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Conserved domains on  [gi|488615772|ref|WP_002552621|]
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MULTISPECIES: cysteine synthase A [Pseudomonas]

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) ...
 8-313 2.45e-162

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: 454.52  E-value: 2.45e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772    8 NAHSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   88 YKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKYFMPAQFENPANPAIHEKTTGPEIWADT 167
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  168 DGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLDLSIVDR 247
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488615772  248 VERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEmQGKTIVVILPDSGERYLSSMLF 313
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 ...
 8-313 2.45e-162

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: 454.52  E-value: 2.45e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772    8 NAHSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   88 YKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKYFMPAQFENPANPAIHEKTTGPEIWADT 167
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  168 DGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLDLSIVDR 247
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488615772  248 VERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEmQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 3-310 1.26e-156

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: 439.87  E-value: 1.26e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   3 RIYADNAHSIGNTPLVQINRIAP-RGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAF 81
Cdd:COG0031    2 RIYDSILELIGNTPLVRLNRLSPgPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  82 VAAARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEkYFMPAQFENPANPAIHEKTTGP 161
Cdd:COG0031   82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPG-AFWPNQFENPANPEAHYETTGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 162 EIWADTDGAIDVLVAgvgtggtitgiSRYIKHtAGKPILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLD 241
Cdd:COG0031  161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLKE-RNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488615772 242 LSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKpEMQGKTIVVILPDSGERYLSS 310
Cdd:COG0031  234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-324 3.80e-141

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 401.93  E-value: 3.80e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   2 SRIYADNAHSIGNTPLVQINRI-APRGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLA 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAsEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  81 FVAAARGYKLMLTMPASMSIERRKVLKALGAELVLTE------PAKGMKGAIAKAEELLAGDPEKYFMPAQFENPANPAI 154
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaapyanPNNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 155 HEKTTGPEIWADTDGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAMAGEEIKPSPHKIQGIGAG 234
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK-VKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 235 FIPKNLDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKpEMQGKTIVVILPDSGERYLSSMLFS 314
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARE-LGPGHTIVTILCDSGERYQSKLFNP 318

                        330
                 ....*....|
gi 488615772 315 DLFTDQELSQ 324
Cdd:PRK10717 319 DFLREKGLPV 328
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 13-309 9.95e-140

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: 396.88  E-value: 9.95e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  13 GNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARGYKLM 91
Cdd:cd01561    1 GNTPLVRLNRLSPGtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  92 LTMPASMSIERRKVLKALGAELVLTEPAK--GMKGAIAKAEELLAGDPEkYFMPAQFENPANPAIHEKTTGPEIWADTDG 169
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 170 AIDVLVAGVGTGGTITGISRYIKhTAGKPILSVAVEPDGSPIITQamageeIKPSPHKIQGIGAGFIPKNLDLSIVDRVE 249
Cdd:cd01561  160 KVDAFVAGVGTGGTITGVARYLK-EKNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 250 RVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEmQGKTIVVILPDSGERYLS 309
Cdd:cd01561  233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-302 1.80e-65

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: 207.93  E-value: 1.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   12 IGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEssgKLKPGMTIVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:pfam00291   5 IGPTPLVRLPRLSKElGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARLGLKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   91 MLTMPASMSIERRKVLKALGAELVLTEPakGMKGAIAKAEELLAgDPEKYFMPAQFENPANPAIHeKTTGPEIWADTDGA 170
Cdd:pfam00291  82 TIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAA-EGPGAYYINQYDNPLNIEGY-GTIGLEILEQLGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  171 IDVLVAGVGTGGTITGISRYIKHTAGKPILsVAVEPDGSPIITQAMAG---EEIKPSPHKIQGIGAGFIPKNLDLSI--- 244
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRV-IGVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALDLlde 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  245 -VDRVERVTDEESKAMARRLMQEEGILCGISCGaAMAAAVRLAEKPEMQGK-TIVVILPD 302
Cdd:pfam00291 237 yVGEVVTVSDEEALEAMRLLARREGIVVEPSSA-AALAALKLALAGELKGGdRVVVVLTG 295
 
Name Accession Description Interval E-value
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 8-313 2.45e-162

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: 454.52  E-value: 2.45e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772    8 NAHSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   88 YKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKYFMPAQFENPANPAIHEKTTGPEIWADT 167
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  168 DGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLDLSIVDR 247
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488615772  248 VERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEmQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 3-310 1.26e-156

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: 439.87  E-value: 1.26e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   3 RIYADNAHSIGNTPLVQINRIAP-RGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAF 81
Cdd:COG0031    2 RIYDSILELIGNTPLVRLNRLSPgPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  82 VAAARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEkYFMPAQFENPANPAIHEKTTGP 161
Cdd:COG0031   82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPG-AFWPNQFENPANPEAHYETTGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 162 EIWADTDGAIDVLVAgvgtggtitgiSRYIKHtAGKPILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLD 241
Cdd:COG0031  161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLKE-RNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488615772 242 LSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKpEMQGKTIVVILPDSGERYLSS 310
Cdd:COG0031  234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 8-313 9.02e-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: 425.16  E-value: 9.02e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772    8 NAHSIGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAAR 86
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   87 GYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDpEKYFMPAQFENPANPAIHEKTTGPEIWAD 166
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAET-NKYVMLDQFENPANPEAHYKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  167 TDGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAMAGeeikpsPHKIQGIGAGFIPKNLDLSIVD 246
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNPN-IQIVAVEPAESPVLSGGEPG------PHKIQGIGAGFIPKILDLSLID 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488615772  247 RVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01136 233 EVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-324 3.80e-141

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 401.93  E-value: 3.80e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   2 SRIYADNAHSIGNTPLVQINRI-APRGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLA 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAsEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  81 FVAAARGYKLMLTMPASMSIERRKVLKALGAELVLTE------PAKGMKGAIAKAEELLAGDPEKYFMPAQFENPANPAI 154
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaapyanPNNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 155 HEKTTGPEIWADTDGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAMAGEEIKPSPHKIQGIGAG 234
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK-VKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 235 FIPKNLDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKpEMQGKTIVVILPDSGERYLSSMLFS 314
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARE-LGPGHTIVTILCDSGERYQSKLFNP 318

                        330
                 ....*....|
gi 488615772 315 DLFTDQELSQ 324
Cdd:PRK10717 319 DFLREKGLPV 328
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 13-309 9.95e-140

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: 396.88  E-value: 9.95e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  13 GNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARGYKLM 91
Cdd:cd01561    1 GNTPLVRLNRLSPGtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  92 LTMPASMSIERRKVLKALGAELVLTEPAK--GMKGAIAKAEELLAGDPEkYFMPAQFENPANPAIHEKTTGPEIWADTDG 169
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 170 AIDVLVAGVGTGGTITGISRYIKhTAGKPILSVAVEPDGSPIITQamageeIKPSPHKIQGIGAGFIPKNLDLSIVDRVE 249
Cdd:cd01561  160 KVDAFVAGVGTGGTITGVARYLK-EKNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 250 RVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEmQGKTIVVILPDSGERYLS 309
Cdd:cd01561  233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PLN02565 PLN02565
cysteine synthase
 2-321 5.86e-111

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 324.95  E-value: 5.86e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   2 SRIYADNAHSIGNTPLVQINRIAPRGVT-ILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTI-VEPTSGNTGIGL 79
Cdd:PLN02565   3 SSIAKDVTELIGKTPLVYLNNVVDGCVArIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  80 AFVAAARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKYFMpAQFENPANPAIHEKTT 159
Cdd:PLN02565  83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYIL-QQFENPANPKIHYETT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 160 GPEIWADTDGAIDVLVAGVGTGGTITGISRYIKHTaGKPILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKN 239
Cdd:PLN02565 162 GPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQ-NPDIKLYGVEPVESAVLSGG------KPGPHKIQGIGAGFIPGV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 240 LDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQGKTIVVILPDSGERYLSSMLFSDLFTD 319
Cdd:PLN02565 235 LDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKE 314


                 ..
gi 488615772 320 QE 321
Cdd:PLN02565 315 AE 316
PLN00011 PLN00011
cysteine synthase
 4-321 1.33e-100

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 298.84  E-value: 1.33e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   4 IYADNAHSIGNTPLVQINRIAPRGVT-ILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGM-TIVEPTSGNTGIGLAF 81
Cdd:PLN00011   7 IKNDVTELIGNTPMVYLNNIVDGCVArIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEATAGNTGIGLAC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  82 VAAARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKYfMPAQFENPANPAIHEKTTGP 161
Cdd:PLN00011  87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGY-IPQQFENPANPEIHYRTTGP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 162 EIWADTDGAIDVLVAGVGTGGTITGISRYIKHTaGKPILSVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLD 241
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKEK-NKDIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNLD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 242 LSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQGKTIVVILPDSGERYLSSMLFSDLFTDQE 321
Cdd:PLN00011 239 LTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAE 318
PLN03013 PLN03013
cysteine synthase
 6-324 2.47e-97

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 294.38  E-value: 2.47e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   6 ADN-AHSIGNTPLVQINRIAPRGVT-ILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTI-VEPTSGNTGIGLAFV 82
Cdd:PLN03013 114 ADNvSQLIGKTPMVYLNSIAKGCVAnIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  83 AAARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKYfMPAQFENPANPAIHEKTTGPE 162
Cdd:PLN03013 194 AASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAY-MLQQFDNPANPKIHYETTGPE 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 163 IWADTDGAIDVLVAGVGTGGTITGISRYIKHTAGKPILsVAVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPKNLDL 242
Cdd:PLN03013 273 IWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQV-IGVEPTESDILSGG------KPGPHKIQGIGAGFIPKNLDQ 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 243 SIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQGKTIVVILPDSGeRYLSSMLFSDLFTDQEL 322
Cdd:PLN03013 346 KIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWR 424


                 ..
gi 488615772 323 SQ 324
Cdd:PLN03013 425 KC 426
cysM PRK11761
cysteine synthase CysM;
5-315 3.69e-92

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 276.37  E-value: 3.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   5 YADNAHSIGNTPLVQINRIAP-RGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVA 83
Cdd:PRK11761   3 YPTLEDTIGNTPLVKLQRLPPdRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  84 AARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAgdPEKYFMPAQFENPANPAIHEKTTGPEI 163
Cdd:PRK11761  83 AIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQA--EGEGKVLDQFANPDNPLAHYETTGPEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 164 WADTDGAIDVLVAGVGTGGTITGISRYIKhTAGKPILSVAVEP-DGSpiitqamageeikpsphKIQGI---GAGFIPKN 239
Cdd:PRK11761 161 WRQTEGRITHFVSSMGTTGTIMGVSRYLK-EQNPAVQIVGLQPeEGS-----------------SIPGIrrwPEEYLPKI 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488615772 240 LDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEkpEMQGKTIVVILPDSGERYLSSMLFSD 315
Cdd:PRK11761 223 FDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAR--ENPNAVIVAIICDRGDRYLSTGVFPA 296
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 2-324 1.98e-88

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 269.14  E-value: 1.98e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   2 SRIYADNAHSIGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPG-MTIVEPTSGNTGIGL 79
Cdd:PLN02556  47 TKIKTDASQLIGKTPLVYLNKVTEGcGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGISL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  80 AFVAAARGYKLMLTMPASMSIERRKVLKALGAELVLTEPAKGMKGAIAKAEELLAGDPEKyFMPAQFENPANPAIHEKTT 159
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDA-FMLQQFSNPANTQVHFETT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 160 GPEIWADTDGAIDVLVAGVGTGGTITGISRYIKhtAGKPILSV-AVEPDGSPIITQAmageeiKPSPHKIQGIGAGFIPK 238
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLK--SKNPNVKIyGVEPAESNVLNGG------KPGPHHITGNGVGFKPD 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 239 NLDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQGKTIVVILPDSGERYLSSMLFSDLFT 318
Cdd:PLN02556 278 ILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRK 357


                 ....*.
gi 488615772 319 DQELSQ 324
Cdd:PLN02556 358 EAENMQ 363
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 12-312 4.31e-87

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: 268.59  E-value: 4.31e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   12 IGNTPLVQINRIAPRG-VTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:TIGR01137   9 IGNTPLVRLNKVSKGLkCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   91 MLTMPASMSIERRKVLKALGAELVLTEPAKGM---KGAIAKAEELLAGDPEKYfMPAQFENPANPAIHEKTTGPEIWADT 167
Cdd:TIGR01137  89 IIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAH-ILDQYRNPSNPLAHYDTTGPEILEQC 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  168 DGAIDVLVAGVGTGGTITGISRYIKHTAGKPILsVAVEPDGSpIITQAMAGEEIKPSPHKIQGIGAGFIPKNLDLSIVDR 247
Cdd:TIGR01137 168 EGKLDMFVAGVGTGGTITGIARYLKESCPGCRI-VGADPEGS-ILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDE 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488615772  248 VERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQGKTIVVILPDSGERYLSSML 312
Cdd:TIGR01137 246 WIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFL 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-302 1.80e-65

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: 207.93  E-value: 1.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   12 IGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEssgKLKPGMTIVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:pfam00291   5 IGPTPLVRLPRLSKElGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARLGLKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   91 MLTMPASMSIERRKVLKALGAELVLTEPakGMKGAIAKAEELLAgDPEKYFMPAQFENPANPAIHeKTTGPEIWADTDGA 170
Cdd:pfam00291  82 TIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAA-EGPGAYYINQYDNPLNIEGY-GTIGLEILEQLGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  171 IDVLVAGVGTGGTITGISRYIKHTAGKPILsVAVEPDGSPIITQAMAG---EEIKPSPHKIQGIGAGFIPKNLDLSI--- 244
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRV-IGVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALDLlde 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  245 -VDRVERVTDEESKAMARRLMQEEGILCGISCGaAMAAAVRLAEKPEMQGK-TIVVILPD 302
Cdd:pfam00291 237 yVGEVVTVSDEEALEAMRLLARREGIVVEPSSA-AALAALKLALAGELKGGdRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 15-303 2.51e-60

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: 193.12  E-value: 2.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLkPGMTIVEPTSGNTGIGLAFVAAARGYKLMLT 93
Cdd:cd00640    1 TPLVRLKRLSKLgGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  94 MPASMSIERRKVLKALGAELVLTEPakGMKGAIAKAEELLAgDPEKYFMPAQFENPANPAIHeKTTGPEIWADTDG-AID 172
Cdd:cd00640   80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAE-EDPGAYYVNQFDNPANIAGQ-GTIGLEILEQLGGqKPD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 173 VLVAgvgtggtitgisryikhtagkpilSVAVepdGSPIItqamageeikpsphkiqGIGAGFIPKNLDLSIV---DRVE 249
Cdd:cd00640  156 AVVV------------------------PVGG---GGNIA-----------------GIARALKELLPNVKVIgvePEVV 191

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488615772 250 RVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPeMQGKTIVVILPDS 303
Cdd:cd00640  192 TVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILTGG 244
PLN02356 PLN02356
phosphateglycerate kinase
 10-309 1.26e-41

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 149.37  E-value: 1.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  10 HSIGNTPLVQINRIA-PRGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARGY 88
Cdd:PLN02356  49 DAIGNTPLIRINSLSeATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGC 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  89 KLMLTMPASMSIERRKVLKALGAEL----------------------------------------VLTEPAKGMKGAIAK 128
Cdd:PLN02356 129 KCHVVIPDDVAIEKSQILEALGATVervrpvsithkdhyvniarrraleanelaskrrkgsetdgIHLEKTNGCISEEEK 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 129 AEELLAGDPEKYFMPAQFENPANPAIHEKTTGPEIWADTDGAIDVLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDG 208
Cdd:PLN02356 209 ENSLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPN-IKCFLIDPPG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 209 SPIITQAMAG-----EEIK------PSPHKIQGIGAGFIPKNLDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGA 277
Cdd:PLN02356 288 SGLFNKVTRGvmytrEEAEgrrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAM 367

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488615772 278 AMAAAVRLAEK--PemqGKTIVVILPDSGERYLS 309
Cdd:PLN02356 368 NCVGAVRVAQSlgP---GHTIVTILCDSGMRHLS 398
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 15-304 1.06e-08

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: 55.57  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRiGA-NMIWDAESSGKLKPgmtIVEPTSGNTGIGLAFVAAARGYKLML 92
Cdd:cd01562   18 TPLLTSPTLSELlGAEVYLKCENLQKTGSFKIR-GAyNKLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPATI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  93 TMPASMSIERRKVLKALGAELVLTEPakGMKGAIAKAEElLAGDPEKYFMPAqFENPANPAIHeKTTGPEIWADTdGAID 172
Cdd:cd01562   94 VMPETAPAAKVDATRAYGAEVVLYGE--DFDEAEAKARE-LAEEEGLTFIHP-FDDPDVIAGQ-GTIGLEILEQV-PDLD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 173 VLVAGVGTGGTITGISRYIKHTAGKpILSVAVEPDGSPIITQAM-AGEEIK-PSPHKIQGIGAGFIPKNLDLSI----VD 246
Cdd:cd01562  168 AVFVPVGGGGLIAGIATAVKALSPN-TKVIGVEPEGAPAMAQSLaAGKPVTlPEVDTIADGLAVKRPGELTFEIirklVD 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488615772 247 RVERVTDEESKAMARRLMQEEGILC----GISCGAAmaaavrLAEKPEMQGKTIVVILpdSG 304
Cdd:cd01562  247 DVVTVSEDEIAAAMLLLFEREKLVAepagALALAAL------LSGKLDLKGKKVVVVL--SG 300
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 13-175 5.90e-07

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: 50.58  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  13 GNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCR---IGANMiwdAESSGKLkpgmTIVEPTSGNTGIGLAFVAAARGY 88
Cdd:COG0498   65 GGTPLVKAPRLADElGKNLYVKEEGHNPTGSFKDRamqVAVSL---ALERGAK----TIVCASSGNGSAALAAYAARAGI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  89 KLMLTMPAS-MSIERRKVLKALGAELVLTEpakgmkGAIAKAEEL---LAGDPEKYfmpaqFENPANPAIHE--KTTGPE 162
Cdd:COG0498  138 EVFVFVPEGkVSPGQLAQMLTYGAHVIAVD------GNFDDAQRLvkeLAADEGLY-----AVNSINPARLEgqKTYAFE 206

                        170
                 ....*....|...
gi 488615772 163 IWADTDGAIDVLV 175
Cdd:COG0498  207 IAEQLGRVPDWVV 219
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 15-304 2.66e-06

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: 48.11  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIW---DAEssgklkPGMTIVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:COG1171   25 TPLLRSPTLSERlGAEVYLKLENLQPTGSFKLRGAYNALAslsEEE------RARGVVAASAGNHAQGVAYAARLLGIPA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  91 MLTMPASMSIERRKVLKALGAELVLTEPAkgMKGAIAKAEELlAGDPEKYFMPAqFENP------AnpaihekTTGPEIW 164
Cdd:COG1171   99 TIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAEL-AEEEGATFVHP-FDDPdviagqG-------TIALEIL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 165 ADTdGAIDVL------------VAGvgtggtitgisrYIKHTAGKPILsVAVEPDGSPIITQAMAGEEIK--PSPHKI-Q 229
Cdd:COG1171  168 EQL-PDLDAVfvpvggggliagVAA------------ALKALSPDIRV-IGVEPEGAAAMYRSLAAGEPVtlPGVDTIaD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 230 GIGAGFI-PKNLDL--SIVDRVERVTDEE-SKAMaRRLMQEEGILCGISCGaamaaaVRLA----EKPEMQGKTIVVILp 301
Cdd:COG1171  234 GLAVGRPgELTFEIlrDLVDDIVTVSEDEiAAAM-RLLLERTKIVVEPAGA------AALAallaGKERLKGKRVVVVL- 305


                 ...
gi 488615772 302 dSG 304
Cdd:COG1171  306 -SG 307
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 13-304 3.27e-06

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: 47.97  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  13 GNTPLVQINRIAPR--GVTILAKIEGRNPGYSVKCRiGANM-IWDAESSGKlkpgMTIVEPTSGNTGIGLAFVAAARGYK 89
Cdd:cd01563   21 GNTPLVRAPRLGERlgGKNLYVKDEGLNPTGSFKDR-GMTVaVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  90 LMLTMPASMSIERRKVLKALGAELVltePAKGMKGAIAKAEELLAGDPEKYFMpaqfeNPANPAIHE--KTTGPEIWADT 167
Cdd:cd01563   96 CVVFLPAGKALGKLAQALAYGATVL---AVEGNFDDALRLVRELAEENWIYLS-----NSLNPYRLEgqKTIAFEIAEQL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 168 DGAI-DVLVAGVGTGGTItgiSRYIK-----HTAGK----PILsVAVEPDG-SPIITQAMAG-EEIKP--SPHKI-QGIG 232
Cdd:cd01563  168 GWEVpDYVVVPVGNGGNI---TAIWKgfkelKELGLidrlPRM-VGVQAEGaAPIVRAFKEGkDDIEPveNPETIaTAIR 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488615772 233 AGFiPKNLD--LSIVDR----VERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEM-QGKTIVVILPDSG 304
Cdd:cd01563  244 IGN-PASGPkaLRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIdKGERVVVVLTGHG 321
PRK08197 PRK08197
threonine synthase; Validated
 13-115 2.85e-05

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 45.38  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  13 GNTPLVQINRIAPR-GV-TILAKIEGRNPGYSVKCRiGANMiwdAESSGKLKPGMTIVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:PRK08197  78 GMTPLLPLPRLGKAlGIgRLWVKDEGLNPTGSFKAR-GLAV---GVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRA 153

                         90       100
                 ....*....|....*....|....*
gi 488615772  91 MLTMPASMSIERRKVLKALGAELVL 115
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYL 178
PRK08246 PRK08246
serine/threonine dehydratase;
9-266 7.05e-05

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 43.79  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   9 AHSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAEssgklKPGMTIVEPTSGNTGIGLAFVAAARGY 88
Cdd:PRK08246  18 APHIRRTPVLEADGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  89 KLMLTMPASMSIERRKVLKALGAELVLTEP--AKGMKGAIAKAEELLAgdpekYFMPAqFENPANPAiHEKTTGPEIWAD 166
Cdd:PRK08246  93 PATVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAETGA-----LLCHA-YDQPEVLA-GAGTLGLEIEEQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 167 TDGAIDVLVAGVGTGGTITGISRYIKHtagkpILSVAVEPDGSPIITQAMAGEEikPSPHKIQGIGA--------GFIPK 238
Cdd:PRK08246 166 APGVDTVLVAVGGGGLIAGIAAWFEGR-----ARVVAVEPEGAPTLHAALAAGE--PVDVPVSGIAAdslgarrvGEIAF 238

                        250       260
                 ....*....|....*....|....*...
gi 488615772 239 NLDLSIVDRVERVTDEESKAMARRLMQE 266
Cdd:PRK08246 239 ALARAHVVTSVLVSDEAIIAARRALWEE 266
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 13-300 7.43e-05

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: 43.91  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   13 GNTPLVQINRIAPR--GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKlkpgMTIVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:TIGR00260  21 GVTPLFRAPALAANvgIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   91 MLTMPASmSIERRKVLKAL--GAELVltepakGMKGAIAKAEEL---LAGDPEKYFMpaqfeNPANPAIH----EKTTGP 161
Cdd:TIGR00260  97 VVLYPAG-KISLGKLAQALgyNAEVV------AIDGNFDDAQRLvkqLFEDKPALGL-----NSANSIPYrlegQKTYAF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  162 EIWADTDG-AIDVLVAGVGTGGTITGISR--YIKHTAGKPILSV--AVEPDG-SPIITQAMAGEEIKP--SPHKIQGIGA 233
Cdd:TIGR00260 165 EAVEQLGWeAPDKVVVPVPNSGNFGAIWKgfKEKKMLGLDSLPVkrGIQAEGaADIVRAFLEGGQWEPieTPETLSTAMD 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488615772  234 GFIPKNLD--LSIVDR----VERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAEKPEMQ-GKTIVVIL 300
Cdd:TIGR00260 245 IGNPANWPraLEAFRRsngyAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADpAERVVCAL 318
PRK12483 PRK12483
threonine dehydratase; Reviewed
 15-220 2.81e-04

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 42.48  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIG----ANMIWDAESSGklkpgmtIVEPTSGNTGIGLAFVAAARGYK 89
Cdd:PRK12483  38 TPLQRAPNLSARlGNQVLLKREDLQPVFSFKIRGAynkmARLPAEQLARG-------VITASAGNHAQGVALAAARLGVK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  90 LMLTMPASMSIERRKVLKALGAELVLTepAKGMKGAIAKAEELLAGDPEKYFMPaqFENPANPAiHEKTTGPEIWADTDG 169
Cdd:PRK12483 111 AVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEEGLTFVPP--FDDPDVIA-GQGTVAMEILRQHPG 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488615772 170 AIDVLVAGVGTGGTITGISRYIKHTagKP-ILSVAVEPDGSPIITQAMAGEE 220
Cdd:PRK12483 186 PLDAIFVPVGGGGLIAGIAAYVKYV--RPeIKVIGVEPDDSNCLQAALAAGE 235
PRK06608 PRK06608
serine/threonine dehydratase;
15-143 4.16e-04

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 41.68  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  15 TPLVQ---INRIAprGVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPgmTIVEPTSGNTGIGLAFVAAARGYKLM 91
Cdd:PRK06608  24 TPIVHsesLNEML--GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAYASKLFGIKTR 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488615772  92 LTMPASMSIERRKVLKALGAELVLTEPAkgmkgAIAKAEELLAGDPEKYFMP 143
Cdd:PRK06608 100 IYLPLNTSKVKQQAALYYGGEVILTNTR-----QEAEEKAKEDEEQGFYYIH 146
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 64-117 8.46e-04

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 40.63  E-value: 8.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488615772  64 GMTIVEPTSGNTGIGLAFVAAARGYKLMLTMPASMSIERRKVLKALGAELVLTE 117
Cdd:PRK08206 116 DITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITD 169
PRK06381 PRK06381
threonine synthase; Validated
 1-117 1.14e-03

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 40.07  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772   1 MSRIYADNAHSIGNTPLVQIN--RIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAessgkLKPGM-TIVEPTSGNTGI 77
Cdd:PRK06381   2 EEELSSSEEKPPGGTPLLRARklEEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRA-----MRLGYsGITVGTCGNYGA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488615772  78 GLAFVAAARGYKLMLTMPASMSIERRKVLKALGAELVLTE 117
Cdd:PRK06381  77 SIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVD 116
PRK06110 PRK06110
threonine dehydratase;
27-114 1.65e-03

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 39.59  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  27 GVTILAKIEGRNPGYSVKCRIGANMIWDAESSGKLKPGmtIVEPTSGNTGIGLAFVAAARGYKLMLTMPASMSIERRKVL 106
Cdd:PRK06110  35 GCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAM 112


                 ....*...
gi 488615772 107 KALGAELV 114
Cdd:PRK06110 113 RALGAELI 120
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 56-117 1.74e-03

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 39.51  E-value: 1.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488615772  56 ESSGKLKPGMTIVEpTSGNTGIGLAFV--AAARGYKLMLTMPASMSIER-RKVLKALGAELVLTE 117
Cdd:cd08290  139 EDFVKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLTE 202
PRK06815 PRK06815
threonine/serine dehydratase;
67-300 8.26e-03

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 37.36  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772  67 IVEPTSGNTGIGLAFVAAARGYKLMLTMPASMSIERRKVLKALGAELVL--TEPAKGMKGAIAKAEEllAGDPekYFMPA 144
Cdd:PRK06815  71 VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLygGDALNAELAARRAAEQ--QGKV--YISPY 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 145 qfeNPANPAIHEKTTGPEIWADTDGAIDVLVAGVGTGGTITGISrYIKhTAGKPILSVAVEPDGSPIITQAM-AGE---- 219
Cdd:PRK06815 147 ---NDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGGGLISGIAT-YLK-TLSPKTEIIGCWPANSPSLYTSLeAGEivev 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488615772 220 EIKP--SPHKIQGIGAGFIPKNLDLSIVDRVERVTDEESKAMARRLMQEEGILCGISCGAAMAAAVRLAekPEMQGKTIV 297
Cdd:PRK06815 222 AEQPtlSDGTAGGVEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLA--PRYQGKKVA 299


                 ...
gi 488615772 298 VIL 300
Cdd:PRK06815 300 VVL 302
 
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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