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Conserved domains on  [gi|1011417748|ref|WP_062329357|]
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MULTISPECIES: cysteine synthase A [Paenibacillus]

Protein Classification

PLP-dependent cysteine synthase family protein( domain architecture ID 10000483)

cysteine synthase family protein is a pyridoxal 5'-phosphate (PLP)-dependent enzyme similar to Helicobacter pylori cysteine synthase

CATH:  3.40.50.1100
Gene Ontology:  GO:0030170
SCOP:  4000798

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
3-305 1.47e-172

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


:

Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 479.93  E-value: 1.47e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAIqsvGGTLDAFVAgigtggtitgtgEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:COG0031   162 IWEQT---DGKVDAFVAgvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLID 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLST 305
Cdd:COG0031   239 EVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
 
Name Accession Description Interval E-value
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
3-305 1.47e-172

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 479.93  E-value: 1.47e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAIqsvGGTLDAFVAgigtggtitgtgEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:COG0031   162 IWEQT---DGKVDAFVAgvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLID 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLST 305
Cdd:COG0031   239 EVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
8-308 2.52e-168

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 469.15  E-value: 2.52e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIvPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENP-SYFMAEQFKNKANVKIHRETTGPEIVEA 166
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnSYFMLQQFENPANPEIHRKTTGPEIWRD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 167 IqsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIH 246
Cdd:TIGR01139 160 T---DGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVIT 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 247 IENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01139 237 VSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
13-304 2.30e-153

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 430.78  E-value: 2.30e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  93 IVMPETMSMERRNLLRAYGAELVLTPGAE--GMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIVEAIqsv 170
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 171 GGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIHIEND 250
Cdd:cd01561   158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011417748 251 DAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLS 304
Cdd:cd01561   238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
PRK10717 PRK10717
cysteine synthase A; Provisional
3-309 2.32e-114

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 333.37  E-value: 2.32e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:PRK10717    2 KIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGA------EGMNGAVKKAEELLKENPS-YFMAEQFKNKANVKIH 155
Cdd:PRK10717   82 VAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNgAIWANQFDNPANREAH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 156 RETTGPEIveaIQSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPI----LAG--GKPGPHKIQGIGA 229
Cdd:PRK10717  162 YETTGPEI---WEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEGIGQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 230 NFIPEILDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTpLYN 309
Cdd:PRK10717  239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK-LFN 317
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
8-296 2.07e-71

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 222.96  E-value: 2.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEgklKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHrETTGPEIVEAI 167
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY-GTIGLEILEQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 qsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGG---------KPGPHKIQGIGANFIPEILDQ 238
Cdd:pfam00291 155 ---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALAL 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 239 EIY----DEIIHIENDDAFETARQVAKEEGILSGISSGAAIRA-GLQVAKQLGAGKRVVVIVP 296
Cdd:pfam00291 232 DLLdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAlKLALAGELKGGDRVVVVLT 294
 
Name Accession Description Interval E-value
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
3-305 1.47e-172

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 479.93  E-value: 1.47e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAIqsvGGTLDAFVAgigtggtitgtgEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:COG0031   162 IWEQT---DGKVDAFVAgvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLID 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLST 305
Cdd:COG0031   239 EVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
8-308 2.52e-168

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 469.15  E-value: 2.52e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIvPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENP-SYFMAEQFKNKANVKIHRETTGPEIVEA 166
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnSYFMLQQFENPANPEIHRKTTGPEIWRD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 167 IqsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIH 246
Cdd:TIGR01139 160 T---DGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVIT 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 247 IENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01139 237 VSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
8-308 8.88e-160

cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273463  Cd Length: 299  Bit Score: 447.50  E-value: 8.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIVEAI 167
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 qsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIHI 247
Cdd:TIGR01136 161 ---DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITV 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 248 ENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLG-AGKRVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01136 238 SDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLSTGLF 299
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
13-304 2.30e-153

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 430.78  E-value: 2.30e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  93 IVMPETMSMERRNLLRAYGAELVLTPGAE--GMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIVEAIqsv 170
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 171 GGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEIIHIEND 250
Cdd:cd01561   158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011417748 251 DAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLS 304
Cdd:cd01561   238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
PRK10717 PRK10717
cysteine synthase A; Provisional
3-309 2.32e-114

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 333.37  E-value: 2.32e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAM 82
Cdd:PRK10717    2 KIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGA------EGMNGAVKKAEELLKENPS-YFMAEQFKNKANVKIH 155
Cdd:PRK10717   82 VAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNgAIWANQFDNPANREAH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 156 RETTGPEIveaIQSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPI----LAG--GKPGPHKIQGIGA 229
Cdd:PRK10717  162 YETTGPEI---WEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEGIGQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 230 NFIPEILDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTpLYN 309
Cdd:PRK10717  239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK-LFN 317
PLN02565 PLN02565
cysteine synthase
4-309 1.54e-112

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 328.81  E-value: 1.54e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   4 VVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTI-IEATSGNTGIGLAM 82
Cdd:PLN02565    5 IAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:PLN02565   85 MAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAiqsVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:PLN02565  165 IWKG---TGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLD 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ-LGAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PLN02565  242 EVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLFE 309
PLN03013 PLN03013
cysteine synthase
4-308 4.05e-101

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 303.24  E-value: 4.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   4 VVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTI-IEATSGNTGIGLAM 82
Cdd:PLN03013  113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAF 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  83 VAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPE 162
Cdd:PLN03013  193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGPE 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 163 IVEAIQsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYD 242
Cdd:PLN03013  273 IWDDTK---GKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMD 349
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011417748 243 EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ-LGAGKRVVVIVPSNGeRYLSTPLY 308
Cdd:PLN03013  350 EVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRpENAGKLIAVSLFASG-RDIYTPRC 415
PLN00011 PLN00011
cysteine synthase
6-309 1.92e-100

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 298.07  E-value: 1.92e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   6 NNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPG-DTIIEATSGNTGIGLAMVA 84
Cdd:PLN00011    9 NDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  85 AAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEIv 164
Cdd:PLN00011   89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPEI- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 165 eaIQSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIYDEI 244
Cdd:PLN00011  168 --WRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEI 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011417748 245 IHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ-LGAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PLN00011  246 IQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVIFPSGGERYLSTKLFE 311
cysM PRK11761
cysteine synthase CysM;
10-309 1.18e-97

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 289.85  E-value: 1.18e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  10 ELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGY 89
Cdd:PRK11761    8 DTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  90 KSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENpSYFMAEQFKNKANVKIHRETTGPEIveaIQS 169
Cdd:PRK11761   88 RMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEG-EGKVLDQFANPDNPLAHYETTGPEI---WRQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 170 VGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPA-ASPIlaggkPGphkIQGIGANFIPEILDQEIYDEIIHIE 248
Cdd:PRK11761  164 TEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEeGSSI-----PG---IRRWPEEYLPKIFDASRVDRVLDVS 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011417748 249 NDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLgAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PRK11761  236 QQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLSTGVFP 295
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
3-309 9.30e-97

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 289.94  E-value: 9.30e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   3 KVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDT-IIEATSGNTGIGLA 81
Cdd:PLN02556   48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  82 MVAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGP 161
Cdd:PLN02556  128 FMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGP 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 162 EIVEaiqSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGGKPGPHKIQGIGANFIPEILDQEIY 241
Cdd:PLN02556  208 EIWE---DTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVM 284
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011417748 242 DEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQL-GAGKRVVVIVPSNGERYLSTPLYN 309
Cdd:PLN02556  285 EKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPeNKGKLIVTVHPSFGERYLSSVLFQ 353
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
7-304 1.44e-93

cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273464 [Multi-domain]  Cd Length: 455  Bit Score: 284.77  E-value: 1.44e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   7 NVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAA 86
Cdd:TIGR01137   4 NILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  87 KGYKSVIVMPETMSMERRNLLRAYGAELVLTPGA---EGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEI 163
Cdd:TIGR01137  84 KGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAaafDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 164 VEAIQsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASpILAGGKP------GPHKIQGIGANFIPEILD 237
Cdd:TIGR01137 164 LEQCE---GKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVLD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011417748 238 QEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGA-GKRVVVIVPSNGERYLS 304
Cdd:TIGR01137 240 RKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQeGQRCVVLLPDSIRNYMT 307
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
8-308 9.00e-87

cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]


Pssm-ID: 130208 [Multi-domain]  Cd Length: 290  Bit Score: 261.77  E-value: 9.00e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR01138   2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEELLKENPSYFMaEQFKNKANVKIHRETTGPEIveaI 167
Cdd:TIGR01138  82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEI---W 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 QSVGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGgkpgphkIQGIGANFIPEILDQEIYDEIIHI 247
Cdd:TIGR01138 158 QQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPG-------IRRWPTEYLPGIFDASLVDRVLDI 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011417748 248 ENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKrVVVIVPSNGERYLSTPLY 308
Cdd:TIGR01138 231 HQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLSTGVF 290
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
8-309 1.16e-84

2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274872 [Multi-domain]  Cd Length: 304  Bit Score: 256.75  E-value: 1.16e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGA--ELVLTPGAEG--MNGAVKKAEELLKENPSYFMAEQFKNKANVKIHRETTGPEI 163
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAevEKVTEPDETGgyLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 164 VEAIqsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILaGGKPGPHKIQGIGANFIPEILDQEIYDE 243
Cdd:TIGR03945 161 ARAF----PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIF-GGPPGRRHIPGLGASVVPELLDESLIDD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011417748 244 IIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLSTpLYN 309
Cdd:TIGR03945 236 VVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDT-VYN 300
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
15-296 1.17e-73

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 226.63  E-value: 1.17e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLkPGDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  95 MPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHReTTGPEIVEaiQSVGGTL 174
Cdd:cd00640    80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILE--QLGGQKP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 175 DAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPaaspilaggkpgphkiqgiganfipeildqeiydEIIHIENDDAFE 254
Cdd:cd00640   155 DAVVVPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------EVVTVSDEEALE 200
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1011417748 255 TARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVP 296
Cdd:cd00640   201 AIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILT 242
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
8-296 2.07e-71

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 222.96  E-value: 2.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEgklKPGDTIIEATSGNTGIGLAMVAAAK 87
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYFMAEQFKNKANVKIHrETTGPEIVEAI 167
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY-GTIGLEILEQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 168 qsvGGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAGG---------KPGPHKIQGIGANFIPEILDQ 238
Cdd:pfam00291 155 ---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALAL 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 239 EIY----DEIIHIENDDAFETARQVAKEEGILSGISSGAAIRA-GLQVAKQLGAGKRVVVIVP 296
Cdd:pfam00291 232 DLLdeyvGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAlKLALAGELKGGDRVVVVLT 294
PLN02356 PLN02356
phosphateglycerate kinase
1-304 9.52e-43

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 152.07  E-value: 9.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   1 MAKVVNNVTELIGGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGDTIIEATSGNTGIGL 80
Cdd:PLN02356   40 KKKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  81 AMVAAAKGYKSVIVMPETMSMERRNLLRAYGA----------------------------ELVLTPG-AEGMNGAVKKA- 130
Cdd:PLN02356  120 ATVAPAYGCKCHVVIPDDVAIEKSQILEALGAtvervrpvsithkdhyvniarrraleanELASKRRkGSETDGIHLEKt 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 131 ----EELLKENPSY-------FMAEQFKNKANVKIHRETTGPEIVEaiqSVGGTLDAFVAGIGTGGTITGTGEVLKESFP 199
Cdd:PLN02356  200 ngciSEEEKENSLFsssctggFFADQFENLANFRAHYEGTGPEIWE---QTQGNLDAFVAAAGTGGTLAGVSRFLQEKNP 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 200 GIKIVAVEPAASPIL-------------AGGK----PGPHKIQGIGANFIPEILDQEIYDEIIHIENDDAFETARQVAKE 262
Cdd:PLN02356  277 NIKCFLIDPPGSGLFnkvtrgvmytreeAEGRrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKN 356
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1011417748 263 EGILSGISSGAAIRAGLQVAKQLGAGKRVVVIVPSNGERYLS 304
Cdd:PLN02356  357 DGLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
15-295 1.50e-19

Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440784 [Multi-domain]  Cd Length: 327  Bit Score: 87.01  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDR---IAISIVEEAEKEGklkpgdTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:COG1171    25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRgayNALASLSEEERAR------GVVAASAGNHAQGVAYAARLLGIPA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  92 VIVMPETMSMERRNLLRAYGAELVLTPG--AEgmngAVKKAEELLKE---------NPSYFMAEQfknkanvkihrETTG 160
Cdd:COG1171    99 TIVMPETAPAVKVAATRAYGAEVVLHGDtyDD----AEAAAAELAEEegatfvhpfDDPDVIAGQ-----------GTIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 161 PEIVEAIQSV--------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVEPAASP-------------------I 213
Cdd:COG1171   164 LEILEQLPDLdavfvpvgGGGLIAGVAA------------ALKALSPDIRVIGVEPEGAAamyrslaagepvtlpgvdtI 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 214 ---LAGGKPGPHkiqgigaNFipEILdQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIrAGLQVAKQLGAGKR 290
Cdd:COG1171   232 adgLAVGRPGEL-------TF--EIL-RDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL-AALLAGKERLKGKR 300

                  ....*
gi 1011417748 291 VVVIV 295
Cdd:COG1171   301 VVVVL 305
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
13-299 6.38e-18

Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 83.33  E-value: 6.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:COG0498    65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGA----KTIVCASSGNGSAALAAYAARAGIEVF 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  93 IVMPET-MSMERRNLLRAYGAELVLTPGaegmN--GAVKKAEELLKENPSYFmaeqfknkANVkIH---RE---TTGPEI 163
Cdd:COG0498   141 VFVPEGkVSPGQLAQMLTYGAHVIAVDG----NfdDAQRLVKELAADEGLYA--------VNS-INparLEgqkTYAFEI 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 164 VEAIQSV-----------GGTLDAFVAGIGTGGTItgtgevLKESFPgiKIVAVEPA-ASPIL---AGGKPGPHKIQG-- 226
Cdd:COG0498   208 AEQLGRVpdwvvvptgngGNILAGYKAFKELKELG------LIDRLP--RLIAVQATgCNPILtafETGRDEYEPERPet 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 227 ------IG--ANFiPEILDqEIYD---EIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ--LGAGKRVVV 293
Cdd:COG0498   280 iapsmdIGnpSNG-ERALF-ALREsggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVV 357

                  ....*.
gi 1011417748 294 IVPSNG 299
Cdd:COG0498   358 LSTGHG 363
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
15-295 1.10e-17

Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 81.76  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIA----ISIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAAAKGYK 90
Cdd:cd01562    18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAynklLSLSEEERAKG-------VVAASAGNHAQGVAYAAKLLGIP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  91 SVIVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKEN-----PSYF----MAEQfknkanvkihrETTGP 161
Cdd:cd01562    91 ATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEgltfiHPFDdpdvIAGQ-----------GTIGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 162 EIVEAIQSV--------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVEPAASPI----LAGGKPGPHKIQG--- 226
Cdd:cd01562   158 EILEQVPDLdavfvpvgGGGLIAGIAT------------AVKALSPNTKVIGVEPEGAPAmaqsLAAGKPVTLPEVDtia 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 227 -------IGANFiPEILdQEIYDEIIHIEND-------DAFETARQVAkeEGilsgiSSGAAIRAGLQVAKQLgAGKRVV 292
Cdd:cd01562   226 dglavkrPGELT-FEII-RKLVDDVVTVSEDeiaaamlLLFEREKLVA--EP-----AGALALAALLSGKLDL-KGKKVV 295

                  ...
gi 1011417748 293 VIV 295
Cdd:cd01562   296 VVL 298
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
13-141 2.64e-16

Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.


Pssm-ID: 107206 [Multi-domain]  Cd Length: 324  Bit Score: 78.02  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:cd01563    21 GNTPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1011417748  92 VIVMPETMSMERRNLLRAYGAELVLTPGaeGMNGAVKKAEELLKENPSYF 141
Cdd:cd01563    97 VVFLPAGKALGKLAQALAYGATVLAVEG--NFDDALRLVRELAEENWIYL 144
PRK06381 PRK06381
threonine synthase; Validated
13-120 2.97e-14

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 72.05  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:PRK06381   14 GGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
                          90       100
                  ....*....|....*....|....*....
gi 1011417748  92 VIVMPETMSMERRNLLRAYGAELVLTPGA 120
Cdd:PRK06381   90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGK 118
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
8-299 1.06e-11

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 64.71  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAA 86
Cdd:TIGR00260  16 VDLGEGVTPLFRAPALAANvGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  87 KGYKSVIVMPE-TMSMERRNLLRAYGAELVltpgaeGMNG----AVKKAEELLKENPSYFMaeqfkNKANVKIHR----E 157
Cdd:TIGR00260  92 AGLKVVVLYPAgKISLGKLAQALGYNAEVV------AIDGnfddAQRLVKQLFEDKPALGL-----NSANSIPYRlegqK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 158 TTGPEIVEAIQ---------SVG--GTLDAFVAgigtggTITGTGEVLKESFPgIKIVAVEPAASPI----LAGGKPGPH 222
Cdd:TIGR00260 161 TYAFEAVEQLGweapdkvvvPVPnsGNFGAIWK------GFKEKKMLGLDSLP-VKRGIQAEGAADIvrafLEGGQWEPI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 223 KIQ---------GIGANFIPEILDQEIYDEIIHIENDDA-FETARQVAKEEGILSGISSGAAIRAGL-QVAK-QLGAGKR 290
Cdd:TIGR00260 234 ETPetlstamdiGNPANWPRALEAFRRSNGYAEDLSDEEiLEAIKLLAREEGYFVEPHSAVAVAALLkLVEKgTADPAER 313

                  ....*....
gi 1011417748 291 VVVIVPSNG 299
Cdd:TIGR00260 314 VVCALTGNG 322
PRK06608 PRK06608
serine/threonine dehydratase;
1-132 2.05e-11

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 63.64  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   1 MAKVVNNVTELIGGTPLVR---LNRIVpegSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKpgDTIIEATSGNTG 77
Cdd:PRK06608   10 IAAAHNRIKQYLHLTPIVHsesLNEML---GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLP--DKIVAYSTGNHG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011417748  78 IGLAMVAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGAEGMNGAVKKAEE 132
Cdd:PRK06608   85 QAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEE 139
PRK06815 PRK06815
threonine/serine dehydratase;
15-295 6.30e-11

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 62.02  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIA----ISIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAAAKGYK 90
Cdd:PRK06815   21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnklRLLNEAQRQQG-------VITASSGNHGQGVALAAKLAGIP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  91 SVIVMPETMSMERRNLLRAYGAELVLTPG----AEgMNGAVKKAEELLKENPSYfmaeqfkNKANVKIHRETTGPEIVEA 166
Cdd:PRK06815   94 VTVYAPEQASAIKLDAIRALGAEVRLYGGdalnAE-LAARRAAEQQGKVYISPY-------NDPQVIAGQGTIGMELVEQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 167 IqsvgGTLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPI----LAGGKPGPHKIQ---------GIGANFIP 233
Cdd:PRK06815  166 Q----PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSlytsLEAGEIVEVAEQptlsdgtagGVEPGAIT 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 234 EILDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLgAGKRVVVIV 295
Cdd:PRK06815  242 FPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY-QGKKVAVVL 302
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
15-207 1.06e-10

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 61.68  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIA---ISIVEEAEKEgklkpgDTIIEATSGNTGIGLAMVAAAKGYKS 91
Cdd:PRK08638   28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKR------KGVVACSAGNHAQGVALSCALLGIDG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  92 VIVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSYFMAEQfkNKANVKIHRETTGPEIVEAIQSV- 170
Cdd:PRK08638  102 KVVMPKGAPKSKVAATCGYGAEVVLH--GDNFNDTIAKVEEIVEEEGRTFIPPY--DDPKVIAGQGTIGLEILEDLWDVd 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1011417748 171 -------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVE 207
Cdd:PRK08638  178 tvivpigGGGLIAGIAV------------ALKSINPTIHIIGVQ 209
PRK08197 PRK08197
threonine synthase; Validated
13-119 1.33e-10

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 61.56  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDR---IAISIVEEAEKEGKLKPgdtiieaTSGNTGIGLAMVAAAKG 88
Cdd:PRK08197   78 GMTPLLPLPRLGKAlGIGRLWVKDEGLNPTGSFKARglaVGVSRAKELGVKHLAMP-------TNGNAGAAWAAYAARAG 150
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1011417748  89 YKSVIVMPETMSMERRNLLRAYGAELVLTPG 119
Cdd:PRK08197  151 IRATIFMPADAPEITRLECALAGAELYLVDG 181
PRK05638 PRK05638
threonine synthase; Validated
13-299 4.10e-10

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 60.21  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRlNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:PRK05638   65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  93 IVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSY-------FMAEQFKNKANVKIHrETTGPEIVE 165
Cdd:PRK05638  140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLNGLYnvtpeynIIGLEGQKTIAFELW-EEINPTHVI 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 166 AIQSVGGTLDAFVagigtggtiTGTGEVLK----ESFPgiKIVAVE-----PAASPILAGGK-------PGPHKIQGIGA 229
Cdd:PRK05638  217 VPTGSGSYLYSIY---------KGFKELLEigviEEIP--KLIAVQtercnPIASEILGNKTkcnetkaLGLYVKNPVMK 285
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748 230 NFIPEILDQeiYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQ--LGAGKRVVVIVPSNG 299
Cdd:PRK05638  286 EYVSEAIKE--SGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGSG 355
PRK08246 PRK08246
serine/threonine dehydratase;
15-295 5.94e-10

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 59.20  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPeGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKegklkPGDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:PRK08246   24 TPVLEADGAGF-GPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  95 MPETMSMERRNLLRAYGAELVLTPG--AEGMNGAVKKAEEllkenpSYFMAEQFKNKANVKIHRETTGPEIVEAIQSV-- 170
Cdd:PRK08246   98 VPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE------TGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVdt 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 171 ------GGTLDAFVAGIGtggtitgtgevlkesFPGIKIVAVEPAASPIL----AGGKPGPHKIQGI-----GANFIPEI 235
Cdd:PRK08246  172 vlvavgGGGLIAGIAAWF---------------EGRARVVAVEPEGAPTLhaalAAGEPVDVPVSGIaadslGARRVGEI 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748 236 LDQ--EIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAIRAGLQV-AKQLGAGKRVVVIV 295
Cdd:PRK08246  237 AFAlaRAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSgAYVPAPGERVAVVL 299
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
15-295 6.08e-10

threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130197 [Multi-domain]  Cd Length: 380  Bit Score: 59.37  E-value: 6.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKpgdTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQR---GVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  95 MPETMSMERRNLLRAYGAELVLtpgaEGMN--GAVKKAEELLKENPSYFMaEQFkNKANVKIHRETTGPEIVEAIqsvgG 172
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIL----HGDDydEAYAFATSLAEEEGRVFV-HPF-DDEFVMAGQGTIGLEIMEDI----P 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 173 TLDAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILAG----GKPGPHKI-----QGIGANFIPEI---LDQEI 240
Cdd:TIGR01127 148 DVDTVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYEslreGKIKAVESvrtiaDGIAVKKPGDLtfnIIKEY 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011417748 241 YDEIIHIeNDDAFETARQVAKEEGILSGISSGAAIRAGLQVAKQLGAGKRVVVIV 295
Cdd:TIGR01127 228 VDDVVTV-DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVL 281
PRK06110 PRK06110
threonine dehydratase;
29-115 4.05e-09

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 56.93  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  29 AEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKPGdtIIEATSGNTGIGLAMVAAAKGYKSVIVMPETMSMERRNLLR 108
Cdd:PRK06110   36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113

                  ....*..
gi 1011417748 109 AYGAELV 115
Cdd:PRK06110  114 ALGAELI 120
PRK06450 PRK06450
threonine synthase; Validated
13-143 3.14e-08

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 54.36  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  13 GGTPLVRLNrivpegsaEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSV 92
Cdd:PRK06450   57 GRTPLIKKG--------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVK 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011417748  93 IVMPETMSMERRNLLRAYGAELVltpGAEGMNGAVKKAeellKENPSYFMA 143
Cdd:PRK06450  125 IFVPETASGGKLKQIESYGAEVV---RVRGSREDVAKA----AENSGYYYA 168
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
15-293 4.12e-08

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 54.08  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPE-GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKLKpgdTIIEATSGNTGIGLAMVAAAKGYKSVI 93
Cdd:cd06446    35 TPLYRAKRLSEYlGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR---VIAETGAGQHGVATATACALFGLECEI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  94 VMPETmSMERRNL----LRAYGAELVltpgaegmngAVKKAEELLKENPSYFMAEQFKNKAN-----------------V 152
Cdd:cd06446   112 YMGAV-DVERQPLnvfrMELLGAEVV----------PVPSGSGTLKDAISEAIRDWVTNVEDthyllgsvvgphpypnmV 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 153 KIHRETTGPEIVEAIQSVGGTL-DAFVA-GIGTGGTITGTGEVLKEsfPGIKIVAVEPAASPI--------LAGGKPG-- 220
Cdd:cd06446   181 RDFQSVIGEEAKKQILEKEGELpDVVIAcVGGGSNAAGLFYPFIND--KDVKLIGVEAGGCGLetgghaayLFGGTAGvl 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 221 -----------------PHKIQ------GIGanfiPEI--LDQEIYDEIIHIENDDAFETARQVAKEEGILSGISSGAAI 275
Cdd:cd06446   259 hglkmytlqdedgqivpPHSISagldypGVG----PEHayLKDSGRVEYVAVTDEEALEAFKLLARTEGIIPALESSHAI 334
                         330
                  ....*....|....*...
gi 1011417748 276 RAGLQVAKQLGAGKRVVV 293
Cdd:cd06446   335 AYAIKLAKKLGKEKVIVV 352
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
67-137 1.06e-07

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 52.57  E-value: 1.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011417748  67 TIIEATSGNTGIGLAMVAAAKGYKSVIVMPETMSMERRNLLRAYGAELVLTPGaegmN--GAVKKAEELLKEN 137
Cdd:PRK08206  118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDG----NydDSVRLAAQEAQEN 186
PRK08329 PRK08329
threonine synthase; Validated
15-114 1.50e-06

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 49.05  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLnrivpegSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpgDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:PRK08329   65 TPTVKR-------SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
                          90       100
                  ....*....|....*....|
gi 1011417748  95 MPETMSMERRNLLRAYGAEL 114
Cdd:PRK08329  134 VSYNASKEKISLLSRLGAEL 153
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
60-172 7.14e-06

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 46.83  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  60 GKLKPGDTIIEaTSGNTGIGLAMV--AAAKGYKSVIVMPETMSMER-RNLLRAYGAELVLTpgaegmngavkkaEEllkE 136
Cdd:cd08290   142 VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT-------------EE---E 204
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1011417748 137 NPSYFMAEQFKNKanvkihretTGPEIVEAIQSVGG 172
Cdd:cd08290   205 LRSLLATELLKSA---------PGGRPKLALNCVGG 231
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
15-116 2.29e-05

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


Pssm-ID: 107209  Cd Length: 316  Bit Score: 45.37  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDR-IAISIVEEAEKEGKLKPGdtIIEATSGNTGIGLAMVAAAKGYKSVI 93
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTI 79
                          90       100
                  ....*....|....*....|...
gi 1011417748  94 VMPETMSMERRNLLRAYGAELVL 116
Cdd:cd06448    80 VVPESTKPRVVEKLRDEGATVVV 102
PRK12483 PRK12483
threonine dehydratase; Reviewed
15-215 4.65e-05

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 44.79  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIVPEGSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKlkpGDTIIEATSGNTGIGLAMVAAAKGYKSVIV 94
Cdd:PRK12483   38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQL---ARGVITASAGNHAQGVALAAARLGVKAVIV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  95 MPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSYFMAEQfkNKANVKIHRETTGPEIVEAIQsvgGTL 174
Cdd:PRK12483  115 MPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPPF--DDPDVIAGQGTVAMEILRQHP---GPL 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1011417748 175 DAFVAGIGTGGTITGTGEVLKESFPGIKIVAVEPAASPILA 215
Cdd:PRK12483  188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQ 228
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
15-215 2.76e-04

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 42.43  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVRLNRIvpegSA----EVFVKLEYQNPGSSVK-----DRIAiSIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAA 85
Cdd:PRK09224   21 TPLEKAPKL----SArlgnQVLLKREDLQPVFSFKlrgayNKMA-QLTEEQLARG-------VITASAGNHAQGVALSAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  86 AKGYKSVIVMPETMSMERRNLLRAYGAELVLTpgAEGMNGAVKKAEELLKENPSYFmaeqfknkanvkIH---------- 155
Cdd:PRK09224   89 RLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLH--GDSFDEAYAHAIELAEEEGLTF------------IHpfddpdviag 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011417748 156 RETTGPEIVEAIQSV---------GGTLDAFVAGigtggtitgtgeVLKESFPGIKIVAVEPAASPILA 215
Cdd:PRK09224  155 QGTIAMEILQQHPHPldavfvpvgGGGLIAGVAA------------YIKQLRPEIKVIGVEPEDSACLK 211
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
51-130 6.34e-04

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 40.89  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  51 SIVEEAEKEGKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSVIVMpeTMSMERRNLLRAYGAELVLTPGAEGMNGAVKKA 130
Cdd:COG1063   148 AVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVV--DRNPERLELARELGADAVVNPREEDLVEAVREL 225
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
60-121 9.03e-04

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 40.38  E-value: 9.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011417748  60 GKLKPGDTIieATSGNTGIGLAMVAAAKGYKSVIVMPEtMSMERRNLLRAYGAELVLTPGAE 121
Cdd:cd05188   130 GVLKPGDTV--LVLGAGGVGLLAAQLAKAAGARVIVTD-RSDEKLELAKELGADHVIDYKEE 188
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
60-118 1.01e-03

Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 40.47  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1011417748  60 GKLKPGDTIIEATSGNTGIGLAMVAAAKGYKSVIVMpeTMSMERRNLLRAYGAELVLTP 118
Cdd:cd08256   170 ANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVL--DLKDERLALARKFGADVVLNP 226
PRK07334 PRK07334
threonine dehydratase; Provisional
15-116 1.26e-03

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 40.26  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  15 TPLVR---LNRIVpegSAEVFVKLEYQNPGSSVKDRIAI----SIVEEAEKEGklkpgdtIIEATSGNTGIGLAMVAAAK 87
Cdd:PRK07334   24 TPCVHsrtLSQIT---GAEVWLKFENLQFTASFKERGALnkllLLTEEERARG-------VIAMSAGNHAQGVAYHAQRL 93
                          90       100
                  ....*....|....*....|....*....
gi 1011417748  88 GYKSVIVMPETMSMERRNLLRAYGAELVL 116
Cdd:PRK07334   94 GIPATIVMPRFTPTVKVERTRGFGAEVVL 122
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
56-129 1.86e-03

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 39.45  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011417748  56 AEKEGKLKPGDTIIEATSGNtgIGLAMVAAAKGYK-SVIVMPEtMSMERRNLLRAYGAELVLTPGAEGMNGAVKK 129
Cdd:cd08233   164 AVRRSGFKPGDTALVLGAGP--IGLLTILALKAAGaSKIIVSE-PSEARRELAEELGATIVLDPTEVDVVAEVRK 235
PLN02550 PLN02550
threonine dehydratase
30-215 3.65e-03

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 38.75  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748  30 EVFVKLEYQNPGSSVKDRIAISIVEEAEKEgKLKPGdtIIEATSGNTGIGLAMVAAAKGYKSVIVMPETMSMERRNLLRA 109
Cdd:PLN02550  125 KVLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVER 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 110 YGAELVLTpgAEGMNGAVKKAEELLKENPSYFMAEqFKNkANVKIHRETTGPEIVEAIQsvgGTLDAFVAGIGTGGTITG 189
Cdd:PLN02550  202 LGATVVLV--GDSYDEAQAYAKQRALEEGRTFIPP-FDH-PDVIAGQGTVGMEIVRQHQ---GPLHAIFVPVGGGGLIAG 274
                         170       180
                  ....*....|....*....|....*.
gi 1011417748 190 TGEVLKESFPGIKIVAVEPAASPILA 215
Cdd:PLN02550  275 IAAYVKRVRPEVKIIGVEPSDANAMA 300
PLN02569 PLN02569
threonine synthase
8-97 3.97e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 38.64  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748   8 VTELIGGTPLVRLNRIVPE--GSAEVFVKLEYQNPGSSVKDRIAISIVEEAEKEGKL-KPGDTIIEATSGNTGIGLAMVA 84
Cdd:PLN02569  127 VSLFEGNSNLFWAERLGKEflGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYC 206
                          90
                  ....*....|...
gi 1011417748  85 AAKGYKSVIVMPE 97
Cdd:PLN02569  207 AAAGIPSIVFLPA 219
PRK12391 PRK12391
TrpB-like pyridoxal phosphate-dependent enzyme;
196-293 4.23e-03

TrpB-like pyridoxal phosphate-dependent enzyme;


Pssm-ID: 237087  Cd Length: 427  Bit Score: 38.62  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417748 196 ESFPGIKIVAVEPAASPILAGG----------KPGP-HKIQGIGANFIPE--------------ILDQEIYDEIIH---I 247
Cdd:PRK12391  280 EGKKDTRFIAVEPAACPTLTKGeyaydfgdtaGLTPlLKMYTLGHDFVPPpihagglryhgmapLVSLLVHEGLIEaraY 359
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1011417748 248 ENDDAFETARQVAKEEGILSGISSGAAIRAGLQVA---KQLGAGKRVVV 293
Cdd:PRK12391  360 PQTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEAlkaKEEGEEKVILF 408
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
61-117 7.50e-03

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 37.59  E-value: 7.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1011417748  61 KLKPGDTI-IEAtsGNTGIGLAMVAAAKGYKSViVMPETMSMERRNLLRAYGAELVLT 117
Cdd:cd08243   139 GLQPGDTLlIRG--GTSSVGLAALKLAKALGAT-VTATTRSPERAALLKELGADEVVI 193
 
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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