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Conserved domains on  [gi|15597905|ref|NP_251399|]
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cysteine synthase A [Pseudomonas aeruginosa PAO1]

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 2.55e-161

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


The actual alignment was detected with superfamily member TIGR01139:

Pssm-ID: 444852  Cd Length: 298  Bit Score: 451.82  E-value: 2.55e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905     8 NAQSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    88 YKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYFMPQQFDNPANPAIHEKTTGPEIWNDT 167
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   168 EGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDLSLVDR 247
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597905   248 VEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSSMLF 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 2.55e-161

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


Pssm-ID: 273465  Cd Length: 298  Bit Score: 451.82  E-value: 2.55e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905     8 NAQSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    88 YKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYFMPQQFDNPANPAIHEKTTGPEIWNDT 167
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   168 EGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDLSLVDR 247
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597905   248 VEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 3-310 8.48e-157

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: 440.25  E-value: 8.48e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   3 RIFADNAQSIGNTPLVQINRIAP-RGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAF 81
Cdd:COG0031   2 RIYDSILELIGNTPLVRLNRLSPgPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  82 VAAARGYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGkYFMPQQFDNPANPAIHEKTTGP 161
Cdd:COG0031  82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPG-AFWPNQFENPANPEAHYETTGP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 162 EIWNDTEGAVDVLVSgvgtggtltgvSRYIKNtRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLD 241
Cdd:COG0031 161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLKE-RNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597905 242 LSLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSS 310
Cdd:COG0031 234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLG-PGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 13-309 7.73e-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: 391.88  E-value: 7.73e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  13 GNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARGYKLI 91
Cdd:cd01561   1 GNTPLVRLNRLSPGtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  92 LTMPASMSLERRKVLKALGAELVLTEPAK--GMKGAIQKAEELVAGDPGkYFMPQQFDNPANPAIHEKTTGPEIWNDTEG 169
Cdd:cd01561  81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 170 AVDVLVSGVGTGGTLTGVSRYIKNtRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDLSLVDRVE 249
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKE-KNPNVRIVGVDPVGSVLFSGG------PPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 250 KIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLS 309
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-324 1.53e-136

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 390.38  E-value: 1.53e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    2 SRIFADNAQSIGNTPLVQINRI-APRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLA 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAsEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   81 FVAAARGYKLILTMPASMSLERRKVLKALGAELVLTE------PAKGMKGAIQKAEELVAGDPGKYFMPQQFDNPANPAI 154
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaapyanPNNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  155 HEKTTGPEIWNDTEGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTLAGEEVKPAPHKIQGIGAG 234
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK-VKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  235 FVPKNLDLSLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSSMLFD 314
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELG-PGHTIVTILCDSGERYQSKLFNP 318

                        330
                 ....*....|
gi 15597905  315 GLFSEQELTQ 324
Cdd:PRK10717 319 DFLREKGLPV 328
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-302 1.83e-60

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: 195.22  E-value: 1.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    12 IGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEasgRLKSGMTLVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:pfam00291   5 IGPTPLVRLPRLSKElGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARLGLKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    91 ILTMPASMSLERRKVLKALGAELVLTEPakGMKGAIQKAEELVAGDPGKYFMPqQFDNPANPAIHeKTTGPEIWNDTEGA 170
Cdd:pfam00291  82 TIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYIN-QYDNPLNIEGY-GTIGLEILEQLGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   171 VDVLVSGVGTGGTLTGVSRYIKNTRGKPILaVAVEPVTSPVISQTLAG---EEVKPAPHKIQGIGAGFVPKNLDLSL--- 244
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRV-IGVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALDLlde 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   245 -VDRVEKIGDDEAKNMALRLMQEEGILCGISSGAA-MAAAVRLAEEPNmQGKTIVVILPD 302
Cdd:pfam00291 237 yVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAlAALKLALAGELK-GGDRVVVVLTG 295
 
Name Accession Description Interval E-value
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 8-313 2.55e-161

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


Pssm-ID: 273465  Cd Length: 298  Bit Score: 451.82  E-value: 2.55e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905     8 NAQSIGNTPLVQINRIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    88 YKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYFMPQQFDNPANPAIHEKTTGPEIWNDT 167
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   168 EGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDLSLVDR 247
Cdd:TIGR01139 161 DGKLDAFVAGVGTGGTITGVGEVLKEQKPN-IKIVAVEPAESPVLSGG------KPGPHKIQGIGAGFIPKNLNRSVIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597905   248 VEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 3-310 8.48e-157

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: 440.25  E-value: 8.48e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   3 RIFADNAQSIGNTPLVQINRIAP-RGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAF 81
Cdd:COG0031   2 RIYDSILELIGNTPLVRLNRLSPgPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  82 VAAARGYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGkYFMPQQFDNPANPAIHEKTTGP 161
Cdd:COG0031  82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPG-AFWPNQFENPANPEAHYETTGP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 162 EIWNDTEGAVDVLVSgvgtggtltgvSRYIKNtRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLD 241
Cdd:COG0031 161 EIWEQTDGKVDAFVAgvgtggtitgvGRYLKE-RNPDIKIVAVEPEGSPLLSGG------EPGPHKIEGIGAGFVPKILD 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597905 242 LSLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSS 310
Cdd:COG0031 234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLG-PGKTIVTILPDSGERYLST 301
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 8-313 4.48e-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: 425.93  E-value: 4.48e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905     8 NAQSIGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAAR 86
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    87 GYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDpGKYFMPQQFDNPANPAIHEKTTGPEIWND 166
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAET-NKYVMLDQFENPANPEAHYKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   167 TEGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTLAGeevkpaPHKIQGIGAGFVPKNLDLSLVD 246
Cdd:TIGR01136 160 TDGRIDHFVAGVGTGGTITGVGRYLKEQNPN-IQIVAVEPAESPVLSGGEPG------PHKIQGIGAGFIPKILDLSLID 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597905   247 RVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNMQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01136 233 EVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 13-309 7.73e-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: 391.88  E-value: 7.73e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  13 GNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARGYKLI 91
Cdd:cd01561   1 GNTPLVRLNRLSPGtGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  92 LTMPASMSLERRKVLKALGAELVLTEPAK--GMKGAIQKAEELVAGDPGkYFMPQQFDNPANPAIHEKTTGPEIWNDTEG 169
Cdd:cd01561  81 IVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPN-AFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 170 AVDVLVSGVGTGGTLTGVSRYIKNtRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDLSLVDRVE 249
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKE-KNPNVRIVGVDPVGSVLFSGG------PPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 250 KIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLS 309
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PRK10717 PRK10717
cysteine synthase A; Provisional
 2-324 1.53e-136

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 390.38  E-value: 1.53e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    2 SRIFADNAQSIGNTPLVQINRI-APRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLA 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAsEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   81 FVAAARGYKLILTMPASMSLERRKVLKALGAELVLTE------PAKGMKGAIQKAEELVAGDPGKYFMPQQFDNPANPAI 154
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaapyanPNNYVKGAGRLAEELVASEPNGAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  155 HEKTTGPEIWNDTEGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTLAGEEVKPAPHKIQGIGAG 234
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK-VKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  235 FVPKNLDLSLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSSMLFD 314
Cdd:PRK10717 240 RITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELG-PGHTIVTILCDSGERYQSKLFNP 318

                        330
                 ....*....|
gi 15597905  315 GLFSEQELTQ 324
Cdd:PRK10717 319 DFLREKGLPV 328
PLN02565 PLN02565
cysteine synthase
 2-321 1.44e-115

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 336.90  E-value: 1.44e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    2 SRIFADNAQSIGNTPLVQINRIAPRGVT-ILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMT-LVEPTSGNTGIGL 79
Cdd:PLN02565   3 SSIAKDVTELIGKTPLVYLNNVVDGCVArIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   80 AFVAAARGYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYFMpQQFDNPANPAIHEKTT 159
Cdd:PLN02565  83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYIL-QQFENPANPKIHYETT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  160 GPEIWNDTEGAVDVLVSGVGTGGTLTGVSRYIKNtRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKN 239
Cdd:PLN02565 162 GPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKE-QNPDIKLYGVEPVESAVLSGG------KPGPHKIQGIGAGFIPGV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  240 LDLSLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNMQGKTIVVILPDSGERYLSSMLFDGLFSE 319
Cdd:PLN02565 235 LDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKE 314


                 ..
gi 15597905  320 QE 321
Cdd:PLN02565 315 AE 316
PLN00011 PLN00011
cysteine synthase
 7-321 7.17e-103

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 304.62  E-value: 7.17e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    7 DNAQSIGNTPLVQINRIAPRGVT-ILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGM-TLVEPTSGNTGIGLAFVAA 84
Cdd:PLN00011  10 DVTELIGNTPMVYLNNIVDGCVArIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEATAGNTGIGLACIGA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   85 ARGYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYfMPQQFDNPANPAIHEKTTGPEIW 164
Cdd:PLN00011  90 ARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGY-IPQQFENPANPEIHYRTTGPEIW 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  165 NDTEGAVDVLVSGVGTGGTLTGVSRYIKNtRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDLSL 244
Cdd:PLN00011 169 RDSAGKVDILVAGVGTGGTATGVGKFLKE-KNKDIKVCVVEPVESAVLSGG------QPGPHLIQGIGSGIIPFNLDLTI 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597905  245 VDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNMQGKTIVVILPDSGERYLSSMLFDGLFSEQE 321
Cdd:PLN00011 242 VDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAE 318
PLN03013 PLN03013
cysteine synthase
 6-324 1.34e-99

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 300.15  E-value: 1.34e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    6 ADN-AQSIGNTPLVQINRIAPRGVT-ILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMT-LVEPTSGNTGIGLAFV 82
Cdd:PLN03013 114 ADNvSQLIGKTPMVYLNSIAKGCVAnIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSvLVEPTSGNTGIGLAFI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   83 AAARGYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYfMPQQFDNPANPAIHEKTTGPE 162
Cdd:PLN03013 194 AASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAY-MLQQFDNPANPKIHYETTGPE 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  163 IWNDTEGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKNLDL 242
Cdd:PLN03013 273 IWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPK-TQVIGVEPTESDILSGG------KPGPHKIQGIGAGFIPKNLDQ 345

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  243 SLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNMQGKTIVVILPDSGeRYLSSMLFDGLFSEQEL 322
Cdd:PLN03013 346 KIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWR 424


                 ..
gi 15597905  323 TQ 324
Cdd:PLN03013 425 KC 426
cysM PRK11761
cysteine synthase CysM;
9-315 3.80e-97

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 289.08  E-value: 3.80e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    9 AQSIGNTPLVQINRIAP-RGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARG 87
Cdd:PRK11761   7 EDTIGNTPLVKLQRLPPdRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   88 YKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAgdPGKYFMPQQFDNPANPAIHEKTTGPEIWNDT 167
Cdd:PRK11761  87 YRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQA--EGEGKVLDQFANPDNPLAHYETTGPEIWRQT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  168 EGAVDVLVSGVGTGGTLTGVSRYIKnTRGKPILAVAVEPvtspvisqtlagEEvkpaPHKIQGI---GAGFVPKNLDLSL 244
Cdd:PRK11761 165 EGRITHFVSSMGTTGTIMGVSRYLK-EQNPAVQIVGLQP------------EE----GSSIPGIrrwPEEYLPKIFDASR 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597905  245 VDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEpnMQGKTIVVILPDSGERYLSSMLFDG 315
Cdd:PRK11761 228 VDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARE--NPNAVIVAIICDRGDRYLSTGVFPA 296
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 2-324 7.37e-91

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 275.69  E-value: 7.37e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    2 SRIFADNAQSIGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSG-MTLVEPTSGNTGIGL 79
Cdd:PLN02556  47 TKIKTDASQLIGKTPLVYLNKVTEGcGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMGISL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   80 AFVAAARGYKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKyFMPQQFDNPANPAIHEKTT 159
Cdd:PLN02556 127 AFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDA-FMLQQFSNPANTQVHFETT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  160 GPEIWNDTEGAVDVLVSGVGTGGTLTGVSRYIKnTRGKPILAVAVEPVTSPVISQTlageevKPAPHKIQGIGAGFVPKN 239
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLK-SKNPNVKIYGVEPAESNVLNGG------KPGPHHITGNGVGFKPDI 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  240 LDLSLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNMQGKTIVVILPDSGERYLSSMLFDGLFSE 319
Cdd:PLN02556 279 LDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKE 358


                 ....*
gi 15597905  320 QELTQ 324
Cdd:PLN02556 359 AENMQ 363
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 12-314 1.14e-84

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: 262.43  E-value: 1.14e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    12 IGNTPLVQINRIAPRG-VTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:TIGR01137   9 IGNTPLVRLNKVSKGLkCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    91 ILTMPASMSLERRKVLKALGAELVLTEPAKGM---KGAIQKAEELVAGDPGKYfMPQQFDNPANPAIHEKTTGPEIWNDT 167
Cdd:TIGR01137  89 IIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdspESHIGVAKRLVREIPGAH-ILDQYRNPSNPLAHYDTTGPEILEQC 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   168 EGAVDVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSpVISQTLAGEEVKPAPHKIQGIGAGFVPKNLDLSLVDR 247
Cdd:TIGR01137 168 EGKLDMFVAGVGTGGTITGIARYLKESCPG-CRIVGADPEGS-ILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDE 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597905   248 VEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNMQGKTIVVILPDSGERYLSSMLFD 314
Cdd:TIGR01137 246 WIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLND 312
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 9-313 3.82e-80

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: 245.59  E-value: 3.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905     9 AQSIGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARG 87
Cdd:TIGR01138   3 EQTVGNTPLVRLQRMGPEnGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    88 YKLILTMPASMSLERRKVLKALGAELVLTEPAKGMKGAIQKAEELVAGDPGKYFmpQQFDNPANPAIHEKTTGPEIWNDT 167
Cdd:TIGR01138  83 YRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL--DQFNNPDNPYAHYTSTGPEIWQQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   168 EGAVDVLVSGVGTGGTLTGVSRYIKnTRGKPILAVAVEPVTSPVISqtlageevkpaphKIQGIGAGFVPKNLDLSLVDR 247
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLK-EQNPPVQIVGLQPEEGSSIP-------------GIRRWPTEYLPGIFDASLVDR 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597905   248 VEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEpnMQGKTIVVILPDSGERYLSSMLF 313
Cdd:TIGR01138 227 VLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARE--LPDAVVVAIICDRGDRYLSTGVF 290
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-302 1.83e-60

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: 195.22  E-value: 1.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    12 IGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEasgRLKSGMTLVEPTSGNTGIGLAFVAAARGYKL 90
Cdd:pfam00291   5 IGPTPLVRLPRLSKElGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARLGLKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    91 ILTMPASMSLERRKVLKALGAELVLTEPakGMKGAIQKAEELVAGDPGKYFMPqQFDNPANPAIHeKTTGPEIWNDTEGA 170
Cdd:pfam00291  82 TIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYIN-QYDNPLNIEGY-GTIGLEILEQLGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   171 VDVLVSGVGTGGTLTGVSRYIKNTRGKPILaVAVEPVTSPVISQTLAG---EEVKPAPHKIQGIGAGFVPKNLDLSL--- 244
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRV-IGVEPEGAPALARSLAAgrpVPVPVADTIADGLGVGDEPGALALDLlde 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   245 -VDRVEKIGDDEAKNMALRLMQEEGILCGISSGAA-MAAAVRLAEEPNmQGKTIVVILPD 302
Cdd:pfam00291 237 yVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAlAALKLALAGELK-GGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 15-303 4.05e-58

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: 187.34  E-value: 4.05e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKsGMTLVEPTSGNTGIGLAFVAAARGYKLILT 93
Cdd:cd00640   1 TPLVRLKRLSKLgGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLP-KGVIIESTGGNTGIALAAAAARLGLKCTIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  94 MPASMSLERRKVLKALGAELVLTEPakGMKGAIQKAEELVAGDPGkYFMPQQFDNPANPAIHeKTTGPEIWNDTEG-AVD 172
Cdd:cd00640  80 MPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPG-AYYVNQFDNPANIAGQ-GTIGLEILEQLGGqKPD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 173 VLVsgvgtggtltgvsryikntrgkpilavavepvtSPV-----ISqtlageevkpaphkiqGIGAGFVPKNLDLSLV-- 245
Cdd:cd00640 156 AVV---------------------------------VPVggggnIA----------------GIARALKELLPNVKVIgv 186

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597905 246 -DRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPNmQGKTIVVILPDS 303
Cdd:cd00640 187 ePEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTGG 244
PLN02356 PLN02356
phosphateglycerate kinase
 10-323 1.25e-35

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 133.58  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   10 QSIGNTPLVQINRIA-PRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGMTLVEPTSGNTGIGLAFVAAARGY 88
Cdd:PLN02356  49 DAIGNTPLIRINSLSeATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGC 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   89 KLILTMPASMSLERRKVLKALGAEL----------------------------------------VLTEPAKGMKGAIQK 128
Cdd:PLN02356 129 KCHVVIPDDVAIEKSQILEALGATVervrpvsithkdhyvniarrraleanelaskrrkgsetdgIHLEKTNGCISEEEK 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  129 AEELVAGDPGKYFMPQQFDNPANPAIHEKTTGPEIWNDTEGAVDVLVSGVGTGGTLTGVSRYI--KNTRGKPILavaVEP 206
Cdd:PLN02356 209 ENSLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLqeKNPNIKCFL---IDP 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  207 VTSPVISQTLAG-----EEVK------PAPHKIQGIGAGFVPKNLDLSLVDRVEKIGDDEAKNMALRLMQEEGILCGISS 275
Cdd:PLN02356 286 PGSGLFNKVTRGvmytrEEAEgrrlknPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSS 365

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15597905  276 GAAMAAAVRLAEEPNmQGKTIVVILPDSGERYLSSMLFDGLFSEQELT 323
Cdd:PLN02356 366 AMNCVGAVRVAQSLG-PGHTIVTILCDSGMRHLSKFHDPQYLSQHGLT 412
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 13-175 1.84e-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: 52.12  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  13 GNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCR---IGANMiwdAEASGRLksgmTLVEPTSGNTGIGLAFVAAARGY 88
Cdd:COG0498  65 GGTPLVKAPRLADElGKNLYVKEEGHNPTGSFKDRamqVAVSL---ALERGAK----TIVCASSGNGSAALAAYAARAGI 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  89 KLILTMPAS-MSLERRKVLKALGAELVLTEpakgmkGAIQKAEELV---AGDPGKYFMpqqfdNPANPAIHE--KTTGPE 162
Cdd:COG0498 138 EVFVFVPEGkVSPGQLAQMLTYGAHVIAVD------GNFDDAQRLVkelAADEGLYAV-----NSINPARLEgqKTYAFE 206

                       170
                ....*....|...
gi 15597905 163 IWNDTEGAVDVLV 175
Cdd:COG0498 207 IAEQLGRVPDWVV 219
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 13-114 1.15e-05

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: 46.43  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  13 GNTPLVQINRIAPR--GVTILAKIEGRNPGYSVKCRiGANM-IWDAEASGRlksgMTLVEPTSGNTGIGLAFVAAARGYK 89
Cdd:cd01563  21 GNTPLVRAPRLGERlgGKNLYVKDEGLNPTGSFKDR-GMTVaVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95

                        90       100
                ....*....|....*....|....*
gi 15597905  90 LILTMPASMSLERRKVLKALGAELV 114
Cdd:cd01563  96 CVVFLPAGKALGKLAQALAYGATVL 120
PRK08197 PRK08197
threonine synthase; Validated
 13-134 1.43e-05

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 46.15  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   13 GNTPLVQINRIAPR-GV-TILAKIEGRNPGYSVKCRiGANMiwdaeASGRLKS-GMT-LVEPTSGNTGIGLAFVAAARGY 88
Cdd:PRK08197  78 GMTPLLPLPRLGKAlGIgRLWVKDEGLNPTGSFKAR-GLAV-----GVSRAKElGVKhLAMPTNGNAGAAWAAYAARAGI 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15597905   89 KLILTMPASMSLERRKVLKALGAELVLTEpakgmkGAIQKAEELVA 134
Cdd:PRK08197 152 RATIFMPADAPEITRLECALAGAELYLVD------GLISDAGKIVA 191
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-304 2.13e-05

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: 45.56  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   9 AQSIGNTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRiGA-NMIWDAEASGRLKsGMtlVEPTSGNTGIGLAFVAAAR 86
Cdd:cd01562  12 KPVVRRTPLLTSPTLSELlGAEVYLKCENLQKTGSFKIR-GAyNKLLSLSEEERAK-GV--VAASAGNHAQGVAYAAKLL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  87 GYKLILTMPASMSLERRKVLKALGAELVLTEPakGMKGAIQKAEELVAGDpGKYFMPqQFDNPANPAIHeKTTGPEIWND 166
Cdd:cd01562  88 GIPATIVMPETAPAAKVDATRAYGAEVVLYGE--DFDEAEAKARELAEEE-GLTFIH-PFDDPDVIAGQ-GTIGLEILEQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 167 TEGAVDVLV--------SgvgtggtltGVSRYIKNTRGKpILAVAVEPVTSPVISQTL-AGEEVK-PAPHKIQGIGAGFV 236
Cdd:cd01562 163 VPDLDAVFVpvggggliA---------GIATAVKALSPN-TKVIGVEPEGAPAMAQSLaAGKPVTlPEVDTIADGLAVKR 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597905 237 PKNLDLSL----VDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEPnmQGKTIVVILpdSG 304
Cdd:cd01562 233 PGELTFEIirklVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVL--SG 300
PRK12483 PRK12483
threonine dehydratase; Reviewed
 15-221 3.11e-05

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 45.56  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMI--WDAEASGRlksgmTLVEPTSGNTGIGLAFVAAARGYKLI 91
Cdd:PRK12483  38 TPLQRAPNLSARlGNQVLLKREDLQPVFSFKIRGAYNKMarLPAEQLAR-----GVITASAGNHAQGVALAAARLGVKAV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   92 LTMPASMSLERRKVLKALGAELVLTepAKGMKGAIQKAEELVAGDpGKYFMPqQFDNPANPAiHEKTTGPEIWNDTEGAV 171
Cdd:PRK12483 113 IVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAHALKLAEEE-GLTFVP-PFDDPDVIA-GQGTVAMEILRQHPGPL 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597905  172 DVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTL-AGEEV 221
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPE-IKVIGVEPDDSNCLQAALaAGERV 237
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 58-117 3.39e-04

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 42.17  E-value: 3.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597905   58 SGRLKS---GMTLVEPTSGNTGIGLAFVAAARGYKLILTMPASMSLERRKVLKALGAELVLTE 117
Cdd:PRK08206 107 SGEVREklgDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITD 169
PRK06608 PRK06608
serine/threonine dehydratase;
10-143 3.94e-04

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 41.68  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   10 QSIGNTPLVQ---INRIAprGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSgmTLVEPTSGNTGIGLAFVAAAR 86
Cdd:PRK06608  19 QYLHLTPIVHsesLNEML--GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAYASKLF 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597905   87 GYKLILTMPASMSLERRKVLKALGAELVLTEPAkgmkgaiQKAEELV--AGDPGKYFMP 143
Cdd:PRK06608  95 GIKTRIYLPLNTSKVKQQAALYYGGEVILTNTR-------QEAEEKAkeDEEQGFYYIH 146
PRK06110 PRK06110
threonine dehydratase;
27-143 1.12e-03

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 40.36  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   27 GVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRLKSGmtLVEPTSGNTGIGLAFVAAARGYKLILTMPASMSLERRKVL 106
Cdd:PRK06110  35 GCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAM 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15597905  107 KALGAELVltEPAKGMKGAIQKAEELVAGDpGKYFMP 143
Cdd:PRK06110 113 RALGAELI--EHGEDFQAAREEAARLAAER-GLHMVP 146
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 15-304 1.82e-03

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: 39.63  E-value: 1.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIW--DAEASGRlksgmTLVEPTSGNTGIGLAFVAAARGYKLI 91
Cdd:COG1171  25 TPLLRSPTLSERlGAEVYLKLENLQPTGSFKLRGAYNALAslSEEERAR-----GVVAASAGNHAQGVAYAARLLGIPAT 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  92 LTMPASMSLERRKVLKALGAELVLTEPAkgMKGAIQKAEELVAgDPGKYFMPQqFDNP------AnpaihekTTGPEIWN 165
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAAAAELAE-EEGATFVHP-FDDPdviagqG-------TIALEILE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905 166 DTeGAVDVL------------VSGvgtggtltgvsrYIKNTRGKPILaVAVEPVTSPVISQTL-AGEEVK-PAPHKI-QG 230
Cdd:COG1171 169 QL-PDLDAVfvpvggggliagVAA------------ALKALSPDIRV-IGVEPEGAAAMYRSLaAGEPVTlPGVDTIaDG 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597905 231 IGAGFV-PKNLDL--SLVDRVEKIGDDEAKNMALRLMQEEGILCGISSGAAMAAAVRLAEEpnMQGKTIVVILpdSG 304
Cdd:COG1171 235 LAVGRPgELTFEIlrDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER--LKGKRVVVVL--SG 307
PRK06381 PRK06381
threonine synthase; Validated
 1-117 3.17e-03

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 38.92  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905    1 MSRIFADNAQSIGNTPLVQIN--RIAPRGVTILAKIEGRNPGYSVKCRIGANMIWDAEASGRlkSGMTLvePTSGNTGIG 78
Cdd:PRK06381   2 EEELSSSEEKPPGGTPLLRARklEEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY--SGITV--GTCGNYGAS 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15597905   79 LAFVAAARGYKLILTMPASMSLERRKVLKALGAELVLTE 117
Cdd:PRK06381  78 IAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVD 116
PRK08246 PRK08246
serine/threonine dehydratase;
73-131 6.09e-03

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 38.01  E-value: 6.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597905   73 GNTGIGLAFVAAARGYKLILTMPASMSLERRKVLKALGAELVLTEP--AKGMKGAIQKAEE 131
Cdd:PRK08246  77 GNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAeyADALEAAQAFAAE 137
PLN02550 PLN02550
threonine dehydratase
 15-221 7.15e-03

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 37.98  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   15 TPLVQINRIAPR-GVTILAKIEGRNPGYSVKCRIGANMIWDAEASgRLKSGmtLVEPTSGNTGIGLAFVAAARGYKLILT 93
Cdd:PLN02550 110 SPLQLAKKLSERlGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIA 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905   94 MPASMSLERRKVLKALGAELVLTEPA--KGMKGAIQKAEElvagdPGKYFMPqQFDNPaNPAIHEKTTGPEIWNDTEGAV 171
Cdd:PLN02550 187 MPVTTPEIKWQSVERLGATVVLVGDSydEAQAYAKQRALE-----EGRTFIP-PFDHP-DVIAGQGTVGMEIVRQHQGPL 259

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597905  172 DVLVSGVGTGGTLTGVSRYIKNTRGKpILAVAVEPVTSPVISQTLA-GEEV 221
Cdd:PLN02550 260 HAIFVPVGGGGLIAGIAAYVKRVRPE-VKIIGVEPSDANAMALSLHhGERV 309
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 14-149 8.14e-03

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: 37.66  E-value: 8.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  14 NTPLVQINRIAPR-GVTILAKIEGRNPGYSVKCR-IGaNMIWDAEASGRLKSgMTLVEPTSGNTGIGLAFvaAARGYKLI 91
Cdd:cd06448   1 KTPLIESTALSKTaGCNVFLKLENLQPSGSFKIRgIG-HLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAY--AARKLGVP 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597905  92 LT--MPASMSLERRKVLKALGAELVLTEPAKGmKGAIQKAEELVAGDPGKYFMPqQFDNP 149
Cdd:cd06448  77 CTivVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAENDPGPVYVH-PFDDP 134
 
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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