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Conserved domains on  [gi|2055789164|emb|CAD6510529|]
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Cysteine synthase A [Candidatus Profftia tarda]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 25-328 8.21e-161

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.


The actual alignment was detected with superfamily member TIGR01139:

Pssm-ID: 444852  Cd Length: 298  Bit Score: 450.67  E-value: 8.21e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  25 NSLTVGHSPLVRLNRI--GNGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRG 102
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIegCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 103 YKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFLLLEQFSNPANPEIHEKTTGPEIWEDT 182
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 183 GGEVDVLVSGVGTGGTLTGTTNYLKNIKGkKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPGFIPDNLDLNLIDR 262
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKP-NIKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055789164 263 VERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSSGERYLSTDLF 328
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
 
Name Accession Description Interval E-value
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 25-328 8.21e-161

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: 450.67  E-value: 8.21e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  25 NSLTVGHSPLVRLNRI--GNGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRG 102
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIegCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 103 YKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFLLLEQFSNPANPEIHEKTTGPEIWEDT 182
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 183 GGEVDVLVSGVGTGGTLTGTTNYLKNIKGkKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPGFIPDNLDLNLIDR 262
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKP-NIKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055789164 263 VERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSSGERYLSTDLF 328
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 20-325 4.97e-144

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: 408.28  E-value: 4.97e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  20 KIFQDNSLTVGHSPLVRLNRI--GNGC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAF 96
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLspGPGAeIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  97 VAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFlLLEQFSNPANPEIHEKTTGP 176
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAF-WPNQFENPANPEAHYETTGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 177 EIWEDTGGEVDVLV------------SGvgtggtltgttnYLKNiKGKKIITVAVEPETSPVITqalaGQEiqPGPHKIQ 244
Cdd:COG0031   161 EIWEQTDGKVDAFVagvgtggtitgvGR------------YLKE-RNPDIKIVAVEPEGSPLLS----GGE--PGPHKIE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 245 GIGPGFIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELeFTNKKIVVILPSSGERYLS 324
Cdd:COG0031   222 GIGAGFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRL-GPGKTIVTILPDSGERYLS 300


                  .
gi 2055789164 325 T 325
Cdd:COG0031   301 T 301
PRK10717 PRK10717
cysteine synthase A; Provisional
 19-329 2.43e-136

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 389.99  E-value: 2.43e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  19 SKIFQDNSLTVGHSPLVRLNRIGN--GC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALA 95
Cdd:PRK10717    1 MKIFEDVSDTIGNTPLIRLNRASEatGCeILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  96 FVAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGT------KGMKGAISKAQEIVASNPDRFLLLEQFSNPANPEI 169
Cdd:PRK10717   81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 170 HEKTTGPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQALAGQEIQPGPHKIQGIGPG 249
Cdd:PRK10717  161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKE-TNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 250 FIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELeFTNKKIVVILPSSGERYLSTDLFA 329
Cdd:PRK10717  240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAREL-GPGHTIVTILCDSGERYQSKLFNP 318
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 30-324 6.10e-127

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: 364.53  E-value: 6.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  30 GHSPLVRLNRI--GNGC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRGYKIT 106
Cdd:cd01561     1 GNTPLVRLNRLspGTGAeIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 107 LTMPDTMSLERRKLLEALGAKLVLTDGTK--GMKGAISKAQEIVASNPDrFLLLEQFSNPANPEIHEKTTGPEIWEDTGG 184
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 185 EVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQalagqeIQPGPHKIQGIGPGFIPDNLDLNLIDRVE 264
Cdd:cd01561   160 KVDAFVAGVGTGGTITGVARYLKE-KNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 265 RVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSSGERYLS 324
Cdd:cd01561   233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 26-291 4.27e-58

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: 189.06  E-value: 4.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRgllKPGIELVESTSGNTGIALAFVAASRG 102
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELgvdVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 103 YKITLTMPDTMSLERRKLLEALGAKLVLTDGtkGMKGAISKAQEIVASNPDRFlLLEQFSNPANPEIHeKTTGPEIWEDT 182
Cdd:pfam00291  79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAY-YINQYDNPLNIEGY-GTIGLEILEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 183 GGEVDVLVSGVGTGGTLTGTTNYLKNIKGK-KIItvAVEPETSPVITQALAG---QEIQPGPHKIQGIGPGFIPDNLDLN 258
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDvRVI--GVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALD 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2055789164 259 LIDR----VERVGNDDSIKMARLLMKDEGILAGISSG 291
Cdd:pfam00291 233 LLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSA 269
 
Name Accession Description Interval E-value
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 25-328 8.21e-161

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: 450.67  E-value: 8.21e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  25 NSLTVGHSPLVRLNRI--GNGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRG 102
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIegCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 103 YKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFLLLEQFSNPANPEIHEKTTGPEIWEDT 182
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 183 GGEVDVLVSGVGTGGTLTGTTNYLKNIKGkKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPGFIPDNLDLNLIDR 262
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKP-NIKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055789164 263 VERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSSGERYLSTDLF 328
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 25-328 3.04e-151

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: 426.70  E-value: 3.04e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  25 NSLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASR 101
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCdarVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 102 GYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNpDRFLLLEQFSNPANPEIHEKTTGPEIWED 181
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAET-NKYVMLDQFENPANPEAHYKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 182 TGGEVDVLVSGVGTGGTLTGTTNYLKnIKGKKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPGFIPDNLDLNLID 261
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLK-EQNPNIQIVAVEPAESPVLSGG------EPGPHKIQGIGAGFIPKILDLSLID 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055789164 262 RVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEFTNKKIVVILPSSGERYLSTDLF 328
Cdd:TIGR01136 233 EVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 20-325 4.97e-144

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: 408.28  E-value: 4.97e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  20 KIFQDNSLTVGHSPLVRLNRI--GNGC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAF 96
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLspGPGAeIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  97 VAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFlLLEQFSNPANPEIHEKTTGP 176
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAF-WPNQFENPANPEAHYETTGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 177 EIWEDTGGEVDVLV------------SGvgtggtltgttnYLKNiKGKKIITVAVEPETSPVITqalaGQEiqPGPHKIQ 244
Cdd:COG0031   161 EIWEQTDGKVDAFVagvgtggtitgvGR------------YLKE-RNPDIKIVAVEPEGSPLLS----GGE--PGPHKIE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 245 GIGPGFIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELeFTNKKIVVILPSSGERYLS 324
Cdd:COG0031   222 GIGAGFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRL-GPGKTIVTILPDSGERYLS 300


                  .
gi 2055789164 325 T 325
Cdd:COG0031   301 T 301
PRK10717 PRK10717
cysteine synthase A; Provisional
 19-329 2.43e-136

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 389.99  E-value: 2.43e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  19 SKIFQDNSLTVGHSPLVRLNRIGN--GC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALA 95
Cdd:PRK10717    1 MKIFEDVSDTIGNTPLIRLNRASEatGCeILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  96 FVAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGT------KGMKGAISKAQEIVASNPDRFLLLEQFSNPANPEI 169
Cdd:PRK10717   81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 170 HEKTTGPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQALAGQEIQPGPHKIQGIGPG 249
Cdd:PRK10717  161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKE-TNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 250 FIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELeFTNKKIVVILPSSGERYLSTDLFA 329
Cdd:PRK10717  240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAREL-GPGHTIVTILCDSGERYQSKLFNP 318
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 30-324 6.10e-127

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: 364.53  E-value: 6.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  30 GHSPLVRLNRI--GNGC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRGYKIT 106
Cdd:cd01561     1 GNTPLVRLNRLspGTGAeIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 107 LTMPDTMSLERRKLLEALGAKLVLTDGTK--GMKGAISKAQEIVASNPDrFLLLEQFSNPANPEIHEKTTGPEIWEDTGG 184
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 185 EVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQalagqeIQPGPHKIQGIGPGFIPDNLDLNLIDRVE 264
Cdd:cd01561   160 KVDAFVAGVGTGGTITGVARYLKE-KNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 265 RVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSSGERYLS 324
Cdd:cd01561   233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PLN02565 PLN02565
cysteine synthase
 19-328 6.09e-108

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 317.64  E-value: 6.09e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  19 SKIFQDNSLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIE-LVESTSGNTGIAL 94
Cdd:PLN02565    3 SSIAKDVTELIGKTPLVYLNNVVDGCvarIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  95 AFVAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFLLlEQFSNPANPEIHEKTT 174
Cdd:PLN02565   83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYIL-QQFENPANPKIHYETT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 175 GPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPGFIPDN 254
Cdd:PLN02565  162 GPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKE-QNPDIKLYGVEPVESAVLSGG------KPGPHKIQGIGAGFIPGV 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055789164 255 LDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEFTNKKIVVILPSSGERYLSTDLF 328
Cdd:PLN02565  235 LDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLF 308
PLN00011 PLN00011
cysteine synthase
 21-328 2.69e-103

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 305.77  E-value: 2.69e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  21 IFQDNSLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIE-LVESTSGNTGIALAF 96
Cdd:PLN00011    7 IKNDVTELIGNTPMVYLNNIVDGCvarIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKStLIEATAGNTGIGLAC 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  97 VAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFLLlEQFSNPANPEIHEKTTGP 176
Cdd:PLN00011   87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIP-QQFENPANPEIHYRTTGP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 177 EIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPGFIPDNLD 256
Cdd:PLN00011  166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKE-KNKDIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNLD 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055789164 257 LNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEFTNKKIVVILPSSGERYLSTDLF 328
Cdd:PLN00011  239 LTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLF 310
PLN03013 PLN03013
cysteine synthase
 5-328 4.89e-93

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 283.59  E-value: 4.89e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164   5 VIFSVFNRVNVPAMSKIFQDNSLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIE 81
Cdd:PLN03013   97 VVCEAVKRETGPDGLNIADNVSQLIGKTPMVYLNSIAKGCvanIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKS 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  82 -LVESTSGNTGIALAFVAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFlLLEQ 160
Cdd:PLN03013  177 vLVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAY-MLQQ 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 161 FSNPANPEIHEKTTGPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQAlagqeiQPGP 240
Cdd:PLN03013  256 FDNPANPKIHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKE-KNPKTQVIGVEPTESDILSGG------KPGP 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 241 HKIQGIGPGFIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEFTNKKIVVILPSSGe 320
Cdd:PLN03013  329 HKIQGIGAGFIPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG- 407


                  ....*...
gi 2055789164 321 RYLSTDLF 328
Cdd:PLN03013  408 RDIYTPRC 415
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 14-328 1.34e-92

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 280.31  E-value: 1.34e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  14 NVPAmSKIFQDNSLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPG-IELVESTSGN 89
Cdd:PLN02556   43 DLPG-TKIKTDASQLIGKTPLVYLNKVTEGCgayIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGN 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  90 TGIALAFVAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRFLLlEQFSNPANPEI 169
Cdd:PLN02556  122 MGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFML-QQFSNPANTQV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 170 HEKTTGPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSPVITQAlagqeiQPGPHKIQGIGPG 249
Cdd:PLN02556  201 HFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKS-KNPNVKIYGVEPAESNVLNGG------KPGPHHITGNGVG 273

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055789164 250 FIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEFTNKKIVVILPSSGERYLSTDLF 328
Cdd:PLN02556  274 FKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLF 352
cysM PRK11761
cysteine synthase CysM;
28-328 2.17e-88

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 266.74  E-value: 2.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  28 TVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRGYK 104
Cdd:PRK11761    9 TIGNTPLVKLQRLPPDRgntILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 105 ITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNpdRFLLLEQFSNPANPEIHEKTTGPEIWEDTGG 184
Cdd:PRK11761   89 MKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEG--EGKVLDQFANPDNPLAHYETTGPEIWRQTEG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 185 EVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPEtspvitqalAGQEIqPGphkIQGIGPGFIPDNLDLNLIDRVE 264
Cdd:PRK11761  167 RITHFVSSMGTTGTIMGVSRYLKE-QNPAVQIVGLQPE---------EGSSI-PG---IRRWPEEYLPKIFDASRVDRVL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055789164 265 RVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEftNKKIVVILPSSGERYLSTDLF 328
Cdd:PRK11761  233 DVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENP--NAVIVAIICDRGDRYLSTGVF 294
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 28-328 2.18e-74

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: 230.96  E-value: 2.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  28 TVGHSPLVRLNRIG---NGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRGYK 104
Cdd:TIGR01138   5 TVGNTPLVRLQRMGpenGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 105 ITLTMPDTMSLERRKLLEALGAKLVLTDGTKGMKGAISKAQEIVASNPDRflLLEQFSNPANPEIHEKTTGPEIWEDTGG 184
Cdd:TIGR01138  85 MKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGK--LLDQFNNPDNPYAHYTSTGPEIWQQTGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 185 EVDVLVSGVGTGGTLTGTTNYLKnIKGKKIITVAVEPETSPVItqalagqeiqPGphkIQGIGPGFIPDNLDLNLIDRVE 264
Cdd:TIGR01138 163 RITHFVSSMGTTGTIMGVSRFLK-EQNPPVQIVGLQPEEGSSI----------PG---IRRWPTEYLPGIFDASLVDRVL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055789164 265 RVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEftNKKIVVILPSSGERYLSTDLF 328
Cdd:TIGR01138 229 DIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELP--DAVVVAIICDRGDRYLSTGVF 290
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 21-324 6.63e-70

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: 224.68  E-value: 6.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  21 IFQDNSLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFV 97
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGLkceLLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  98 AASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKGM---KGAISKAQEIVASNPDRFlLLEQFSNPANPEIHEKTT 174
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAH-ILDQYRNPSNPLAHYDTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 175 GPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSpVITQALAGQEIQPGPHKIQGIGPGFIPDN 254
Cdd:TIGR01137 160 GPEILEQCEGKLDMFVAGVGTGGTITGIARYLKE-SCPGCRIVGADPEGS-ILAQPEELNQTGRTPYKVEGIGYDFIPTV 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 255 LDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEFTNKKIVVILPSSGERYLS 324
Cdd:TIGR01137 238 LDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 26-291 4.27e-58

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: 189.06  E-value: 4.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRgllKPGIELVESTSGNTGIALAFVAASRG 102
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELgvdVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 103 YKITLTMPDTMSLERRKLLEALGAKLVLTDGtkGMKGAISKAQEIVASNPDRFlLLEQFSNPANPEIHeKTTGPEIWEDT 182
Cdd:pfam00291  79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAY-YINQYDNPLNIEGY-GTIGLEILEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 183 GGEVDVLVSGVGTGGTLTGTTNYLKNIKGK-KIItvAVEPETSPVITQALAG---QEIQPGPHKIQGIGPGFIPDNLDLN 258
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDvRVI--GVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALD 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2055789164 259 LIDR----VERVGNDDSIKMARLLMKDEGILAGISSG 291
Cdd:pfam00291 233 LLDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSA 269
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 32-318 6.23e-56

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: 181.94  E-value: 6.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  32 SPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIeLVESTSGNTGIALAFVAASRGYKITLT 108
Cdd:cd00640     1 TPLVRLKRLSKLGganIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGV-IIESTGGNTGIALAAAAARLGLKCTIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 109 MPDTMSLERRKLLEALGAKLVLTDGtkGMKGAISKAQEIVASNPDRFLLLeQFSNPANPEIHeKTTGPEIWEDTGGE-VD 187
Cdd:cd00640    80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVN-QFDNPANIAGQ-GTIGLEILEQLGGQkPD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 188 VLVsgvgtggtltgttnylknikgkkiitvavepetSPVITQALAGqeiqpgphkiqGIGPGFIPDNLDLNLI---DRVE 264
Cdd:cd00640   156 AVV---------------------------------VPVGGGGNIA-----------GIARALKELLPNVKVIgvePEVV 191

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055789164 265 RVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSS 318
Cdd:cd00640   192 TVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTGG 244
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
 28-325 7.57e-53

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: 175.85  E-value: 7.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  28 TVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRGYK 104
Cdd:TIGR03945   4 LIGNTPLVKLERLFPDApfrLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 105 -ITLTMPDTmSLERRKLLEALGAKLVLT---DGTKGMKGA-ISKAQEIVASNPDRFlLLEQFSNPANPEIHEKTTGPEIW 179
Cdd:TIGR03945  84 fICVVDPNI-SPQNLKLLRAYGAEVEKVtepDETGGYLGTrIARVRELLASIPDAY-WPNQYANPDNPRAHYHGTGREIA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 180 EDTgGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSpvitqALAGQEiqPGPHKIQGIGPGFIPDNLDLNL 259
Cdd:TIGR03945 162 RAF-PTLDYLFVGVSTTGTLMGCSRRLRE-RGPNTKVIAVDAVGS-----VIFGGP--PGRRHIPGLGASVVPELLDESL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055789164 260 IDRVERVGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEfTNKKIVVILPSSGERYLST 325
Cdd:TIGR03945 233 IDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIP-EGSTVVAILPDRGERYLDT 297
PLN02356 PLN02356
phosphateglycerate kinase
 29-324 5.08e-33

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 126.64  E-value: 5.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  29 VGHSPLVRLNRI--GNGC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIELVESTSGNTGIALAFVAASRGYKI 105
Cdd:PLN02356   51 IGNTPLIRINSLseATGCeILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKC 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 106 TLTMPDTMSLERRKLLEALGA--------------------------------KLVLTDGTKG-----MKGAIS---KAQ 145
Cdd:PLN02356  131 HVVIPDDVAIEKSQILEALGAtvervrpvsithkdhyvniarrraleanelasKRRKGSETDGihlekTNGCISeeeKEN 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 146 EIVASNPDRFLLLEQFSNPANPEIHEKTTGPEIWEDTGGEVDVLVSGVGTGGTLTGTTNYLKNiKGKKIITVAVEPETSP 225
Cdd:PLN02356  211 SLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQE-KNPNIKCFLIDPPGSG 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 226 VITQALAG-----QEIQ------PGPHKIQGIGPGFIPDNLDLNLIDRVERVGNDDSIKMARLLMKDEGILAGISSGAAV 294
Cdd:PLN02356  290 LFNKVTRGvmytrEEAEgrrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNC 369

                         330       340       350
                  ....*....|....*....|....*....|
gi 2055789164 295 IAAVRIANELEfTNKKIVVILPSSGERYLS 324
Cdd:PLN02356  370 VGAVRVAQSLG-PGHTIVTILCDSGMRHLS 398
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 26-190 1.65e-12

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: 67.53  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNRIGNGC---ILAKVESRNPSFSVKDR---IGANMiwdAEKRGLlkpgIELVESTSGNTGIALAFVAA 99
Cdd:COG0498    61 SLGEGGTPLVKAPRLADELgknLYVKEEGHNPTGSFKDRamqVAVSL---ALERGA----KTIVCASSGNGSAALAAYAA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 100 SRGYKITLTMP-DTMSLERRKLLEALGAKLVLTDGT-----KGMKgAISKAQEIVASNPDRFLLLE-QfsnpanpeiheK 172
Cdd:COG0498   134 RAGIEVFVFVPeGKVSPGQLAQMLTYGAHVIAVDGNfddaqRLVK-ELAADEGLYAVNSINPARLEgQ-----------K 201

                         170
                  ....*....|....*...
gi 2055789164 173 TTGPEIWEDTGGEVDVLV 190
Cdd:COG0498   202 TYAFEIAEQLGRVPDWVV 219
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 31-319 3.50e-12

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: 65.97  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  31 HSPLVR---LNRIGNGCILAKVESRNPSFSVKDRiGA-NMIW--DAEKRgllKPGIelVESTSGNTGIALAFVAASRGYK 104
Cdd:cd01562    17 RTPLLTsptLSELLGAEVYLKCENLQKTGSFKIR-GAyNKLLslSEEER---AKGV--VAASAGNHAQGVAYAAKLLGIP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 105 ITLTMPDTMSLERRKLLEALGAKLVLTDGTkgMKGAISKAQEIVASNpdRFLLLEQFSnpaNPEIHE--KTTGPEIWEDT 182
Cdd:cd01562    91 ATIVMPETAPAAKVDATRAYGAEVVLYGED--FDEAEAKARELAEEE--GLTFIHPFD---DPDVIAgqGTIGLEILEQV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 183 gGEVDVL------------VSGvgtggtltgttnYLKNIKGK-KIItvAVEPETSPVITQALAGQEIQPGPHKIQ---GI 246
Cdd:cd01562   164 -PDLDAVfvpvggggliagIAT------------AVKALSPNtKVI--GVEPEGAPAMAQSLAAGKPVTLPEVDTiadGL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 247 G---PGFIPDNLDLNLIDRVERVgNDDSIKMA-RLLMKDEGI---------LAGISSGaaviaavrianELEFTNKKIVV 313
Cdd:cd01562   229 AvkrPGELTFEIIRKLVDDVVTV-SEDEIAAAmLLLFEREKLvaepagalaLAALLSG-----------KLDLKGKKVVV 296


                  ....*.
gi 2055789164 314 ILpsSG 319
Cdd:cd01562   297 VL--SG 300
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 26-190 5.53e-12

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: 65.69  E-value: 5.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNRI----GNGCILAKVESRNPSFSVKDRiGANM-IWDAEKRGLlkpgIELVESTSGNTGIALAFVAAS 100
Cdd:cd01563    17 SLGEGNTPLVRAPRLgerlGGKNLYVKDEGLNPTGSFKDR-GMTVaVSKAKELGV----KAVACASTGNTSASLAAYAAR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 101 RGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTkgMKGAISKAQEIVASNPdrFLLleqfSNPANPEIHE--KTTGPEI 178
Cdd:cd01563    92 AGIKCVVFLPAGKALGKLAQALAYGATVLAVEGN--FDDALRLVRELAEENW--IYL----SNSLNPYRLEgqKTIAFEI 163

                         170
                  ....*....|...
gi 2055789164 179 WEDTGGEV-DVLV 190
Cdd:cd01563   164 AEQLGWEVpDYVV 176
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 31-319 5.37e-10

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: 59.66  E-value: 5.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  31 HSPLVR---LNRIGNGCILAKVESRNPSFSVKDRIGANMIW----DAEKRGLlkpgielVESTSGNTGIALAFVAASRGY 103
Cdd:COG1171    24 RTPLLRsptLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslseEERARGV-------VAASAGNHAQGVAYAARLLGI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 104 KITLTMPDTMSLERRKLLEALGAKLVLTDGTkgMKGAISKAQEIVASN-----PDrfllleqFSNP------Anpeihek 172
Cdd:COG1171    97 PATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELAEEEgatfvHP-------FDDPdviagqG------- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 173 TTGPEIWEDTgGEVDVL------------VSGvgtggtltgttnYLKNIKgKKIITVAVEPETSPVITQALAGQEIQ--P 238
Cdd:COG1171   161 TIALEILEQL-PDLDAVfvpvggggliagVAA------------ALKALS-PDIRVIGVEPEGAAAMYRSLAAGEPVtlP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 239 GPHKI-QGIGPGFI-PDNLDL--NLIDRVERVgNDDSIKMA-RLLMKDEGI---------LAGISSGAaviaavrianeL 304
Cdd:COG1171   227 GVDTIaDGLAVGRPgELTFEIlrDLVDDIVTV-SEDEIAAAmRLLLERTKIvvepagaaaLAALLAGK-----------E 294

                         330
                  ....*....|....*
gi 2055789164 305 EFTNKKIVVILpsSG 319
Cdd:COG1171   295 RLKGKRVVVVL--SG 307
PRK06381 PRK06381
threonine synthase; Validated
 30-133 2.56e-07

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 51.63  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  30 GHSPLVRLNRIGNGC----ILAKVESRNPSFSVKDRIGANMIWDAEKRGLlkPGIELveSTSGNTGIALAFVAASRGYKI 105
Cdd:PRK06381   14 GGTPLLRARKLEEELglrkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY--SGITV--GTCGNYGASIAYFARLYGLKA 89

                          90       100
                  ....*....|....*....|....*...
gi 2055789164 106 TLTMPDTMSLERRKLLEALGAKLVLTDG 133
Cdd:PRK06381   90 VIFIPRSYSNSRVKEMEKYGAEIIYVDG 117
PRK08246 PRK08246
serine/threonine dehydratase;
78-232 3.06e-07

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 51.11  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  78 PGIELVESTSGNTGIALAFVAASRGYKITLTMPDTMSLERRKLLEALGAKLVLTDGTKG--MKGAISKAQEIVAsnpdrf 155
Cdd:PRK08246   67 PAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYAdaLEAAQAFAAETGA------ 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 156 LLLEQFSnpaNPEI--HEKTTGPEIwEDTGGEVD-VLVSGVGTGGTLTGTTNYLKNIKgkkiiTVAVEPETSPVITQALA 232
Cdd:PRK08246  141 LLCHAYD---QPEVlaGAGTLGLEI-EEQAPGVDtVLVAVGGGGLIAGIAAWFEGRAR-----VVAVEPEGAPTLHAALA 211
PRK06608 PRK06608
serine/threonine dehydratase;
29-132 3.86e-07

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 50.92  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  29 VGHSPLVR---LNRIGNGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIelVESTSGNTGIALAFVAASRGYKI 105
Cdd:PRK06608   21 LHLTPIVHsesLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPDKI--VAYSTGNHGQAVAYASKLFGIKT 98

                          90       100
                  ....*....|....*....|....*..
gi 2055789164 106 TLTMPDTMSLERRKLLEALGAKLVLTD 132
Cdd:PRK06608   99 RIYLPLNTSKVKQQAALYYGGEVILTN 125
PRK08197 PRK08197
threonine synthase; Validated
 26-149 3.91e-07

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 51.15  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNR----IGNGCILAKVESRNPSFSVKDRiGANM-IWDAEKRGLLKpgieLVESTSGNTGIALAFVAAS 100
Cdd:PRK08197   74 SLGEGMTPLLPLPRlgkaLGIGRLWVKDEGLNPTGSFKAR-GLAVgVSRAKELGVKH----LAMPTNGNAGAAWAAYAAR 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2055789164 101 RGYKITLTMP-DTMSLERRKlLEALGAKLVLTDGTkgmkgaISKAQEIVA 149
Cdd:PRK08197  149 AGIRATIFMPaDAPEITRLE-CALAGAELYLVDGL------ISDAGKIVA 191
PRK06450 PRK06450
threonine synthase; Validated
 26-135 7.70e-07

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 50.12  E-value: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRlnrigNGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLLkpgiELVESTSGNTGIALAFVAASRGYKI 105
Cdd:PRK06450   53 SLGEGRTPLIK-----KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIK----QISEDSSGNAGASIAAYGAAAGIEV 123

                          90       100       110
                  ....*....|....*....|....*....|
gi 2055789164 106 TLTMPDTMSLERRKLLEALGAKLVLTDGTK 135
Cdd:PRK06450  124 KIFVPETASGGKLKQIESYGAEVVRVRGSR 153
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 31-237 1.43e-06

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: 49.22  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  31 HSPLVR---LNRIGNGCILAKVESRNPSFSVKDR-IGaNMIWDAEKRGLLKPgIELVESTSGNTGIALAFVAASRGYKIT 106
Cdd:cd06448     1 KTPLIEstaLSKTAGCNVFLKLENLQPSGSFKIRgIG-HLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARKLGVPCT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 107 LTMPDTMSLERRKLLEALGAKLVLTdGTKGMKGAISKAQEiVASNPDRFLLLEQFSNPANPEIHeKTTGPEIWED--TGG 184
Cdd:cd06448    79 IVVPESTKPRVVEKLRDEGATVVVH-GKVWWEADNYLREE-LAENDPGPVYVHPFDDPLIWEGH-SSMVDEIAQQlqSQE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055789164 185 EVDVLVSGVGTGGTLTGTTNYLKNIKGKKIITVAVEPETSPVITQAL-AGQEIQ 237
Cdd:cd06448   156 KVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLkAGKLVT 209
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 26-286 2.81e-06

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: 48.15  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNR----IGNGCILAKVESRNPSFSVKDRIGANMIWDAEKRGLlkpgIELVESTSGNTGIALAFVAASR 101
Cdd:TIGR00260  17 DLGEGVTPLFRAPAlaanVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 102 GYKITLTMP-DTMSLErrKLLEAL--GAKLVltdgtkGMKGAISKAQEIVAS-NPDRFLLLeqfSNPANPEIH----EKT 173
Cdd:TIGR00260  93 GLKVVVLYPaGKISLG--KLAQALgyNAEVV------AIDGNFDDAQRLVKQlFEDKPALG---LNSANSIPYrlegQKT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 174 TGPEIWEDTGGEV-DVLVsgvGTGGTLTGTTNYLKNIKGKKIITVAVEPE--------TSPVITQALAGQEIQPgPHKIQ 244
Cdd:TIGR00260 162 YAFEAVEQLGWEApDKVV---VPVPNSGNFGAIWKGFKEKKMLGLDSLPVkrgiqaegAADIVRAFLEGGQWEP-IETPE 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2055789164 245 GIGPGF---IPDNLD--LNLIDR----VERVGNDDSIKMARLLMKDEGILA 286
Cdd:TIGR00260 238 TLSTAMdigNPANWPraLEAFRRsngyAEDLSDEEILEAIKLLAREEGYFV 288
PRK08329 PRK08329
threonine synthase; Validated
 26-138 3.24e-05

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 45.20  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRLNRIgngcILAKVESRNPSFSVKDRigANMIWDAEkrgLLKPGI-ELVESTSGNTGIALAFVAASRGYK 104
Cdd:PRK08329   59 HLTPPITPTVKRSIK----VYFKLDYLQPTGSFKDR--GTYVTVAK---LKEEGInEVVIDSSGNAALSLALYSLSEGIK 129

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2055789164 105 ITLTMPDTMSLERRKLLEALGAKLVLTDGTKgMK 138
Cdd:PRK08329  130 VHVFVSYNASKEKISLLSRLGAELHFVEGDR-ME 162
PRK05638 PRK05638
threonine synthase; Validated
 26-319 1.11e-04

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 43.65  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  26 SLTVGHSPLVRlNRIG---NGCILAKVESRNPSFSVKDRIGANMIWDaekrGLLKPGIELVESTSGNTGIALAFVAASRG 102
Cdd:PRK05638   61 SLGEGGTPLIR-ARISeklGENVYIKDETRNPTGSFRDRLATVAVSY----GLPYAANGFIVASDGNAAASVAAYSARAG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 103 YKITLTMPDTMSLERRKLLEALGAKLVLTDgtKGMKGAISKAQEIV-------ASNPDRFLLLEQfsnpanpeihEKTTG 175
Cdd:PRK05638  136 KEAFVVVPRKVDKGKLIQMIAFGAKIIRYG--ESVDEAIEYAEELArlnglynVTPEYNIIGLEG----------QKTIA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 176 PEIWEDTGGEvDVLVSGVGTGgtltgttnYLKNI-KG-KKIIT----------VAVEPETSPVITQALAGQEIQPGPHKI 243
Cdd:PRK05638  204 FELWEEINPT-HVIVPTGSGS--------YLYSIyKGfKELLEigvieeipklIAVQTERCNPIASEILGNKTKCNETKA 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 244 QGIgpgFIPDNLDLNLIDRVER-------VGNDDSIKMARLLMKDEGILAGISSGAAVIAAVRIANELEF-TNKKIVVIL 315
Cdd:PRK05638  275 LGL---YVKNPVMKEYVSEAIKesggtavVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIeKGDKVVLVV 351


                  ....
gi 2055789164 316 PSSG 319
Cdd:PRK05638  352 TGSG 355
PRK06815 PRK06815
threonine/serine dehydratase;
31-279 3.44e-04

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 41.99  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  31 HSPlvRLNRIGNGCILAKVESRNPSFSVKDRIGANMI--WDAEKRgllKPGIelVESTSGNTGIALAFVAASRGYKITLT 108
Cdd:PRK06815   25 HSP--LLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLrlLNEAQR---QQGV--ITASSGNHGQGVALAAKLAGIPVTVY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 109 MPDTMSLERRKLLEALGAKLVL--TDGTKGMKGAISKAQEivASNPdrfllleqFSNPAN-PEI--HEKTTGPEIWEDTG 183
Cdd:PRK06815   98 APEQASAIKLDAIRALGAEVRLygGDALNAELAARRAAEQ--QGKV--------YISPYNdPQViaGQGTIGMELVEQQP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164 184 GEVDVLVSGVGTGGTLTGTTnYLKNIKgKKIITVAVEPETSPVITQALAGQEIQPGPHK-------IQGIGPGFIPDNLD 256
Cdd:PRK06815  168 DLDAVFVAVGGGGLISGIAT-YLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQptlsdgtAGGVEPGAITFPLC 245

                         250       260
                  ....*....|....*....|...
gi 2055789164 257 LNLIDRVERVgNDDSIKMARLLM 279
Cdd:PRK06815  246 QQLIDQKVLV-SEEEIKEAMRLI 267
PRK06110 PRK06110
threonine dehydratase;
43-129 8.67e-03

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 37.67  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055789164  43 GC-ILAKVESRNPSFSVKDRIGANMIWDAEKRGLLKPGIelVESTSGNTGIALAFVAASRGYKITLTMPDTMSLERRKLL 121
Cdd:PRK06110   35 GCeVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRGV--ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAM 112


                  ....*...
gi 2055789164 122 EALGAKLV 129
Cdd:PRK06110  113 RALGAELI 120
 
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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