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Conserved domains on  [gi|2270541331|gb|KAI5253729|]
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tryptophan synthase beta subunit-like PLP-dependent enzyme [Aureobasidium subglaciale]

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) ...
 44-375 3.56e-85

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 PRK08206:

Pssm-ID: 444852  Cd Length: 399  Bit Score: 264.05  E-value: 3.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  44 IALHHAFPESMTTPLIELPELAAELGIGYVFVKDESLRFGLPSFKILGASWGVFKAVCEKTGLP-SSVSLGE--AGRAAQ 120
Cdd:PRK08206   33 RAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALGGAYAVARLLAEKLGLDiSELSFEEltSGEVRE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 121 KAG-ISLVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVM 199
Cdd:PRK08206  113 KLGdITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQ 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 200 DTSWEGYSQVPKWVVDGYATMHVEVDRQLQEaCGKRPSLCIASVGVGSWAQSVVTHYA---GDNSATNVVtVESEAAPCL 276
Cdd:PRK08206  193 DTAWEGYEEIPTWIMQGYGTMADEAVEQLKE-MGVPPTHVFLQAGVGSLAGAVLGYFAevyGEQRPHFVV-VEPDQADCL 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 277 LESLHVGEIVSVETST-TIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-----NDHGVNAGPCGAAPLAA 350
Cdd:PRK08206  271 YQSAVDGKPVAVTGDMdTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGMRILanplgGDPPIVSGESGAVGLGA 350

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2270541331 351 LRKLHKQGLFP-------LDSDAVVVLFSTEG 375
Cdd:PRK08206  351 LAALMTDPDYQelreklgLDEDSRVLLISTEG 382
 
Name Accession Description Interval E-value
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 44-375 3.56e-85

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 264.05  E-value: 3.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  44 IALHHAFPESMTTPLIELPELAAELGIGYVFVKDESLRFGLPSFKILGASWGVFKAVCEKTGLP-SSVSLGE--AGRAAQ 120
Cdd:PRK08206   33 RAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALGGAYAVARLLAEKLGLDiSELSFEEltSGEVRE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 121 KAG-ISLVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVM 199
Cdd:PRK08206  113 KLGdITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQ 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 200 DTSWEGYSQVPKWVVDGYATMHVEVDRQLQEaCGKRPSLCIASVGVGSWAQSVVTHYA---GDNSATNVVtVESEAAPCL 276
Cdd:PRK08206  193 DTAWEGYEEIPTWIMQGYGTMADEAVEQLKE-MGVPPTHVFLQAGVGSLAGAVLGYFAevyGEQRPHFVV-VEPDQADCL 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 277 LESLHVGEIVSVETST-TIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-----NDHGVNAGPCGAAPLAA 350
Cdd:PRK08206  271 YQSAVDGKPVAVTGDMdTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGMRILanplgGDPPIVSGESGAVGLGA 350

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2270541331 351 LRKLHKQGLFP-------LDSDAVVVLFSTEG 375
Cdd:PRK08206  351 LAALMTDPDYQelreklgLDEDSRVLLISTEG 382
diampropi_NH3ly TIGR01747
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ...
 44-378 7.15e-63

diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]


Pssm-ID: 130808  Cd Length: 376  Bit Score: 205.90  E-value: 7.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  44 IALHHAFPESMTTPLIELPELAAELGIGYVFVKDESLRFGLPSFKILGASWGVFKAVCEKTGLP-SSVSLGEAGRAAQKA 122
Cdd:TIGR01747  11 LAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDiETLSFEHLKNDAIGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 123 GI---SLVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVM 199
Cdd:TIGR01747  91 KMgqaTFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQMAQQHGWVVVQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 200 DTSWEGYSQVPKWVVDGYATMHVEVDRQLQEACGKRPSLCIASVGVGSWAQSVVTHYAGDNSAT--NVVTVESEAAPCLL 277
Cdd:TIGR01747 171 DTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHVLLQAGVGSMAGGVLGYFVDVYSENnpHSIVVEPDKADCLY 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 278 ES--LHVGEIVSVETS-TTIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-----NDHGVNAGPCGAAPLA 349
Cdd:TIGR01747 251 QSavKKDGDIVNVGGDmATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLgapygGDPRIISGESGAVGLG 330

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2270541331 350 ALRKL----HKQGL---FPLDSDAVVVLFSTEGHRD 378
Cdd:TIGR01747 331 LLAAVmyhpQYQSLmekLQLDKDAVVLVISTEGDTD 366
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 56-375 3.02e-53

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: 179.46  E-value: 3.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRFgLPSFKILGASWGVFkavcektglpssvSLGEAGRAAqkaGIslVTCTDGNWG 135
Cdd:COG1171    25 TPLLRSPTLSERLGAE-VYLKLENLQP-TGSFKLRGAYNALA-------------SLSEEERAR---GV--VAASAGNHA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVMDTSwegysqvPKWVVD 215
Cdd:COG1171    85 QGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFD-------DPDVIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 216 GYATMHVEVDRQLQEacgkrPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTIM 295
Cdd:COG1171   158 GQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 296 DGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAALRKlHKQGLfpldSDAVVVLFSTE 374
Cdd:COG1171   233 DGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLlERTKIVVEPAGAAALAALLA-GKERL----KGKRVVVVLSG 307


                  .
gi 2270541331 375 G 375
Cdd:COG1171   308 G 308
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 56-372 4.88e-47

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: 162.09  E-value: 4.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRFGLpSFKILGASWGVFKAvcektglpssvslgeagrAAQKAGISLVTCTDGNWG 135
Cdd:pfam00291   8 TPLVRLPRLSKELGVD-VYLKLESLNPTG-SFKDRGALNLLLRL------------------KEGEGGKTVVEASSGNHG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAIN-ETQGSDATLVMDTSwegysqvPKWVV 214
Cdd:pfam00291  68 RALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARElAAEGPGAYYINQYD-------NPLNI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 215 DGYATMHVEVDRQLqeacGKRPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTI 294
Cdd:pfam00291 141 EGYGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 295 MDGMNCG-TVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAALrKLHKQGLFPlDSDAVVVLFS 372
Cdd:pfam00291 217 ADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLaRREGIVVEPSSAAALAAL-KLALAGELK-GGDRVVVVLT 294
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 56-372 1.92e-32

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: 123.75  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGiGYVFVKDESL-RFGlpSFKILGASWGVFkavcektglpssvSLGEAGRAAqkaGIslVTCTDGNW 134
Cdd:cd01562    18 TPLLTSPTLSELLG-AEVYLKCENLqKTG--SFKIRGAYNKLL-------------SLSEEERAK---GV--VAASAGNH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 135 GRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVmdtswEGYSQVpkWVV 214
Cdd:cd01562    77 AQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFI-----HPFDDP--DVI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 215 DGYATMHVEVDRQLQEacgkrPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTI 294
Cdd:cd01562   150 AGQGTIGLEILEQVPD-----LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTI 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2270541331 295 MDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAALrklhKQGLFPLDSDAVVVLFS 372
Cdd:cd01562   225 ADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLfEREKLVAEPAGALALAAL----LSGKLDLKGKKVVVVLS 299
 
Name Accession Description Interval E-value
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 44-375 3.56e-85

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 264.05  E-value: 3.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  44 IALHHAFPESMTTPLIELPELAAELGIGYVFVKDESLRFGLPSFKILGASWGVFKAVCEKTGLP-SSVSLGE--AGRAAQ 120
Cdd:PRK08206   33 RAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALGGAYAVARLLAEKLGLDiSELSFEEltSGEVRE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 121 KAG-ISLVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVM 199
Cdd:PRK08206  113 KLGdITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQ 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 200 DTSWEGYSQVPKWVVDGYATMHVEVDRQLQEaCGKRPSLCIASVGVGSWAQSVVTHYA---GDNSATNVVtVESEAAPCL 276
Cdd:PRK08206  193 DTAWEGYEEIPTWIMQGYGTMADEAVEQLKE-MGVPPTHVFLQAGVGSLAGAVLGYFAevyGEQRPHFVV-VEPDQADCL 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 277 LESLHVGEIVSVETST-TIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-----NDHGVNAGPCGAAPLAA 350
Cdd:PRK08206  271 YQSAVDGKPVAVTGDMdTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGMRILanplgGDPPIVSGESGAVGLGA 350

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2270541331 351 LRKLHKQGLFP-------LDSDAVVVLFSTEG 375
Cdd:PRK08206  351 LAALMTDPDYQelreklgLDEDSRVLLISTEG 382
diampropi_NH3ly TIGR01747
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ...
 44-378 7.15e-63

diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]


Pssm-ID: 130808  Cd Length: 376  Bit Score: 205.90  E-value: 7.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  44 IALHHAFPESMTTPLIELPELAAELGIGYVFVKDESLRFGLPSFKILGASWGVFKAVCEKTGLP-SSVSLGEAGRAAQKA 122
Cdd:TIGR01747  11 LAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDiETLSFEHLKNDAIGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 123 GI---SLVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVM 199
Cdd:TIGR01747  91 KMgqaTFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQMAQQHGWVVVQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 200 DTSWEGYSQVPKWVVDGYATMHVEVDRQLQEACGKRPSLCIASVGVGSWAQSVVTHYAGDNSAT--NVVTVESEAAPCLL 277
Cdd:TIGR01747 171 DTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHVLLQAGVGSMAGGVLGYFVDVYSENnpHSIVVEPDKADCLY 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 278 ES--LHVGEIVSVETS-TTIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-----NDHGVNAGPCGAAPLA 349
Cdd:TIGR01747 251 QSavKKDGDIVNVGGDmATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLgapygGDPRIISGESGAVGLG 330

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2270541331 350 ALRKL----HKQGL---FPLDSDAVVVLFSTEGHRD 378
Cdd:TIGR01747 331 LLAAVmyhpQYQSLmekLQLDKDAVVLVISTEGDTD 366
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 56-375 3.02e-53

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: 179.46  E-value: 3.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRFgLPSFKILGASWGVFkavcektglpssvSLGEAGRAAqkaGIslVTCTDGNWG 135
Cdd:COG1171    25 TPLLRSPTLSERLGAE-VYLKLENLQP-TGSFKLRGAYNALA-------------SLSEEERAR---GV--VAASAGNHA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVMDTSwegysqvPKWVVD 215
Cdd:COG1171    85 QGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFD-------DPDVIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 216 GYATMHVEVDRQLQEacgkrPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTIM 295
Cdd:COG1171   158 GQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 296 DGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAALRKlHKQGLfpldSDAVVVLFSTE 374
Cdd:COG1171   233 DGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLlERTKIVVEPAGAAALAALLA-GKERL----KGKRVVVVLSG 307


                  .
gi 2270541331 375 G 375
Cdd:COG1171   308 G 308
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 56-372 4.88e-47

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: 162.09  E-value: 4.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRFGLpSFKILGASWGVFKAvcektglpssvslgeagrAAQKAGISLVTCTDGNWG 135
Cdd:pfam00291   8 TPLVRLPRLSKELGVD-VYLKLESLNPTG-SFKDRGALNLLLRL------------------KEGEGGKTVVEASSGNHG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAIN-ETQGSDATLVMDTSwegysqvPKWVV 214
Cdd:pfam00291  68 RALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARElAAEGPGAYYINQYD-------NPLNI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 215 DGYATMHVEVDRQLqeacGKRPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTI 294
Cdd:pfam00291 141 EGYGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 295 MDGMNCG-TVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAALrKLHKQGLFPlDSDAVVVLFS 372
Cdd:pfam00291 217 ADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLaRREGIVVEPSSAAALAAL-KLALAGELK-GGDRVVVVLT 294
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 56-372 1.92e-32

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: 123.75  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGiGYVFVKDESL-RFGlpSFKILGASWGVFkavcektglpssvSLGEAGRAAqkaGIslVTCTDGNW 134
Cdd:cd01562    18 TPLLTSPTLSELLG-AEVYLKCENLqKTG--SFKIRGAYNKLL-------------SLSEEERAK---GV--VAASAGNH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 135 GRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVmdtswEGYSQVpkWVV 214
Cdd:cd01562    77 AQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFI-----HPFDDP--DVI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 215 DGYATMHVEVDRQLQEacgkrPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTI 294
Cdd:cd01562   150 AGQGTIGLEILEQVPD-----LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTI 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2270541331 295 MDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAALrklhKQGLFPLDSDAVVVLFS 372
Cdd:cd01562   225 ADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLfEREKLVAEPAGALALAAL----LSGKLDLKGKKVVVVLS 299
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 56-272 2.72e-26

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: 105.67  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRFGLpSFKILGASWGVFKAvcEKTGLpssvslgeagraaqKAGISLVTCTDGNWG 135
Cdd:cd00640     1 TPLVRLKRLSKLGGAN-IYLKLEFLNPTG-SFKDRGALNLILLA--EEEGK--------------LPKGVIIESTGGNTG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVMDtswegySQVPKWVVD 215
Cdd:cd00640    63 IALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVN------QFDNPANIA 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2270541331 216 GYATMHVEVDRQLQeacGKRPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEA 272
Cdd:cd00640   137 GQGTIGLEILEQLG---GQKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPEV 190
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 55-369 4.52e-23

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: 98.14  E-value: 4.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  55 TTPLIELPELAAELGIGyVFVKDESLRfglP--SFKILGASwgvfkAVCEKtglpssvslgEAGRAAQKAgISLVTCTDG 132
Cdd:cd06448     1 KTPLIESTALSKTAGCN-VFLKLENLQ---PsgSFKIRGIG-----HLCQK----------SAKQGLNEC-VHVVCSSGG 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 133 NWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVM------DTSWEGY 206
Cdd:cd06448    61 NAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPVYvhpfddPLIWEGH 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 207 SqvpkwvvdgyaTMHVEVDRQLQEacGKRPSLCIASVGVGSW----AQSVVTHYAGDnsaTNVVTVESEAAPCLLESLHV 282
Cdd:cd06448   141 S-----------SMVDEIAQQLQS--QEKVDAIVCSVGGGGLlngiVQGLERNGWGD---IPVVAVETEGAHSLNASLKA 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 283 GEIVSVETSTTIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVV-YLNDHGVNAGP-CGAApLAA------LRKL 354
Cdd:cd06448   205 GKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLrFADDERILVEPaCGAA-LAVvysgkiLDLQ 283

                         330
                  ....*....|....*
gi 2270541331 355 HKQGLFPLDSDAVVV 369
Cdd:cd06448   284 LEVLLTPLDNVVVVV 298
PRK08246 PRK08246
serine/threonine dehydratase;
55-351 1.02e-19

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 88.47  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  55 TTPLIELPelAAELGIGYVFVKDESLRFGlPSFKILGAswgvFKAVcektglpssvslgeagRAAQKAGISLVTCTDGNW 134
Cdd:PRK08246   23 RTPVLEAD--GAGFGPAPVWLKLEHLQHT-GSFKARGA----FNRL----------------LAAPVPAAGVVAASGGNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 135 GRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVmdtswEGYSQVPkwVV 214
Cdd:PRK08246   80 GLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLC-----HAYDQPE--VL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 215 DGYATMHVEVDRQLqeacGKRPSLCIAsVGVGSWAQSVVTHYAGdnsATNVVTVESEAAPCLLESLHVGEIVSVETSTTI 294
Cdd:PRK08246  153 AGAGTLGLEIEEQA----PGVDTVLVA-VGGGGLIAGIAAWFEG---RARVVAVEPEGAPTLHAALAAGEPVDVPVSGIA 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2270541331 295 MDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYL-NDHGVNAGPCGAAPLAAL 351
Cdd:PRK08246  225 ADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALwEELRLAVEPGAATALAAL 282
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 56-370 1.10e-18

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: 85.72  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGYVFVKDESLrfgLP--SFKILGASWGVFKAVcektglpssvslgeagraaqKAGISLVTC-TDG 132
Cdd:cd01563    23 TPLVRAPRLGERLGGKNLYVKDEGL---NPtgSFKDRGMTVAVSKAK--------------------ELGVKAVACaSTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 133 NWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVmdTSWEGYSqvpkw 212
Cdd:cd01563    80 NTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS--NSLNPYR----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 213 vVDGYATMHVEVDRQLQeacGKRPSLCIASVGVGSwaqSVVTHYAG---------DNSATNVVTVESEAAPCLLESLHVG 283
Cdd:cd01563   153 -LEGQKTIAFEIAEQLG---WEVPDYVVVPVGNGG---NITAIWKGfkelkelglIDRLPRMVGVQAEGAAPIVRAFKEG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 284 --EIVSVETSTTIMDGMNCGT-VStncWPSLKSGVYAS----VIVND--IDSHQSVVYLNDhGVNAGPCGAAPLAALRKL 354
Cdd:cd01563   226 kdDIEPVENPETIATAIRIGNpAS---GPKALRAVRESggtaVAVSDeeILEAQKLLARTE-GIFVEPASAASLAGLKKL 301

                         330
                  ....*....|....*.
gi 2270541331 355 HKQGLFPLDSDAVVVL 370
Cdd:cd01563   302 REEGIIDKGERVVVVL 317
PRK08197 PRK08197
threonine synthase; Validated
 56-228 8.32e-16

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 78.12  E-value: 8.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGYVFVKDESLrfgLP--SFKILGASWGVFKAVcektglpssvslgeagraaqKAGIS-LVTCTDG 132
Cdd:PRK08197   80 TPLLPLPRLGKALGIGRLWVKDEGL---NPtgSFKARGLAVGVSRAK--------------------ELGVKhLAMPTNG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 133 NWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDS---IAAAINETQGSDATlvmdTSWEGYSqv 209
Cdd:PRK08197  137 NAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAgkiVAEAVAEYGWFDVS----TLKEPYR-- 210

                         170
                  ....*....|....*....
gi 2270541331 210 pkwvVDGYATMHVEVDRQL 228
Cdd:PRK08197  211 ----IEGKKTMGLELAEQL 225
PRK08639 PRK08639
threonine dehydratase; Validated
 31-351 1.99e-15

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 77.15  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  31 NTLPRSAQIDPDLIALHHAFPEsmtTPLIELPELAAELGIGyVFVKDESL---RfglpSFKILGAswgvFKAVcektglp 107
Cdd:PRK08639    4 KMTVSAKDIDKAAKRLKDVVPE---TPLQRNDYLSEKYGAN-VYLKREDLqpvR----SYKLRGA----YNAI------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 108 ssVSLGEAGRAAqkaGIslVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGA---TVNVVNGSYDDSIA 184
Cdd:PRK08639   65 --SQLSDEELAA---GV--VCASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAA 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 185 AAINETQGSDATLV--MDTswegysqvPKwVVDGYATMHVEVDRQLQEAcgKRPSLCIASVGVGSWAQSVVTHYAGDNSA 262
Cdd:PRK08639  138 AAQEYAEETGATFIppFDD--------PD-VIAGQGTVAVEILEQLEKE--GSPDYVFVPVGGGGLISGVTTYLKERSPK 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 263 TNVVTVESEAAPCLLESLHVGEIVSVETSTTIMDGMNCGTVSTNCWPSLKSGVyASVIVND--------IDshqsvvYLN 334
Cdd:PRK08639  207 TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDVV-DDVVLVPegavcttiLE------LYN 279

                         330
                  ....*....|....*..
gi 2270541331 335 DHGVNAGPCGAAPLAAL 351
Cdd:PRK08639  280 KEGIVAEPAGALSIAAL 296
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 40-376 2.50e-14

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: 73.70  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  40 DPDLIALHHAFpesmtTPLIELPELAAELGIGyVFVKDESLrfgLP--SFKILGASWgvfkavcektglpssvslgeAGR 117
Cdd:COG0498    56 EEKAVSLGEGG-----TPLVKAPRLADELGKN-LYVKEEGH---NPtgSFKDRAMQV--------------------AVS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 118 AAQKAGISLVTC-TDGNWGRAVSRTAKYLGINATIFVPKT-MDEATRAKLRSEGATVNVVNGSYDD--SIAAAINETQGs 193
Cdd:COG0498   107 LALERGAKTIVCaSSGNGSAALAAYAARAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDaqRLVKELAADEG- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 194 datLVMDTSWEgysqvPkWVVDGYATMHVEVDRQLqeacGKRPSLCIASVGvgswaqsvvthyagdnSATNVV------- 266
Cdd:COG0498   186 ---LYAVNSIN-----P-ARLEGQKTYAFEIAEQL----GRVPDWVVVPTG----------------NGGNILagykafk 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 267 -------------TVESEAAPC--LLESLHVGE-IVSVETSTTIMDGMNCGtVStncwPSLKSGVYA-------SVIVND 323
Cdd:COG0498   237 elkelglidrlprLIAVQATGCnpILTAFETGRdEYEPERPETIAPSMDIG-NP----SNGERALFAlresggtAVAVSD 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2270541331 324 --IDSHQSVVYlNDHGVNAGPCGAAPLAALRKLHKQGLfpLDSDAVVVLFSTeGH 376
Cdd:COG0498   312 eeILEAIRLLA-RREGIFVEPATAVAVAGLRKLREEGE--IDPDEPVVVLST-GH 362
eutB PRK07476
threonine dehydratase; Provisional
 56-296 3.13e-13

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 69.99  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRfglP--SFKILGASWGVfkavcektglpssVSLGEAGRAAqkagiSLVTCTDGN 133
Cdd:PRK07476   20 TPLVASASLSARAGVP-VWLKLETLQ---PtgSFKLRGATNAL-------------LSLSAQERAR-----GVVTASTGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 134 WGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINetqgsdatLVMDtswEGYSQVPKW- 212
Cdd:PRK07476   78 HGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVER--------LVRE---EGLTMVPPFd 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 213 ---VVDGYATMHVEVDRQLQEAcgkrpSLCIASVGVGSWAQSVVTHYAGDNSATNV--VTVESEAApcLLESLHVGEIVS 287
Cdd:PRK07476  147 dprIIAGQGTIGLEILEALPDV-----ATVLVPLSGGGLASGVAAAVKAIRPAIRVigVSMERGAA--MHASLAAGRPVQ 219


                  ....*....
gi 2270541331 288 VETSTTIMD 296
Cdd:PRK07476  220 VEEVPTLAD 228
PRK06815 PRK06815
threonine/serine dehydratase;
51-297 7.72e-13

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 68.57  E-value: 7.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  51 PESMTTPLIELPELAAELGiGYVFVKDESLRFgLPSFKILGASwgvfkavcEKTGLPSSvslgeagrAAQKAGIslVTCT 130
Cdd:PRK06815   16 PQVRVTPLEHSPLLSQHTG-CEVYLKCEHLQH-TGSFKFRGAS--------NKLRLLNE--------AQRQQGV--ITAS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 131 DGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLVmdtswEGYSQVP 210
Cdd:PRK06815   76 SGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYI-----SPYNDPQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 211 kwVVDGYATMHVEVDRQLqeacgKRPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVET 290
Cdd:PRK06815  151 --VIAGQGTIGMELVEQQ-----PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAE 223


                  ....*..
gi 2270541331 291 STTIMDG 297
Cdd:PRK06815  224 QPTLSDG 230
PRK06110 PRK06110
threonine dehydratase;
47-353 2.16e-12

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 67.33  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  47 HHAFPesmTTPLIELPELAAELGIGyVFVKDESlrfGLP--SFKILGaswgvfkavcektGLPSSVSLGEAGRaaQKAGI 124
Cdd:PRK06110   16 YAAMP---PTPQYRWPLLAERLGCE-VWVKHEN---HTPtgAFKVRG-------------GLVYFDRLARRGP--RVRGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 125 slVTCTDGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVnVVNGS-YDDSIAAAINETQGsdatlvmdtsw 203
Cdd:PRK06110   74 --ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAEL-IEHGEdFQAAREEAARLAAE----------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 204 EGYSQVP---KWVVDGYATMHVEVDRQLqeacgkrPSLCIASV--GVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLE 278
Cdd:PRK06110  140 RGLHMVPsfhPDLVRGVATYALELFRAV-------PDLDVVYVpiGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYAL 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2270541331 279 SLHVGEIVSVETSTTIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSV-VYLND-HGVNAGpCGAAPLAALRK 353
Cdd:PRK06110  213 SFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMrAYFTDtHNVAEG-AGAAALAAALQ 288
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 39-370 1.19e-11

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 65.10  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  39 IDPDLIALHhafpeSMTTPLIELPELAAELGIGYVFVKDESLRFGLpSFKILGASWGVFKAVcektglpssvslgEAGRA 118
Cdd:TIGR00260  11 TEKDLVDLG-----EGVTPLFRAPALAANVGIKNLYVKELGHNPTL-SFKDRGMAVALTKAL-------------ELGND 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 119 AqkagisLVTCTDGNWGRAVSRTAKYLGINATIFVPKtmDEATRAKLRS---EGATVNVVNGSYDDSIAAAINETQGSDA 195
Cdd:TIGR00260  72 T------VLCASTGNTGAAAAAYAGKAGLKVVVLYPA--GKISLGKLAQalgYNAEVVAIDGNFDDAQRLVKQLFEDKPA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 196 TLVMDTSWEGYSqvpkwvVDGYATMHVEVDRQLQeacGKRPSLCIASVGVGS-----WAQSVVTHYAGDNSATNVVTVES 270
Cdd:TIGR00260 144 LGLNSANSIPYR------LEGQKTYAFEAVEQLG---WEAPDKVVVPVPNSGnfgaiWKGFKEKKMLGLDSLPVKRGIQA 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 271 E-AAPCLLESLHVGEIVSVETSTTIMDGMNCGtvSTNCWPSL-----KSGVYASVIVNDIDSHQSVVYLNDHGVNAGPCG 344
Cdd:TIGR00260 215 EgAADIVRAFLEGGQWEPIETPETLSTAMDIG--NPANWPRAleafrRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHS 292

                         330       340
                  ....*....|....*....|....*.
gi 2270541331 345 AAPLAALRKLHKQGLFPLDSDAVVVL 370
Cdd:TIGR00260 293 AVAVAALLKLVEKGTADPAERVVCAL 318
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
56-351 3.07e-11

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 63.99  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGiGYVFVKDESLRFgLPSFKILGAswgvFKAVCektglpssvSLGEAGRAAqkaGIslVTCTDGNWG 135
Cdd:PRK08638   28 TPLPRSNYLSERCK-GEIFLKLENMQR-TGSFKIRGA----FNKLS---------SLTDAEKRK---GV--VACSAGNHA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAA--INETqgsdatlvmdtswEGYSQVPKW- 212
Cdd:PRK08638   88 QGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVeeIVEE-------------EGRTFIPPYd 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 213 ---VVDGYATMHVEVDRQLQEAcgkrpSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVE 289
Cdd:PRK08638  155 dpkVIAGQGTIGLEILEDLWDV-----DTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHR 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2270541331 290 TSTTIMDGMNCGTVSTNCWPSLKSGVYASVIVNDIDSHQSVVYLNDHG--VNAGpCGAAPLAAL 351
Cdd:PRK08638  230 TTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNkvVTEG-AGALATAAL 292
PRK12483 PRK12483
threonine dehydratase; Reviewed
 56-308 4.90e-09

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 57.88  E-value: 4.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGiGYVFVKDESLRfglP--SFKILGASWGVfkavcektglpssvslgeAGRAAQKAGISLVTCTDGN 133
Cdd:PRK12483   38 TPLQRAPNLSARLG-NQVLLKREDLQ---PvfSFKIRGAYNKM------------------ARLPAEQLARGVITASAGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 134 WGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGSDATLvmdtswegysqVPKW- 212
Cdd:PRK12483   96 HAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTF-----------VPPFd 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 213 ---VVDGYATMHVEVDRQLQeacGKRPSLCIaSVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVE 289
Cdd:PRK12483  165 dpdVIAGQGTVAMEILRQHP---GPLDAIFV-PVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLG 240

                         250
                  ....*....|....*....
gi 2270541331 290 TSTTIMDGMNCGTVSTNCW 308
Cdd:PRK12483  241 QVGLFADGVAVAQIGEHTF 259
PLN02970 PLN02970
serine racemase
 56-323 4.99e-09

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 57.00  E-value: 4.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  56 TPLIELPELAAELGIGyVFVKDESLRFGlPSFKILGASWGVFKAVCEKtglpssvslgeagraAQKAgisLVTCTDGNWG 135
Cdd:PLN02970   28 TPVLTSSSLDALAGRS-LFFKCECFQKG-GAFKFRGACNAIFSLSDDQ---------------AEKG---VVTHSSGNHA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 136 RAVSRTAKYLGINATIFVPKTmdeATRAKLR---SEGATVNVVNGSYD--DSIAAAINETQGsdATLVmdtswEGYSQVP 210
Cdd:PLN02970   88 AALALAAKLRGIPAYIVVPKN---APACKVDaviRYGGIITWCEPTVEsrEAVAARVQQETG--AVLI-----HPYNDGR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 211 kwVVDGYATMHVEVDRQLQEAcgkrpSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVET 290
Cdd:PLN02970  158 --VISGQGTIALEFLEQVPEL-----DVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV 230

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2270541331 291 STTIMDGMNcGTVSTNCWPSLKSGVYASVIVND 323
Cdd:PLN02970  231 TNTIADGLR-ASLGDLTWPVVRDLVDDVITVDD 262
PRK06381 PRK06381
threonine synthase; Validated
 43-370 5.22e-09

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 57.02  E-value: 5.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  43 LIALHHAFPESmtTPLIELPELAAELGIGYVFVKDESlrfGLPSfkilgaswGVFKAVCEKTGLPSSVSLGeagraaqKA 122
Cdd:PRK06381    5 LSSSEEKPPGG--TPLLRARKLEEELGLRKIYLKFEG---ANPT--------GTQKDRIAEAHVRRAMRLG-------YS 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 123 GISLVTCtdGNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIaaainETQGSDAtlvMDTS 202
Cdd:PRK06381   65 GITVGTC--GNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAV-----ERSRKFA---KENG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 203 WegYSQVP---KWVVD--GYATMHVEVDRQLqeacGKRPSLCIASVGVGSwaqSVVTHYAG-----DNSATNV----VTV 268
Cdd:PRK06381  135 I--YDANPgsvNSVVDieAYSAIAYEIYEAL----GDVPDAVAVPVGNGT---TLAGIYHGfrrlyDRGKTSRmprmIGV 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 269 ESEAAPCLLESLHVG--EIVSVETSTTIMDGMNCGTVStncWPSLkSGVYA-SVIVndiDSHQSVVYLND---------- 335
Cdd:PRK06381  206 STSGGNQIVESFKRGssEVVDLEVDEIRETAVNEPLVS---YRSF-DGDNAlEAIY---DSHGYAFGFSDdemvkyaell 278

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2270541331 336 ---HGVNAGPCGAAPLAALRKLHKQglFPLDSDAVVVL 370
Cdd:PRK06381  279 rrmEGLNALPASASALAALVKYLKK--NGVNDNVVAVI 314
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
73-297 2.64e-07

threo-3-hydroxy-L-aspartate ammonia-lyase;


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 51.94  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  73 VFVKDESL-RFGlpSFKILGAswgvFKAVCEKTglpssvslgeagrAAQK-AGIslVTCTDGNWGRAVSRTAKYLGINAT 150
Cdd:PRK07048   41 VFFKCENFqRMG--AFKFRGA----YNALSQFS-------------PEQRrAGV--VTFSSGNHAQAIALSARLLGIPAT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 151 IFVPKTMDEATRAKLRSEGATVNVVNGSYDD--SIAAAINETQGsdATLvmdtswegysqVPKW----VVDGYATmhveV 224
Cdd:PRK07048  100 IVMPQDAPAAKVAATRGYGGEVVTYDRYTEDreEIGRRLAEERG--LTL-----------IPPYdhphVIAGQGT----A 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2270541331 225 DRQLQEACGKRPSLCIASVGVGSWAQSVVTHYAgDNSATNVVTVESEAAPCLLESLHVGEIVSVETSTTIMDG 297
Cdd:PRK07048  163 AKELFEEVGPLDALFVCLGGGGLLSGCALAARA-LSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADG 234
PLN02550 PLN02550
threonine dehydratase
 53-303 9.37e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 50.69  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  53 SMTTPLIELPELAAELGIGyVFVKDESLRfGLPSFKILGASWGVFKAVCEKtgLPSSVSLGEAGRAAQkaGISLvtctdg 132
Cdd:PLN02550  107 AIESPLQLAKKLSERLGVK-VLLKREDLQ-PVFSFKLRGAYNMMAKLPKEQ--LDKGVICSSAGNHAQ--GVAL------ 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 133 nwgravsrTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGsdatlvmdtswEGYSQVPKW 212
Cdd:PLN02550  175 --------SAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALE-----------EGRTFIPPF 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 213 ----VVDGYATMHVEVDRQLQEacgkrPSLCI-ASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVS 287
Cdd:PLN02550  236 dhpdVIAGQGTVGMEIVRQHQG-----PLHAIfVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVM 310

                         250
                  ....*....|....*.
gi 2270541331 288 VETSTTIMDGMNCGTV 303
Cdd:PLN02550  311 LDQVGGFADGVAVKEV 326
PRK06608 PRK06608
serine/threonine dehydratase;
55-312 3.71e-05

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 45.15  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331  55 TTPLIELPELAAELGiGYVFVKDESL-RFGlpSFKILGAswgvfkavcektgLPSSVSLGEAGRAAQKagisLVTCTDGN 133
Cdd:PRK06608   23 LTPIVHSESLNEMLG-HEIFFKVESLqKTG--AFKVRGV-------------LNHLLELKEQGKLPDK----IVAYSTGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 134 WGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINETQGsdatlvmdTSWEGYSQVPKwV 213
Cdd:PRK06608   83 HGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEEQG--------FYYIHPSDSDS-T 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2270541331 214 VDGYATMHVEVDRQLqeacGKRPSLCIASVGVGSWAQSVVTHYAGDNSATNVVTVESEAAPCLLESLHVGEIVSVETS-T 292
Cdd:PRK06608  154 IAGAGTLCYEALQQL----GFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpN 229

                         250       260
                  ....*....|....*....|
gi 2270541331 293 TIMDGMNCGTVSTNCWPSLK 312
Cdd:PRK06608  230 TIADGLKTLSVSARTFEYLK 249
PRK06450 PRK06450
threonine synthase; Validated
 132-189 1.74e-03

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 40.10  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2270541331 132 GNWGRAVSRTAKYLGINATIFVPKTMDEATRAKLRSEGATVNVVNGSYDDSIAAAINE 189
Cdd:PRK06450  106 GNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGSREDVAKAAENS 163
 
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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