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Conserved domains on  [gi|515629334|ref|WP_017061934|]
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MULTISPECIES: cysteine synthase A [Vibrio]

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) ...
 8-311 4.31e-169

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: 471.47  E-value: 4.31e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    8 NTLTIGNTPLVRLNKVSK--GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARG 85
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGcnANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   86 YKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLLLQQFNNPANPQIHEQTTGPEIWEAT 165
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  166 DGEIDVFVAGVGTGGTITGTSRYIKGEKGKaITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLDLEIIDR 245
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515629334  246 VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEfAGKTIVTVLPSSGERYLSTALF 311
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 ...
 8-311 4.31e-169

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: 471.47  E-value: 4.31e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    8 NTLTIGNTPLVRLNKVSK--GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARG 85
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGcnANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   86 YKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLLLQQFNNPANPQIHEQTTGPEIWEAT 165
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  166 DGEIDVFVAGVGTGGTITGTSRYIKGEKGKaITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLDLEIIDR 245
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515629334  246 VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEfAGKTIVTVLPSSGERYLSTALF 311
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 3-308 3.88e-159

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: 446.42  E-value: 3.88e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   3 KIYEDNTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAF 79
Cdd:COG0031    2 RIYDSILELIGNTPLVRLNRLSPGpgaEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDkYLLLQQFNNPANPQIHEQTTGP 159
Cdd:COG0031   82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPG-AFWPNQFENPANPEAHYETTGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 160 EIWEATDGEIDVFVAgvgtggtitgtSRYIKgEKGKAITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLD 239
Cdd:COG0031  161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLK-ERNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 240 LEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIA-ELPEfaGKTIVTVLPSSGERYLST 308
Cdd:COG0031  234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAkRLGP--GKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-322 5.94e-144

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 408.87  E-value: 5.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   2 SKIYEDNTLTIGNTPLVRLNKVSK---GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALA 78
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRASEatgCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  79 FVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAP------KGMNGAIAKAEEIVASDPDKYLLLQQFNNPANPQI 152
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 153 HEQTTGPEIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQALAGEEIKPAPHKIQGIGAG 232
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLK-ETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 233 FIPGNLDLEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAElPEFAGKTIVTVLPSSGERYLSTALFA 312
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAR-ELGPGHTIVTILCDSGERYQSKLFNP 318

                        330
                 ....*....|
gi 515629334 313 GIFTEKENQQ 322
Cdd:PRK10717 319 DFLREKGLPV 328
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 13-307 1.69e-138

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: 393.80  E-value: 1.69e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  13 GNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARGYKLT 89
Cdd:cd01561    1 GNTPLVRLNRLSPGtgaEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  90 LTMPESMSLERRKLLKALGANLVLTEAPK--GMNGAIAKAEEIVASDPDkYLLLQQFNNPANPQIHEQTTGPEIWEATDG 167
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 168 EIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIaqalagEEIKPAPHKIQGIGAGFIPGNLDLEIIDRVE 247
Cdd:cd01561  160 KVDAFVAGVGTGGTITGVARYLK-EKNPNVRIVGVDPVGSVLF------SGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 248 SVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEfAGKTIVTVLPSSGERYLS 307
Cdd:cd01561  233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 9-299 1.28e-67

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: 213.33  E-value: 1.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    9 TLTIGNTPLVRLNKVSK---GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAgtlKPGIELVEPTSGNTGVALAFVAAARG 85
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKelgVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   86 YKLTLTMPESMSLERRKLLKALGANLVLTEApkGMNGAIAKAEEIvASDPDKYLLLQQFNNPANPQIHEqTTGPEIWEAT 165
Cdd:pfam00291  79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAAREL-AAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  166 DGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQALAG---EEIKPAPHKIQGIGAGFIPGNLDLEI 242
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLK-ELGPDVRVIGVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALDL 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515629334  243 IDR----VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAAnRIAELPEFAGK-TIVTVLP 299
Cdd:pfam00291 234 LDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL-KLALAGELKGGdRVVVVLT 294
 
Name Accession Description Interval E-value
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 8-311 4.31e-169

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: 471.47  E-value: 4.31e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    8 NTLTIGNTPLVRLNKVSK--GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARG 85
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGcnANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   86 YKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLLLQQFNNPANPQIHEQTTGPEIWEAT 165
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  166 DGEIDVFVAGVGTGGTITGTSRYIKGEKGKaITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLDLEIIDR 245
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515629334  246 VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEfAGKTIVTVLPSSGERYLSTALF 311
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 8-311 5.76e-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: 448.27  E-value: 5.76e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    8 NTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAAR 84
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGcdaRVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   85 GYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDpDKYLLLQQFNNPANPQIHEQTTGPEIWEA 164
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAET-NKYVMLDQFENPANPEAHYKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  165 TDGEIDVFVAGVGTGGTITGTSRYIKGEKGKaITSVAVEPAESPVIAQALAGeeikpaPHKIQGIGAGFIPGNLDLEIID 244
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNPN-IQIVAVEPAESPVLSGGEPG------PHKIQGIGAGFIPKILDLSLID 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515629334  245 RVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFAGKTIVTVLPSSGERYLSTALF 311
Cdd:TIGR01136 233 EVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 3-308 3.88e-159

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: 446.42  E-value: 3.88e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   3 KIYEDNTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAF 79
Cdd:COG0031    2 RIYDSILELIGNTPLVRLNRLSPGpgaEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDkYLLLQQFNNPANPQIHEQTTGP 159
Cdd:COG0031   82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPG-AFWPNQFENPANPEAHYETTGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 160 EIWEATDGEIDVFVAgvgtggtitgtSRYIKgEKGKAITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLD 239
Cdd:COG0031  161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLK-ERNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 240 LEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIA-ELPEfaGKTIVTVLPSSGERYLST 308
Cdd:COG0031  234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAkRLGP--GKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-322 5.94e-144

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 408.87  E-value: 5.94e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   2 SKIYEDNTLTIGNTPLVRLNKVSK---GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALA 78
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRASEatgCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  79 FVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAP------KGMNGAIAKAEEIVASDPDKYLLLQQFNNPANPQI 152
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAApyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 153 HEQTTGPEIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQALAGEEIKPAPHKIQGIGAG 232
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLK-ETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 233 FIPGNLDLEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAElPEFAGKTIVTVLPSSGERYLSTALFA 312
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAR-ELGPGHTIVTILCDSGERYQSKLFNP 318

                        330
                 ....*....|
gi 515629334 313 GIFTEKENQQ 322
Cdd:PRK10717 319 DFLREKGLPV 328
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 13-307 1.69e-138

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: 393.80  E-value: 1.69e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  13 GNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARGYKLT 89
Cdd:cd01561    1 GNTPLVRLNRLSPGtgaEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  90 LTMPESMSLERRKLLKALGANLVLTEAPK--GMNGAIAKAEEIVASDPDkYLLLQQFNNPANPQIHEQTTGPEIWEATDG 167
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 168 EIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIaqalagEEIKPAPHKIQGIGAGFIPGNLDLEIIDRVE 247
Cdd:cd01561  160 KVDAFVAGVGTGGTITGVARYLK-EKNPNVRIVGVDPVGSVLF------SGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 248 SVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEfAGKTIVTVLPSSGERYLS 307
Cdd:cd01561  233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PLN02565 PLN02565
cysteine synthase
 2-320 6.31e-118

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 342.67  E-value: 6.31e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   2 SKIYEDNTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIE-LVEPTSGNTGVAL 77
Cdd:PLN02565   3 SSIAKDVTELIGKTPLVYLNNVVDGcvaRIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  78 AFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLLlQQFNNPANPQIHEQTT 157
Cdd:PLN02565  83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYIL-QQFENPANPKIHYETT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 158 GPEIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGN 237
Cdd:PLN02565 162 GPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLK-EQNPDIKLYGVEPVESAVLSGG------KPGPHKIQGIGAGFIPGV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 238 LDLEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFAGKTIVTVLPSSGERYLSTALFAGIFTE 317
Cdd:PLN02565 235 LDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKE 314


                 ...
gi 515629334 318 KEN 320
Cdd:PLN02565 315 AEN 317
PLN00011 PLN00011
cysteine synthase
 4-320 3.37e-107

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 315.40  E-value: 3.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   4 IYEDNTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIE-LVEPTSGNTGVALAF 79
Cdd:PLN00011   7 IKNDVTELIGNTPMVYLNNIVDGcvaRIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKStLIEATAGNTGIGLAC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLLlQQFNNPANPQIHEQTTGP 159
Cdd:PLN00011  87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIP-QQFENPANPEIHYRTTGP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 160 EIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLD 239
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLK-EKNKDIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNLD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 240 LEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFAGKTIVTVLPSSGERYLSTALFAGIFTEKE 319
Cdd:PLN00011 239 LTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAE 318


                 .
gi 515629334 320 N 320
Cdd:PLN00011 319 N 319
PLN03013 PLN03013
cysteine synthase
 4-322 3.64e-106

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 316.72  E-value: 3.64e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   4 IYEDNTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIE-LVEPTSGNTGVALAF 79
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGcvaNIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSvLVEPTSGNTGIGLAF 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  80 VAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYlLLQQFNNPANPQIHEQTTGP 159
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAY-MLQQFDNPANPKIHYETTGP 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 160 EIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGNLD 239
Cdd:PLN03013 272 EIWDDTKGKVDIFVAGIGTGGTITGVGRFIK-EKNPKTQVIGVEPTESDILSGG------KPGPHKIQGIGAGFIPKNLD 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 240 LEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFAGKTIVTVLPSSGeRYLSTALFAGIFTEKE 319
Cdd:PLN03013 345 QKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRW 423


                 ...
gi 515629334 320 NQQ 322
Cdd:PLN03013 424 RKC 426
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 2-322 2.08e-101

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 302.26  E-value: 2.08e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   2 SKIYEDNTLTIGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPG-IELVEPTSGNTGVAL 77
Cdd:PLN02556  47 TKIKTDASQLIGKTPLVYLNKVTEGcgaYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGISL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  78 AFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLLlQQFNNPANPQIHEQTT 157
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFML-QQFSNPANTQVHFETT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 158 GPEIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQAlageeiKPAPHKIQGIGAGFIPGN 237
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLK-SKNPNVKIYGVEPAESNVLNGG------KPGPHHITGNGVGFKPDI 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 238 LDLEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFAGKTIVTVLPSSGERYLSTALFAGIFTE 317
Cdd:PLN02556 279 LDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKE 358


                 ....*
gi 515629334 318 KENQQ 322
Cdd:PLN02556 359 AENMQ 363
cysM PRK11761
cysteine synthase CysM;
11-311 1.17e-95

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 285.23  E-value: 1.17e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  11 TIGNTPLVRLNKVSKGN---VLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARGYK 87
Cdd:PRK11761   9 TIGNTPLVKLQRLPPDRgntILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  88 LTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASdpDKYLLLQQFNNPANPQIHEQTTGPEIWEATDG 167
Cdd:PRK11761  89 MKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAE--GEGKVLDQFANPDNPLAHYETTGPEIWRQTEG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 168 EIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAqalageeikpaphkiqGI---GAGFIPGNLDLEIID 244
Cdd:PRK11761 167 RITHFVSSMGTTGTIMGVSRYLK-EQNPAVQIVGLQPEEGSSIP----------------GIrrwPEEYLPKIFDASRVD 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515629334 245 RVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAElpEFAGKTIVTVLPSSGERYLSTALF 311
Cdd:PRK11761 230 RVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAR--ENPNAVIVAIICDRGDRYLSTGVF 294
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 12-307 1.59e-82

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: 257.04  E-value: 1.59e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   12 IGNTPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARGYKL 88
Cdd:TIGR01137   9 IGNTPLVRLNKVSKGlkcELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   89 TLTMPESMSLERRKLLKALGANLVLTE---APKGMNGAIAKAEEIVASDPDKYlLLQQFNNPANPQIHEQTTGPEIWEAT 165
Cdd:TIGR01137  89 IIVLPEKMSSEKVDVLRALGAEIVRTPtaaAFDSPESHIGVAKRLVREIPGAH-ILDQYRNPSNPLAHYDTTGPEILEQC 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  166 DGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPaESPVIAQALAGEEIKPAPHKIQGIGAGFIPGNLDLEIIDR 245
Cdd:TIGR01137 168 EGKLDMFVAGVGTGGTITGIARYLK-ESCPGCRIVGADP-EGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDE 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515629334  246 VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFAGKTIVTVLPSSGERYLS 307
Cdd:TIGR01137 246 WIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMT 307
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 11-311 1.88e-79

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: 243.67  E-value: 1.88e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   11 TIGNTPLVRLNKVSKGN---VLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARGYK 87
Cdd:TIGR01138   5 TVGNTPLVRLQRMGPENgseVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   88 LTLTMPESMSLERRKLLKALGANLVLTEAPKGMNGAIAKAEEIVASDPDKYLllQQFNNPANPQIHEQTTGPEIWEATDG 167
Cdd:TIGR01138  85 MKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL--DQFNNPDNPYAHYTSTGPEIWQQTGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  168 EIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIaqalagEEIKPAPHKIqgigagfIPGNLDLEIIDRVE 247
Cdd:TIGR01138 163 RITHFVSSMGTTGTIMGVSRFLK-EQNPPVQIVGLQPEEGSSI------PGIRRWPTEY-------LPGIFDASLVDRVL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515629334  248 SVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAElpEFAGKTIVTVLPSSGERYLSTALF 311
Cdd:TIGR01138 229 DIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLAR--ELPDAVVVAIICDRGDRYLSTGVF 290
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 9-299 1.28e-67

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: 213.33  E-value: 1.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    9 TLTIGNTPLVRLNKVSK---GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAgtlKPGIELVEPTSGNTGVALAFVAAARG 85
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKelgVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   86 YKLTLTMPESMSLERRKLLKALGANLVLTEApkGMNGAIAKAEEIvASDPDKYLLLQQFNNPANPQIHEqTTGPEIWEAT 165
Cdd:pfam00291  79 LKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAAREL-AAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  166 DGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESPVIAQALAG---EEIKPAPHKIQGIGAGFIPGNLDLEI 242
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLK-ELGPDVRVIGVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALDL 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515629334  243 IDR----VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAAnRIAELPEFAGK-TIVTVLP 299
Cdd:pfam00291 234 LDEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL-KLALAGELKGGdRVVVVLT 294
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 15-301 2.62e-59

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: 190.42  E-value: 2.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  15 TPLVRLNKVSKG---NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIeLVEPTSGNTGVALAFVAAARGYKLTLT 91
Cdd:cd00640    1 TPLVRLKRLSKLggaNIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGV-IIESTGGNTGIALAAAAARLGLKCTIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  92 MPESMSLERRKLLKALGANLVLTEApkGMNGAIAKAEEIVASDPdKYLLLQQFNNPANPQIHeQTTGPEIWEATDGE-ID 170
Cdd:cd00640   80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDP-GAYYVNQFDNPANIAGQ-GTIGLEILEQLGGQkPD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 171 VFVAgvgtggtitgtsryikgekgkaitsvavepaesPV-----IAqalageeikpaphkiqGIGAGFIPGNLDLEII-- 243
Cdd:cd00640  156 AVVV---------------------------------PVggggnIA----------------GIARALKELLPNVKVIgv 186

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515629334 244 -DRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEfAGKTIVTVLPSS 301
Cdd:cd00640  187 ePEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTGG 244
PLN02356 PLN02356
phosphateglycerate kinase
 12-307 2.10e-39

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 143.59  E-value: 2.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  12 IGNTPLVRLNKVSKGN---VLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIELVEPTSGNTGVALAFVAAARGYKL 88
Cdd:PLN02356  51 IGNTPLIRINSLSEATgceILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKC 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  89 TLTMPESMSLERRKLLKALGAN--------------------------------LVLTEAPKG-----MNGAIAKAEE-- 129
Cdd:PLN02356 131 HVVIPDDVAIEKSQILEALGATvervrpvsithkdhyvniarrraleanelaskRRKGSETDGihlekTNGCISEEEKen 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 130 -IVASDPDKYLLLQQFNNPANPQIHEQTTGPEIWEATDGEIDVFVAGVGTGGTITGTSRYIKgEKGKAITSVAVEPAESP 208
Cdd:PLN02356 211 sLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQ-EKNPNIKCFLIDPPGSG 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 209 VIAQALAG-----EEIK------PAPHKIQGIGAGFIPGNLDLEIIDRVESVTSEEAIEMAQRLMKEEGILAGISSGAAV 277
Cdd:PLN02356 290 LFNKVTRGvmytrEEAEgrrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNC 369

                        330       340       350
                 ....*....|....*....|....*....|
gi 515629334 278 VAANRIAELPEfAGKTIVTVLPSSGERYLS 307
Cdd:PLN02356 370 VGAVRVAQSLG-PGHTIVTILCDSGMRHLS 398
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 15-298 1.46e-14

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: 73.15  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  15 TPLVRLNKVSK---GNVLAKIEARNPSFSVKCRIGSNMIW---EAEKAGTLkpgielVEPTSGNTGVALAFVAAARGYKL 88
Cdd:COG1171   25 TPLLRSPTLSErlgAEVYLKLENLQPTGSFKLRGAYNALAslsEEERARGV------VAASAGNHAQGVAYAARLLGIPA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  89 TLTMPESMSLERRKLLKALGANLVLTeapkGMNG--AIAKAEEIVASdpDKYLLLQQFNNPAnpQIHEQTT-GPEIWEAT 165
Cdd:COG1171   99 TIVMPETAPAVKVAATRAYGAEVVLH----GDTYddAEAAAAELAEE--EGATFVHPFDDPD--VIAGQGTiALEILEQL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 166 dGEID-VFV-----------AGvgtggtitgtsrYIKgEKGKAITSVAVEPAESPVIAQALAGEEIKPAPH--KI-QGIG 230
Cdd:COG1171  171 -PDLDaVFVpvggggliagvAA------------ALK-ALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGvdTIaDGLA 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515629334 231 AGfIPGNLDLEII----DRVESVtSEEAIEMAQR-LMKEEGILAGiSSGAAVVAAnRIAELPEFAGKTIVTVL 298
Cdd:COG1171  237 VG-RPGELTFEILrdlvDDIVTV-SEDEIAAAMRlLLERTKIVVE-PAGAAALAA-LLAGKERLKGKRVVVVL 305
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 15-302 5.84e-14

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: 70.98  E-value: 5.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  15 TPLVR---LNKVSKGNVLAKIEARNPSFSVKCRIGSNMIW---EAEKAGtlkpGIelVEPTSGNTGVALAFVAAARGYKL 88
Cdd:cd01562   18 TPLLTsptLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLslsEEERAK----GV--VAASAGNHAQGVAYAAKLLGIPA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  89 TLTMPESMSLERRKLLKALGANLVLTEApkGMNGAIAKAEEIVASdpDKYLLLQQFNNPAnpQIHEQ-TTGPEIWEATdG 167
Cdd:cd01562   92 TIVMPETAPAAKVDATRAYGAEVVLYGE--DFDEAEAKARELAEE--EGLTFIHPFDDPD--VIAGQgTIGLEILEQV-P 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 168 EID-VFV-----------AGvgtggtitgtsrYIKGEKGKaITSVAVEPAESPVIAQALAGEEIKPAPH--KIQGIGAGF 233
Cdd:cd01562  165 DLDaVFVpvggggliagiAT------------AVKALSPN-TKVIGVEPEGAPAMAQSLAAGKPVTLPEvdTIADGLAVK 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515629334 234 IPGNLDLEII----DRVESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAAnrIAELPEFAGKTIVTVLpsSG 302
Cdd:cd01562  232 RPGELTFEIIrklvDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAAL--LSGKLDLKGKKVVVVL--SG 300
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 9-302 1.09e-11

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: 64.54  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   9 TLTIGNTPLVRLNKVSK----GNVLAKIEARNPSFSVKCRiGSNMIWEAEKAGTLKpgiELVEPTSGNTGVALAFVAAAR 84
Cdd:cd01563   17 SLGEGNTPLVRAPRLGErlggKNLYVKDEGLNPTGSFKDR-GMTVAVSKAKELGVK---AVACASTGNTSASLAAYAARA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  85 GYKLTLTMPESMSLErrKLLKAL--GANLVlteapkGMNGAIAKAEEIVASDPDKYLLLqqFNNPANPQIHE--QTTGPE 160
Cdd:cd01563   93 GIKCVVFLPAGKALG--KLAQALayGATVL------AVEGNFDDALRLVRELAEENWIY--LSNSLNPYRLEgqKTIAFE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 161 IWEATDGEI-DVFVAgvgTGGTITGTSRYIKG-----EKGKaITS----VAVEPAESPVIAQAL--AGEEIKP--APHKI 226
Cdd:cd01563  163 IAEQLGWEVpDYVVV---PVGNGGNITAIWKGfkelkELGL-IDRlprmVGVQAEGAAPIVRAFkeGKDDIEPveNPETI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 227 -QGIGAGFiPGNLD--LEIIDR----VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEFA-GKTIVTVL 298
Cdd:cd01563  239 aTAIRIGN-PASGPkaLRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDkGERVVVVL 317


                 ....
gi 515629334 299 PSSG 302
Cdd:cd01563  318 TGHG 321
PRK06815 PRK06815
threonine/serine dehydratase;
15-298 1.67e-10

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 60.86  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  15 TPL---VRLNKVSKGNVLAKIEARNPSFSVKCRIGSNMIW----EAEKAGtlkpgieLVEPTSGNTGVALAFVAAARGYK 87
Cdd:PRK06815  21 TPLehsPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRllneAQRQQG-------VITASSGNHGQGVALAAKLAGIP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  88 LTLTMPESMSLERRKLLKALGANLVLteAPKGMNGAIAKAEEIVASDPDKYLllqqfnNPAN-PQI--HEQTTGPEIWEA 164
Cdd:PRK06815  94 VTVYAPEQASAIKLDAIRALGAEVRL--YGGDALNAELAARRAAEQQGKVYI------SPYNdPQViaGQGTIGMELVEQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 165 TDGEIDVFVAGVGTGGTITGTSrYIKgEKGKAITSVAVEPAESPVIAQAL-AGEEIKPA--PHKIQGIGAGFIPGNLDLE 241
Cdd:PRK06815 166 QPDLDAVFVAVGGGGLISGIAT-YLK-TLSPKTEIIGCWPANSPSLYTSLeAGEIVEVAeqPTLSDGTAGGVEPGAITFP 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515629334 242 IIDRV--ESVT-SEEAIEMAQRLM--KEEGILAGiSSGAAVVAANRIAelPEFAGKTIVTVL 298
Cdd:PRK06815 244 LCQQLidQKVLvSEEEIKEAMRLIaeTDRWLIEG-AAGVALAAALKLA--PRYQGKKVAVVL 302
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 9-312 2.06e-10

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: 60.98  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   9 TLTIGNTPLVRLNKVSK---GNVLAKIEARNPSFSVKCRiGSNMiweaekAGT--LKPG-IELVEPTSGNTGVALAFVAA 82
Cdd:COG0498   61 SLGEGGTPLVKAPRLADelgKNLYVKEEGHNPTGSFKDR-AMQV------AVSlaLERGaKTIVCASSGNGSAALAAYAA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  83 ARGYKLTLTMPES-MSLERRKLLKALGANLVLTEapkgmnGAIAKAEEIV---ASDPDKYLLlqqfnNPANP-----QIh 153
Cdd:COG0498  134 RAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVD------GNFDDAQRLVkelAADEGLYAV-----NSINParlegQK- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 154 eqTTGPEIWEATDGEIDVFVagvgtggtitgtsrY--------IKGEKGK-------AITS----VAVEPAESPVIAQAL 214
Cdd:COG0498  202 --TYAFEIAEQLGRVPDWVV--------------VptgnggniLAGYKAFkelkelgLIDRlprlIAVQATGCNPILTAF 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 215 AGEEIKPAPHKIQGIGAG---FIPGNLD--LEIIDR----VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANR-IA 284
Cdd:COG0498  266 ETGRDEYEPERPETIAPSmdiGNPSNGEraLFALREsggtAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKlRE 345

                        330       340
                 ....*....|....*....|....*...
gi 515629334 285 ELPEFAGKTIVTVLPSSGERYLSTALFA 312
Cdd:COG0498  346 EGEIDPDEPVVVLSTGHGLKFPDAVREA 373
PRK08197 PRK08197
threonine synthase; Validated
 9-132 7.81e-08

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 53.08  E-value: 7.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   9 TLTIGNTPLVRLNKVSK----GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKpgieLVEPTSGNTGVALAFVAAAR 84
Cdd:PRK08197  74 SLGEGMTPLLPLPRLGKalgiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARA 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515629334  85 GYKLTLTMPESMSLERRKLLKALGANLVLteapkgMNGAIAKAEEIVA 132
Cdd:PRK08197 150 GIRATIFMPADAPEITRLECALAGAELYL------VDGLISDAGKIVA 191
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 14-147 6.23e-07

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: 50.38  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  14 NTPLVR---LNKVSKGNVLAKIEARNPSFSVKCR-IGsNMIWEAEKAGTLKPgIELVEPTSGNTGVALAFVAAARGYKLT 89
Cdd:cd06448    1 KTPLIEstaLSKTAGCNVFLKLENLQPSGSFKIRgIG-HLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARKLGVPCT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515629334  90 LTMPESMSLERRKLLKALGANLVLTEAPKGmNGAIAKAEEIVASDPdKYLLLQQFNNP 147
Cdd:cd06448   79 IVVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAENDP-GPVYVHPFDDP 134
PRK06450 PRK06450
threonine synthase; Validated
 9-282 2.07e-06

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 48.58  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   9 TLTIGNTPLVRlnkvsKGNVLAKIEARNPSFSVKCRIGSNMI-WEAEKagtlkpGI-ELVEPTSGNTGVALAFVAAARGY 86
Cdd:PRK06450  53 SLGEGRTPLIK-----KGNIWFKLDFLNPTGSYKDRGSVTLIsYLAEK------GIkQISEDSSGNAGASIAAYGAAAGI 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  87 KLTLTMPESMSLERRKLLKALGANLVLTEapkGMNGAIAKAEEIVASDPDKYLLLQQFNNPAnpqiheQTTGPEIWEATD 166
Cdd:PRK06450 122 EVKIFVPETASGGKLKQIESYGAEVVRVR---GSREDVAKAAENSGYYYASHVLQPQFRDGI------RTLAYEIAKDLD 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 167 GEI--DVFVAGVGTGGTITGTS----RYIKGEKGKAITSVAVEP-AESPVIAQaLAGEEIKPaPHKIQGIGAGFIPGN-- 237
Cdd:PRK06450 193 WKIpnYVFIPVSAGTLLLGVYSgfkhLLDSGVISEMPKIVAVQTeQVSPLCAK-FKGISYTP-PDKVTSIADALVSTRpf 270

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515629334 238 -LD--LEII---DRVESVTSEEAIEMAQRLMKeEGILAGISSgAAVVAANR 282
Cdd:PRK06450 271 lLDymVKALseyGECIVVSDNEIVEAWKELAK-KGLLVEYSS-ATVYAAYK 319
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 9-298 2.59e-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: 48.53  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334    9 TLTIGNTPLVRLNKVSK----GNVLAKIEARNPSFSVKCRIGSNMIweaEKAGTLKPGIELVEpTSGNTGVALAFVAAAR 84
Cdd:TIGR00260  17 DLGEGVTPLFRAPALAAnvgiKNLYVKELGHNPTLSFKDRGMAVAL---TKALELGNDTVLCA-STGNTGAAAAAYAGKA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   85 GYKLTLTMPESmSLERRKLLKALGANLVLTeapkGMNGAIAKAEEIVASDPDKYLLLqQFNNpANPQIH----EQTTGPE 160
Cdd:TIGR00260  93 GLKVVVLYPAG-KISLGKLAQALGYNAEVV----AIDGNFDDAQRLVKQLFEDKPAL-GLNS-ANSIPYrlegQKTYAFE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  161 IWEATDGE------IDVFVAGVGTGGTITGTSRYIKGEKGKAITSVAVEPAESPVIAQALAGEEIKP--APHKIQGIGAG 232
Cdd:TIGR00260 166 AVEQLGWEapdkvvVPVPNSGNFGAIWKGFKEKKMLGLDSLPVKRGIQAEGAADIVRAFLEGGQWEPieTPETLSTAMDI 245

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515629334  233 FIPGNLD--LEIIDR----VESVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEF-AGKTIVTVL 298
Cdd:TIGR00260 246 GNPANWPraLEAFRRsngyAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTAdPAERVVCAL 318
PRK06381 PRK06381
threonine synthase; Validated
 1-117 8.75e-06

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 46.62  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   1 MSKIYEDNTLTIGNTPLVRLNKVSK----GNVLAKIEARNPSFSVKCRIGSNMIWEAEKAG--TLKPGielvepTSGNTG 74
Cdd:PRK06381   2 EEELSSSEEKPPGGTPLLRARKLEEelglRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGysGITVG------TCGNYG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515629334  75 VALAFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEAP 117
Cdd:PRK06381  76 ASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGK 118
PRK08246 PRK08246
serine/threonine dehydratase;
61-280 1.66e-05

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 45.72  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  61 PGIELVEPTSGNTGVALAFVAAARGYKLTLTMPESMSLERRKLLKALGANLVLTEA--PKGMNGAIAKAEEIVAsdpdky 138
Cdd:PRK08246  67 PAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAETGA------ 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 139 LLLQQFNNPanPQIHEQ-TTGPEIwEATDGEID-VFVAGVGTGGTITGTSRYikgekGKAITSVAVEPAESPVIAQALAG 216
Cdd:PRK08246 141 LLCHAYDQP--EVLAGAgTLGLEI-EEQAPGVDtVLVAVGGGGLIAGIAAWF-----EGRARVVAVEPEGAPTLHAALAA 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515629334 217 EEikPAPHKIQGIGAGFIP----GNLDLEIIDR--VESV-TSEEAIEMAQRLMKEEGILAGISSGAAVVAA 280
Cdd:PRK08246 213 GE--PVDVPVSGIAADSLGarrvGEIAFALARAhvVTSVlVSDEAIIAARRALWEELRLAVEPGAATALAA 281
PRK05638 PRK05638
threonine synthase; Validated
 9-302 5.79e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 44.42  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334   9 TLTIGNTPLVRLNKVSKG--NVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKpgieLVEPTSGNTGVALAFVAAARGY 86
Cdd:PRK05638  61 SLGEGGTPLIRARISEKLgeNVYIKDETRNPTGSFRDRLATVAVSYGLPYAANG----FIVASDGNAAASVAAYSARAGK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  87 KLTLTMPESMSLERRKLLKALGANLVLTEapKGMNGAIAKAEEIV-------ASDPDKYLLLQQfnnpanpqihEQTTGP 159
Cdd:PRK05638 137 EAFVVVPRKVDKGKLIQMIAFGAKIIRYG--ESVDEAIEYAEELArlnglynVTPEYNIIGLEG----------QKTIAF 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334 160 EIWEATdGEIDVFVAGVGTGGTITGTSRYIKGEKGKAITS----VAVEPAESPVIAQALAGEEIKPAPHKIQGIGA-GFI 234
Cdd:PRK05638 205 ELWEEI-NPTHVIVPTGSGSYLYSIYKGFKELLEIGVIEEipklIAVQTERCNPIASEILGNKTKCNETKALGLYVkNPV 283

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515629334 235 PGNLDLEIIDRVES---VTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAELPEF-AGKTIVTVLPSSG 302
Cdd:PRK05638 284 MKEYVSEAIKESGGtavVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIeKGDKVVLVVTGSG 355
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
15-134 1.29e-04

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 43.19  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  15 TPLVRLNKVS---KGNVLAKIEARNPSFSVKCRIGSNMI---WEAEKagtlKPGIelVEPTSGNTGVALAFVAAARGYKL 88
Cdd:PRK08638  28 TPLPRSNYLSercKGEIFLKLENMQRTGSFKIRGAFNKLsslTDAEK----RKGV--VACSAGNHAQGVALSCALLGIDG 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515629334  89 TLTMPESMSLERRKLLKALGANLVLteAPKGMNGAIAKAEEIVASD 134
Cdd:PRK08638 102 KVVMPKGAPKSKVAATCGYGAEVVL--HGDNFNDTIAKVEEIVEEE 145
PRK06608 PRK06608
serine/threonine dehydratase;
15-114 3.69e-04

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 41.68  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  15 TPLVR---LNKVSKGNVLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIelVEPTSGNTGVALAFVAAARGYKLTLT 91
Cdd:PRK06608  24 TPIVHsesLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPDKI--VAYSTGNHGQAVAYASKLFGIKTRIY 101

                         90       100
                 ....*....|....*....|...
gi 515629334  92 MPESMSLERRKLLKALGANLVLT 114
Cdd:PRK06608 102 LPLNTSKVKQQAALYYGGEVILT 124
PRK08329 PRK08329
threonine synthase; Validated
 10-111 2.37e-03

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 39.42  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  10 LTIGNTPLVRLNKvskgNVLAKIEARNPSFSVKCRIGSNMIweaekAGTLKPGI-ELVEPTSGNTGVALAFVAAARGYKL 88
Cdd:PRK08329  60 LTPPITPTVKRSI----KVYFKLDYLQPTGSFKDRGTYVTV-----AKLKEEGInEVVIDSSGNAALSLALYSLSEGIKV 130

                         90       100
                 ....*....|....*....|...
gi 515629334  89 TLTMPESMSLERRKLLKALGANL 111
Cdd:PRK08329 131 HVFVSYNASKEKISLLSRLGAEL 153
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
 243-297 3.28e-03

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 38.89  E-value: 3.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515629334 243 IDRVE--SVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIAelPEFAGKTIVTV 297
Cdd:PRK04346 322 IGRAEyvSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLA--PTLGKDQIIVV 376
PRK06110 PRK06110
threonine dehydratase;
28-112 3.69e-03

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 38.44  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515629334  28 VLAKIEARNPSFSVKCRIGSNMIWEAEKAGTLKPGIelVEPTSGNTGVALAFVAAARGYKLTLTMPESMSLERRKLLKAL 107
Cdd:PRK06110  38 VWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRGV--ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRAL 115


                 ....*
gi 515629334 108 GANLV 112
Cdd:PRK06110 116 GAELI 120
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 245-295 4.18e-03

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: 38.67  E-value: 4.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515629334 245 RVE--SVTSEEAIEMAQRLMKEEGILAGISSGAAVVAANRIA-ELPEfaGKTIV 295
Cdd:cd06446  300 RVEyvAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAkKLGK--EKVIV 351
 
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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