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIH 248
Cdd:TIGR01136 157 WRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEpAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVIT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 298289240  249 VDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIE-EGATIVTILPDRGDRYL 305
Cdd:TIGR01136 237 VSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYL 294
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
14-305 5.76e-80

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: 245.35  E-value: 5.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   14 DSVGQTPMVQLHQLFPKH-EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIKGLK 92
Cdd:TIGR01139   3 ELIGNTPLVRLNRIEGCNaNVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   93 LTCVVDPKISPTNLKIIKSYGANVEMVeePDAHGGYLMtrIAKVQELLATIDDAYWI-NQYANELNWQSHYHGAGTEIVE 171
Cdd:TIGR01139  83 LILTMPETMSIERRKLLKAYGAELVLT--PGAEGMKGA--IAKAEEIAASTPNSYFMlQQFENPANPEIHRKTTGPEIWR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  172 TIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGS-VIFGDKPINRELPGIGASRVPEILNRSEINQVIHVD 250
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESpVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVS 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 298289240  251 DYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYL 305
Cdd:TIGR01139 239 DEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYL 293
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
12-299 2.39e-75

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: 233.36  E-value: 2.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGlitENTHLIESTSGNLGIALAMIAKIK 89
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELgvDVYLKLESLNPTGSFKDRGALNLLLRLKEGE---GGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   90 GLKLTCVVDPKISPTNLKIIKSYGANVEMVeepdahGGYLMTRIAKVQELLATIDDAYWINQYANELNWQShYHGAGTEI 169
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV------GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  170 VETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGD----------KPINRELPGIGASRVPEILN 239
Cdd:pfam00291 151 LEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARslaagrpvpvPVADTIADGLGVGDEPGALA 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298289240  240 RSEINQ----VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLI-TSIEEGATIVTILPD 299
Cdd:pfam00291 231 LDLLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALaGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
19-300 2.76e-69

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: 216.23  E-value: 2.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  19 TPMVQLHQLF--PKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLItENTHLIESTSGNLGIALAMIAKIKGLKLTCV 96
Cdd:cd00640    1 TPLVRLKRLSklGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  97 VDPKISPTNLKIIKSYGANVEMVEepdahgGYLMTRIAKVQELLATIDDAYWINQYANELNWQSHYhGAGTEIVETIK-Q 175
Cdd:cd00640   80 MPEGASPEKVAQMRALGAEVVLVP------GDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGgQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 176 PIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKgsvifgdkpinrelpgigasrvpeilnrseinqVIHVDDYQSA 255
Cdd:cd00640  153 KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------VVTVSDEEAL 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 298289240 256 LGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDR 300
Cdd:cd00640  200 EAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
9-316 6.19e-69

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: 221.98  E-value: 6.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240    9 HDSLLDSVGQTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:TIGR01137   2 LDNILDLIGNTPLVRLNKVSKglKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMV------EEPDAHGGylmtrIAKvqELLATIDDAYWINQYANELNWQS 160
Cdd:TIGR01137  82 AIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTptaaafDSPESHIG-----VAK--RLVREIPGAHILDQYRNPSNPLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  161 HYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFGDKPINR------ELPGIGASRV 234
Cdd:TIGR01137 155 HYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQtgrtpyKVEGIGYDFI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  235 PEILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTGS-IIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTW 313
Cdd:TIGR01137 235 PTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSaVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDEW 314

                  ...
gi 298289240  314 LEK 316
Cdd:TIGR01137 315 MLD 317
PRK10717 PRK10717
cysteine synthase A; Provisional
9-314 1.75e-65

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 209.33  E-value: 1.75e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   9 HDSLLDSVGQTPMVQLHQL--FPKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIA 86
Cdd:PRK10717   4 FEDVSDTIGNTPLIRLNRAseATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEE-PDAHGG-YLMTRIAKVQELLAT-IDDAYWINQYANELNWQSHYH 163
Cdd:PRK10717  84 AARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAaPYANPNnYVKGAGRLAEELVASePNGAIWANQFDNPANREAHYE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 164 GAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGSVIFG-------DKPINRELPGIGASRVPE 236
Cdd:PRK10717 164 TTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITEGIGQGRITA 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298289240 237 ILNRSEINQVIHVDDyQSALG-CRKLIDYEGIFAGGSTGSIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:PRK10717 244 NLEGAPIDDAIRIPD-EEALStAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFL 321
cysM PRK11761
cysteine synthase CysM;
11-305 3.17e-64

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 204.72  E-value: 3.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  11 SLLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKI 88
Cdd:PRK11761   5 TLEDTIGNTPLVKLQRLPPDRgnTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  89 KGLKLTCVVdpkisPTNLKI-----IKSYGANVEMVEepdAHGGYLMTR---IAKVQELLATIddaywINQYANELNWQS 160
Cdd:PRK11761  85 KGYRMKLIM-----PENMSQerraaMRAYGAELILVP---KEQGMEGARdlaLQMQAEGEGKV-----LDQFANPDNPLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 161 HYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIfgdkpinrelPGI---GASRVPE 236
Cdd:PRK11761 152 HYETTGPEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQpEEGSSI----------PGIrrwPEEYLPK 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298289240 237 ILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIeEGATIVTILPDRGDRYL 305
Cdd:PRK11761 222 IFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYL 289
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
16-323 4.51e-47

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 162.82  E-value: 4.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  16 VGQTPMVQLHQLFPKHEVF--AKLEYMNPGGSMKDRPAKYIIEHGIKHGLITE-NTHLIESTSGNLGIALAMIAKIKGLK 92
Cdd:PLN02556  57 IGKTPLVYLNKVTEGCGAYiaAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPgKTTLIEPTSGNMGISLAFMAAMKGYK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  93 LTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGylmtRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVET 172
Cdd:PLN02556 137 MILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGG----TVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWED 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 173 IKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHVDD 251
Cdd:PLN02556 213 TLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEpAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSS 292
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298289240 252 YQSALGCRKLIDYEGIFAGGSTGS-IIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWLEKMKSRQGV 323
Cdd:PLN02556 293 EDAVNMARELALKEGLMVGISSGAnTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENMQPV 365
PLN02565 PLN02565
cysteine synthase
16-312 9.35e-44

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 152.77  E-value: 9.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  16 VGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTH-LIESTSGNLGIALAMIAKIKGLK 92
Cdd:PLN02565  13 IGKTPLVYLNNVVDGcvARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGLAFMAAAKGYK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  93 LTCVVDPKISPTNLKIIKSYGAnvEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVET 172
Cdd:PLN02565  93 LIITMPASMSLERRIILLAFGA--ELVLTDPAKG--MKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 173 IKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQVIHVDD 251
Cdd:PLN02565 169 TGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEpVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSS 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298289240 252 YQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIE-EGATIVTILPDRGDRYLDLVYSDT 312
Cdd:PLN02565 249 DEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFES 310
PLN03013 PLN03013
cysteine synthase
10-305 1.51e-41

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 149.54  E-value: 1.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  10 DSLLDSVGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITE-NTHLIESTSGNLGIALAMIA 86
Cdd:PLN03013 115 DNVSQLIGKTPMVYLNSIAKGcvANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPgKSVLVEPTSGNTGIGLAFIA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  87 KIKGLKLTCVVDPKISPTNLKIIKSYGAnvEMVEEPDAHGgyLMTRIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:PLN03013 195 ASRGYRLILTMPASMSMERRVLLKAFGA--ELVLTDPAKG--MTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTG 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGS-VIFGDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:PLN03013 271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESdILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE 350
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298289240 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEE-GATIVTILPDRGdRYL 305
Cdd:PLN03013 351 VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENaGKLIAVSLFASG-RDI 410
PLN00011 PLN00011
cysteine synthase
10-305 7.79e-39

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 139.75  E-value: 7.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  10 DSLLDSVGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITE-NTHLIESTSGNLGIALAMIA 86
Cdd:PLN00011   9 NDVTELIGNTPMVYLNNIVDGcvARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPgKSTLIEATAGNTGIGLACIG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  87 KIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEPDAHGGylmtRIAKVQELLATIDDAYWINQYANELNWQSHYHGAG 166
Cdd:PLN00011  89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKG----MLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 167 TEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVD-AKGSVIFGDKPINRELPGIGASRVPEILNRSEINQ 245
Cdd:PLN00011 165 PEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEpVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDE 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298289240 246 VIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITSIEE-GATIVTILPDRGDRYL 305
Cdd:PLN00011 245 IIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYL 305
PLN02356 PLN02356
phosphateglycerate kinase
12-314 3.56e-35

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 132.04  E-value: 3.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  12 LLDSVGQTPMVQLHQLFPKH--EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENTHLIESTSGNLGIALAMIAKIK 89
Cdd:PLN02356  47 LIDAIGNTPLIRINSLSEATgcEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  90 GLKLTCVVDPKISPTNLKIIKSYGANVEMV--------------------------------EEPDAHG-----GYLMTR 132
Cdd:PLN02356 127 GCKCHVVIPDDVAIEKSQILEALGATVERVrpvsithkdhyvniarrraleanelaskrrkgSETDGIHlektnGCISEE 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 133 IAKVQELLATIDDAYWINQYANELNWQSHYHGAGTEIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAK 212
Cdd:PLN02356 207 EKENSLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPP 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 213 GSVIFG------------------DKPINRELPGIGASRVPEILNRSEINQVIHVDDYQSALGCRKLIDYEGIFAGGSTG 274
Cdd:PLN02356 287 GSGLFNkvtrgvmytreeaegrrlKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSA 366
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 298289240 275 SIIAAIEQLITSIEEGATIVTILPDRGDRYLDLVYSDTWL 314
Cdd:PLN02356 367 MNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYL 406
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
17-297 3.35e-13

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: 69.16  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  17 GQTPMVQLHQLFPKH---EVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLitenTHLIESTSGNLGIALAMIAKIKGLKl 93
Cdd:cd01563   21 GNTPLVRAPRLGERLggkNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  94 TCVVDPK-ISPTNLKIIKSYGANVEMVEepdahggylmTRIAKVQELLATIDDAYWInqYANelNWQSHYHGAGT----- 167
Cdd:cd01563   96 CVVFLPAgKALGKLAQALAYGATVLAVE----------GNFDDALRLVRELAEENWI--YLS--NSLNPYRLEGQktiaf 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 168 EIVETIKQPI-DYFVAPVSTTGSIMGMSRKIKEVH--------PnaQIVAVDAKGS------VIFGDKPINR-ELP---- 227
Cdd:cd01563  162 EIAEQLGWEVpDYVVVPVGNGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAapivraFKEGKDDIEPvENPetia 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298289240 228 -GI------GASRVPEILNRSEInQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITS--IEEGATIVTIL 297
Cdd:cd01563  240 tAIrignpaSGPKALRAVRESGG-TAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
16-297 4.92e-13

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: 69.07  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  16 VGQTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITenthLIESTSGNLGIALAMIAKIKGLKL 93
Cdd:COG0498   64 EGGTPLVKAPRLADElgKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKT----IVCASSGNGSAALAAYAARAGIEV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  94 TCVVdP--KISPTNLKIIKSYGANVEMVEepdahGGYlMTRIAKVQELLAtidDAYWINqyANELNWqshY--HGAGT-- 167
Cdd:COG0498  140 FVFV-PegKVSPGQLAQMLTYGAHVIAVD-----GNF-DDAQRLVKELAA---DEGLYA--VNSINP---ArlEGQKTya 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 168 -EIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVH--------PnaQIVAVDAKGSV-IF-----GDKPINRELPG---- 228
Cdd:COG0498  205 fEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKelglidrlP--RLIAVQATGCNpILtafetGRDEYEPERPEtiap 282
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298289240 229 ---IGAS----RVPEILNRSEiNQVIHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLI--TSIEEGATIVTIL 297
Cdd:COG0498  283 smdIGNPsngeRALFALRESG-GTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLReeGEIDPDEPVVVLS 359
PRK08329 PRK08329
threonine synthase; Validated
19-213 1.53e-12

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 67.54  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  19 TPMVQLHQlfpkhEVFAKLEYMNPGGSMKDRpAKYIIEHGIKHGLITENThlIEStSGNLGIALAMIAKIKGLKLTCVVD 98
Cdd:PRK08329  65 TPTVKRSI-----KVYFKLDYLQPTGSFKDR-GTYVTVAKLKEEGINEVV--IDS-SGNAALSLALYSLSEGIKVHVFVS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  99 PKISPTNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQELLATiddAYWINQYANElnwqshyhgaGT-----EIVETI 173
Cdd:PRK08329 136 YNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYV---SHWLNPYFLE----------GTktiayEIYEQI 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 298289240 174 KQPiDYFVAPVSTTGSIMGMSRKIKEVHPNAQI------VAVDAKG 213
Cdd:PRK08329 203 GVP-DYAFVPVGSGTLFLGIWKGFKELHEMGEIskmpklVAVQAEG 247
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
18-280 7.17e-12

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: 65.01  E-value: 7.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  18 QTPMVQLHQLFPK--HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLiTENTHLIESTSGNLGIALAMIAKIKGLKLTC 95
Cdd:cd06448    1 KTPLIESTALSKTagCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGL-NECVHVVCSSGGNAGLAAAYAARKLGVPCTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  96 VVDPKISPTNLKIIKSYGANVEMV-----EEPDAHGgylmtriakvQELLATIDDAYWINQYANELNWQSHyhgagTEIV 170
Cdd:cd06448   80 VVPESTKPRVVEKLRDEGATVVVHgkvwwEADNYLR----------EELAENDPGPVYVHPFDDPLIWEGH-----SSMV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 171 ETIKQ------PIDYFVAPVSTTGSIMGMSRKIKEVHPN-AQIVAVDAKGSVIF-----GDKPInrELPGI-------GA 231
Cdd:cd06448  145 DEIAQqlqsqeKVDAIVCSVGGGGLLNGIVQGLERNGWGdIPVVAVETEGAHSLnaslkAGKLV--TLPKItsvatslGA 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 298289240 232 SRVPEILNRSEINQVIH---VDDYQSALGCRKLIDYEGIFAGGSTGSIIAAI 280
Cdd:cd06448  223 KTVSSQALEYAQEHNIKsevVSDRDAVQACLRFADDERILVEPACGAALAVV 274
PRK06450 PRK06450
threonine synthase; Validated
17-120 7.94e-11

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 62.06  E-value: 7.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  17 GQTPMVQlhqlfpKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLitenTHLIESTSGNLGIALAMIAKIKGLKLTCV 96
Cdd:PRK06450  57 GRTPLIK------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIF 126
                         90       100
                 ....*....|....*....|....
gi 298289240  97 VDPKISPTNLKIIKSYGANVEMVE 120
Cdd:PRK06450 127 VPETASGGKLKQIESYGAEVVRVR 150
PRK05638 PRK05638
threonine synthase; Validated
17-301 1.24e-09

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 59.06  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  17 GQTPMVQLHQLFPKHE-VFAKLEYMNPGGSMKDRPAKYIIEHGIKHGliteNTHLIESTSGNLGIALAMIAKIKGLKLTC 95
Cdd:PRK05638  65 GGTPLIRARISEKLGEnVYIKDETRNPTGSFRDRLATVAVSYGLPYA----ANGFIVASDGNAAASVAAYSARAGKEAFV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  96 VVDPKISPTNLKIIKSYGANVEMVEEpdahggylmtriaKVQELLatiddaywinQYANEL-------NWQSHYHGAGTE 168
Cdd:PRK05638 141 VVPRKVDKGKLIQMIAFGAKIIRYGE-------------SVDEAI----------EYAEELarlnglyNVTPEYNIIGLE 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 169 IVETIKQPI------DYFVAPVSTTGSIMGMSRKIKEVHPNAQI------VAVDAK-----GSVIFGDKPINRELPGIG- 230
Cdd:PRK05638 198 GQKTIAFELweeinpTHVIVPTGSGSYLYSIYKGFKELLEIGVIeeipklIAVQTErcnpiASEILGNKTKCNETKALGl 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 231 -------ASRVPEILNRS-EINQVIHVDDYQSAlgcRKLIDYEGIFAGGSTGSIIAAIEQLITS--IEEGATIVTILPDR 300
Cdd:PRK05638 278 yvknpvmKEYVSEAIKESgGTAVVVNEEEIMAG---EKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354

                 .
gi 298289240 301 G 301
Cdd:PRK05638 355 G 355
PLN02970 PLN02970
serine racemase
32-214 8.06e-09

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 56.23  E-value: 8.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  32 EVFAKLEYMNPGGSMKDRPAKYIIEHGI----KHGLITentHliesTSGNLGIALAMIAKIKGLKLTCVVdPKISPtNLK 107
Cdd:PLN02970  43 SLFFKCECFQKGGAFKFRGACNAIFSLSddqaEKGVVT---H----SSGNHAAALALAAKLRGIPAYIVV-PKNAP-ACK 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 108 I--IKSYGANVEMVEEpdahggYLMTRIAKVQELLATIDdAYWINQYanelNWQSHYHGAGT---EIVETIKQpIDYFVA 182
Cdd:PLN02970 114 VdaVIRYGGIITWCEP------TVESREAVAARVQQETG-AVLIHPY----NDGRVISGQGTialEFLEQVPE-LDVIIV 181
                        170       180       190
                 ....*....|....*....|....*....|..
gi 298289240 183 PVSTTGSIMGMSRKIKEVHPNAQIVAVDAKGS 214
Cdd:PLN02970 182 PISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
PRK06815 PRK06815
threonine/serine dehydratase;
1-209 1.55e-08

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 55.08  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240   1 MIEKSQACHDSLLDSVGQTPM---VQLHQLfPKHEVFAKLEYMNPGGSMKDRPAKYII----EHGIKHGLITenthlieS 73
Cdd:PRK06815   3 LFDAILEAHQRLRPQVRVTPLehsPLLSQH-TGCEVYLKCEHLQHTGSFKFRGASNKLrllnEAQRQQGVIT-------A 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  74 TSGNLGIALAMIAKIKGLKLTCVVDPKISPTNLKIIKSYGANVEMVEEpDAHGGYLMTRI-AKVQELLatiddayWINQY 152
Cdd:PRK06815  75 SSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGG-DALNAELAARRaAEQQGKV-------YISPY 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 153 aNELNWQShyhGAGT---EIVETIKQPIDYFVApVSTTGSIMGMSRKIKEVHPNAQIVAV 209
Cdd:PRK06815 147 -NDPQVIA---GQGTigmELVEQQPDLDAVFVA-VGGGGLISGIATYLKTLSPKTEIIGC 201
PRK06608 PRK06608
serine/threonine dehydratase;
16-208 7.33e-08

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 53.24  E-value: 7.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  16 VGQTPMVQ---LHQLFpKHEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITEntHLIESTSGNLGIALAMIAKIKGLK 92
Cdd:PRK06608  21 LHLTPIVHsesLNEML-GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAYASKLFGIK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  93 LTCVVDPKISPTNLKIIKSYGANVEmveepdahggYLMTRI-AKVQELLATIDDAYWINQYanelNWQSHYHGAGT---E 168
Cdd:PRK06608  98 TRIYLPLNTSKVKQQAALYYGGEVI----------LTNTRQeAEEKAKEDEEQGFYYIHPS----DSDSTIAGAGTlcyE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 298289240 169 IVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVA 208
Cdd:PRK06608 164 ALQQLGFSPDAIFASCGGGGLISGTYLAKELISPTSLLIG 203
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
18-211 2.26e-05

bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 45.50  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  18 QTPMVQLHQLFP--KHEVFAKLEYMNPGGSMKDRPAKYIIEHgikhglITENTH---LIESTSGNLGIALAMIAKIKGLK 92
Cdd:PRK08638  27 KTPLPRSNYLSErcKGEIFLKLENMQRTGSFKIRGAFNKLSS------LTDAEKrkgVVACSAGNHAQGVALSCALLGID 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  93 LTcVVDPKISP-TNLKIIKSYGANVEMveepdaHGGYLMTRIAKVQElLATIDDAYWINQYANELNwqshYHGAGT---E 168
Cdd:PRK08638 101 GK-VVMPKGAPkSKVAATCGYGAEVVL------HGDNFNDTIAKVEE-IVEEEGRTFIPPYDDPKV----IAGQGTiglE 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 298289240 169 IVETIKQpIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDA 211
Cdd:PRK08638 169 ILEDLWD-VDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQS 210
PRK06381 PRK06381
threonine synthase; Validated
33-116 3.74e-05

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 44.70  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  33 VFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLITENThlieSTSGNLGIALAMIAKIKGLKLTCVVDPKISPTNLKIIKSY 112
Cdd:PRK06381  33 IYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITV----GTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKY 108

                 ....
gi 298289240 113 GANV 116
Cdd:PRK06381 109 GAEI 112
PRK08197 PRK08197
threonine synthase; Validated
17-308 6.91e-05

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 44.22  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  17 GQTPMVQLHQLFPK---HEVFAKLEYMNPGGSMKDRPAKYIIEHGIKHGLitenTHLIESTSGNLGIALAMIAKIKGLKL 93
Cdd:PRK08197  78 GMTPLLPLPRLGKAlgiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGV----KHLAMPTNGNAGAAWAAYAARAGIRA 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  94 TCVVdPKISP-TNLKIIKSYGANVEMVEEPDAHGGYLMTRIAKVQEL--LATIDDAYWIN-------QYANELNWqshyh 163
Cdd:PRK08197 154 TIFM-PADAPeITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWfdVSTLKEPYRIEgkktmglELAEQLGW----- 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 164 gagtEIVETIKQPidyfvapvstTG---SIMGMSRKIKEVH-------PNAQIVAVDAKGSVifgdkPINREL------- 226
Cdd:PRK08197 228 ----RLPDVILYP----------TGggvGLIGIWKAFDELEalgwiggKRPRLVAVQAEGCA-----PIVKAWeegkees 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 227 ----------PGIgasRVPEILNRSEINQV--------IHVDDYQSALGCRKLIDYEGIFAGGSTGSIIAAIEQLITS-- 286
Cdd:PRK08197 289 efwedahtvaFGI---RVPKALGDFLVLDAvretggcaIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESgw 365
                        330       340
                 ....*....|....*....|..
gi 298289240 287 IEEGATIVTILPDRGDRYLDLV 308
Cdd:PRK08197 366 LKGDERVVLFNTGSGLKYPDTV 387
PRK08639 PRK08639
threonine dehydratase; Validated
164-213 1.70e-04

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 42.87  E-value: 1.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 298289240 164 GAGT---EIVETIKQP--IDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDAKG 213
Cdd:PRK08639 162 GQGTvavEILEQLEKEgsPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
PRK08246 PRK08246
serine/threonine dehydratase;
18-121 2.04e-04

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 42.63  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  18 QTPMVQLH-QLFPKHEVFAKLEYMNPGGSMKDRPAKY-IIEHGI-KHGLITenthlieSTSGNLGIALAMIAKIKGLKLT 94
Cdd:PRK08246  23 RTPVLEADgAGFGPAPVWLKLEHLQHTGSFKARGAFNrLLAAPVpAAGVVA-------ASGGNAGLAVAYAAAALGVPAT 95
                         90       100
                 ....*....|....*....|....*...
gi 298289240  95 CVVdPKISPTN-LKIIKSYGANVEMVEE 121
Cdd:PRK08246  96 VFV-PETAPPAkVARLRALGAEVVVVGA 122
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
71-214 6.18e-03

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 38.20  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240  71 IESTSGN--LGIALAmiAKIKGLKLTCVVdPKISPtNLKI--IKSYGANVEMveepdaHGgylmtriakvqellATIDDA 146
Cdd:PRK09224  72 ITASAGNhaQGVALS--AARLGIKAVIVM-PVTTP-DIKVdaVRAFGGEVVL------HG--------------DSFDEA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298289240 147 YwinQYANELNWQSHY---H---------GAGT---EIVETIKQPIDYFVAPVSTTGSIMGMSRKIKEVHPNAQIVAVDA 211
Cdd:PRK09224 128 Y---AHAIELAEEEGLtfiHpfddpdviaGQGTiamEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEP 204

                 ...
gi 298289240 212 KGS 214
Cdd:PRK09224 205 EDS 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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