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Conserved domains on  [gi|505807461|ref|WP_015705214|]
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MULTISPECIES: diaminopropionate ammonia-lyase [Klebsiella]

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) ...
 5-393 0e+00

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 TIGR03528:

Pssm-ID: 444852  Cd Length: 396  Bit Score: 711.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461    5 SLKMDIADNRF-FTGETSPLFSRQQAQQARHFHQKIAGYQPTPLYALKELATLFGVKNILVKDESQRFGLNAFKMLGGAY 83
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   84 AIAQLLCEKYHLDINAFSFETLKST-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGA 159
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNeIREKLgdiTFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  160 ECIVTDMNYDDTVRFTMQTAQKNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAG 239
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  240 GVLGYLVDVFGARDLHSVIVEPELADCIYRSGLK--GDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDAV 317
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461  318 AALGMRVLGNPVGNDHRVISGESGAVGLGTLAAVHFHPQRQALMNKLGLDSHSVVLVISTEGDTDVQHYREVVWEG 393
Cdd:TIGR03528 321 AAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
 
Name Accession Description Interval E-value
2_3_DAP_am_ly TIGR03528
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ...
 5-393 0e+00

diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.


Pssm-ID: 274631  Cd Length: 396  Bit Score: 711.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461    5 SLKMDIADNRF-FTGETSPLFSRQQAQQARHFHQKIAGYQPTPLYALKELATLFGVKNILVKDESQRFGLNAFKMLGGAY 83
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   84 AIAQLLCEKYHLDINAFSFETLKST-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGA 159
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNeIREKLgdiTFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  160 ECIVTDMNYDDTVRFTMQTAQKNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAG 239
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  240 GVLGYLVDVFGARDLHSVIVEPELADCIYRSGLK--GDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDAV 317
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461  318 AALGMRVLGNPVGNDHRVISGESGAVGLGTLAAVHFHPQRQALMNKLGLDSHSVVLVISTEGDTDVQHYREVVWEG 393
Cdd:TIGR03528 321 AAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-396 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 682.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   1 MSAFSLKMDIADNRFFTGETSPLFSRQQAQQARHFHQKIAGYQPTPLYALKELATLFGVKNILVKDESQRFGLNAFKMLG 80
Cdd:PRK08206   1 MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  81 GAYAIAQLLCEKYHLDINAFSFETLKS----TIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILR 156
Cdd:PRK08206  81 GAYAVARLLAEKLGLDISELSFEELTSgevrEKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 157 LGAECIVTDMNYDDTVRFTMQTAQKNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGiARPTHVFLQAGVGA 236
Cdd:PRK08206 161 LGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMG-VPPTHVFLQAGVGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 237 MAGGVLGYLVDVFGARDLHSVIVEPELADCIYRSGLKGDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDA 316
Cdd:PRK08206 240 LAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAVDGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 317 VAALGMRVLGNPVGNDHRVISGESGAVGLGTLAAVHFHPQRQALMNKLGLDSHSVVLVISTEGDTDVQHYREVVWEGKLP 396
Cdd:PRK08206 320 VAALGMRILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA 399
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 20-395 1.62e-91

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: 278.46  E-value: 1.62e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  20 TSPLFSRQQAQQARHFHQKIagYQPTPLYALKELATLFGVkNILVKDESQRFgLNAFKMLGGAYAIAQLlcekyhldina 99
Cdd:COG1171    2 TALMPTLADIEAAAARIAGV--VRRTPLLRSPTLSERLGA-EVYLKLENLQP-TGSFKLRGAYNALASL----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 100 fsfetlkSTIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTA 179
Cdd:COG1171   67 -------SEEERARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 180 QKNGWEVVQDTAwegytkiPTWIMQGYATLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIV 259
Cdd:COG1171  140 EEEGATFVHPFD-------DPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAALKAL--SPDIRVIGV 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 260 EPELADCIYRSGLKGDIVNVGGdMATIMAGLACGEPNPLGWEILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGE 339
Cdd:COG1171  206 EPEGAAAMYRSLAAGEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLL----LERTKIVVEP 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461 340 SGAVGlgtLAAVHFHPQRQAlmnklgldsHSVVLVISTEGDTDVQHYREVVWEGKL 395
Cdd:COG1171  281 AGAAA---LAALLAGKERLK---------GKRVVVVLSGGNIDPDRLAEILERGLV 324
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 41-378 4.25e-42

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: 149.38  E-value: 4.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   41 GYQPTPLYALKELATLFGVkNILVKDES-QRFGlnAFKMLGGAYAIAQLLcekyhldinafsfetlksTIKEKMTFATTT 119
Cdd:pfam00291   4 GIGPTPLVRLPRLSKELGV-DVYLKLESlNPTG--SFKDRGALNLLLRLK------------------EGEGGKTVVEAS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  120 DGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtaWEGYTKIP 199
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAE----------GPGAYYIN 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  200 ----TWIMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFGARDLhsVIVEPELADCIYRSGLKGD 275
Cdd:pfam00291 133 qydnPLNIEGYGTIGLEILEQLG----GDPDAVVVPVGGGGLIAGIARGLKELGPDVRV--IGVEPEGAPALARSLAAGR 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  276 IVNVGGdMATIMAGLACG-EPNPLGWEILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGESGAVGLGTLAAVhfh 354
Cdd:pfam00291 207 PVPVPV-ADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLL----ARREGIVVEPSSAAALAALKLA--- 278

                         330       340
                  ....*....|....*....|....
gi 505807461  355 pqrqalmNKLGLDSHSVVLVISTE 378
Cdd:pfam00291 279 -------LAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 45-262 5.77e-32

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: 121.08  E-value: 5.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGVkNILVKDESQRFGLnAFKMLGGAYAIAQLLCEKyhldinafsfetlkstIKEKMTFATTTDGNHG 124
Cdd:cd00640    1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTG-SFKDRGALNLILLAEEEG----------------KLPKGVIIESTGGNTG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 125 RGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKN-GWEVVQDTawegytkIPTWIM 203
Cdd:cd00640   63 IALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQF-------DNPANI 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505807461 204 QGYATLADEAVEQMAAMgiaRPTHVFLQAGVGAMAGGVLGYLVDvfGARDLHSVIVEPE 262
Cdd:cd00640  136 AGQGTIGLEILEQLGGQ---KPDAVVVPVGGGGNIAGIARALKE--LLPNVKVIGVEPE 189
 
Name Accession Description Interval E-value
2_3_DAP_am_ly TIGR03528
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ...
 5-393 0e+00

diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.


Pssm-ID: 274631  Cd Length: 396  Bit Score: 711.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461    5 SLKMDIADNRF-FTGETSPLFSRQQAQQARHFHQKIAGYQPTPLYALKELATLFGVKNILVKDESQRFGLNAFKMLGGAY 83
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   84 AIAQLLCEKYHLDINAFSFETLKST-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGA 159
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNeIREKLgdiTFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  160 ECIVTDMNYDDTVRFTMQTAQKNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAG 239
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  240 GVLGYLVDVFGARDLHSVIVEPELADCIYRSGLK--GDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDAV 317
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461  318 AALGMRVLGNPVGNDHRVISGESGAVGLGTLAAVHFHPQRQALMNKLGLDSHSVVLVISTEGDTDVQHYREVVWEG 393
Cdd:TIGR03528 321 AAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-396 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 682.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   1 MSAFSLKMDIADNRFFTGETSPLFSRQQAQQARHFHQKIAGYQPTPLYALKELATLFGVKNILVKDESQRFGLNAFKMLG 80
Cdd:PRK08206   1 MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  81 GAYAIAQLLCEKYHLDINAFSFETLKS----TIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILR 156
Cdd:PRK08206  81 GAYAVARLLAEKLGLDISELSFEELTSgevrEKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 157 LGAECIVTDMNYDDTVRFTMQTAQKNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGiARPTHVFLQAGVGA 236
Cdd:PRK08206 161 LGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMG-VPPTHVFLQAGVGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 237 MAGGVLGYLVDVFGARDLHSVIVEPELADCIYRSGLKGDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDA 316
Cdd:PRK08206 240 LAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAVDGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 317 VAALGMRVLGNPVGNDHRVISGESGAVGLGTLAAVHFHPQRQALMNKLGLDSHSVVLVISTEGDTDVQHYREVVWEGKLP 396
Cdd:PRK08206 320 VAALGMRILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA 399
diampropi_NH3ly TIGR01747
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ...
 23-392 0e+00

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: 624.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   23 LFSRQQAQQARHFHQKIAGYQPTPLYALKELATLFGVKNILVKDESQRFGLNAFKMLGGAYAIAQLLCEKYHLDINAFSF 102
Cdd:TIGR01747   1 LFSQSQAKLALAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDIETLSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  103 ETLKST-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQT 178
Cdd:TIGR01747  81 EHLKNDaIGEKMgqaTFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  179 AQKNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAGGVLGYLVDVFGARDLHSVI 258
Cdd:TIGR01747 161 AQQHGWVVVQDTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHVLLQAGVGSMAGGVLGYFVDVYSENNPHSIV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  259 VEPELADCIYRSGLK--GDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDAVAALGMRVLGNPVGNDHRVI 336
Cdd:TIGR01747 241 VEPDKADCLYQSAVKkdGDIVNVGGDMATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGGDPRII 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461  337 SGESGAVGLGTLAAVHFHPQRQALMNKLGLDSHSVVLVISTEGDTDVQHYREVVWE 392
Cdd:TIGR01747 321 SGESGAVGLGLLAAVMYHPQYQSLMEKLQLDKDAVVLVISTEGDTDPDHYREIVWE 376
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 20-395 1.62e-91

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: 278.46  E-value: 1.62e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  20 TSPLFSRQQAQQARHFHQKIagYQPTPLYALKELATLFGVkNILVKDESQRFgLNAFKMLGGAYAIAQLlcekyhldina 99
Cdd:COG1171    2 TALMPTLADIEAAAARIAGV--VRRTPLLRSPTLSERLGA-EVYLKLENLQP-TGSFKLRGAYNALASL----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 100 fsfetlkSTIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTA 179
Cdd:COG1171   67 -------SEEERARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 180 QKNGWEVVQDTAwegytkiPTWIMQGYATLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIV 259
Cdd:COG1171  140 EEEGATFVHPFD-------DPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAALKAL--SPDIRVIGV 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 260 EPELADCIYRSGLKGDIVNVGGdMATIMAGLACGEPNPLGWEILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGE 339
Cdd:COG1171  206 EPEGAAAMYRSLAAGEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLL----LERTKIVVEP 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461 340 SGAVGlgtLAAVHFHPQRQAlmnklgldsHSVVLVISTEGDTDVQHYREVVWEGKL 395
Cdd:COG1171  281 AGAAA---LAALLAGKERLK---------GKRVVVVLSGGNIDPDRLAEILERGLV 324
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 41-378 4.25e-42

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: 149.38  E-value: 4.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   41 GYQPTPLYALKELATLFGVkNILVKDES-QRFGlnAFKMLGGAYAIAQLLcekyhldinafsfetlksTIKEKMTFATTT 119
Cdd:pfam00291   4 GIGPTPLVRLPRLSKELGV-DVYLKLESlNPTG--SFKDRGALNLLLRLK------------------EGEGGKTVVEAS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  120 DGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtaWEGYTKIP 199
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAE----------GPGAYYIN 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  200 ----TWIMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFGARDLhsVIVEPELADCIYRSGLKGD 275
Cdd:pfam00291 133 qydnPLNIEGYGTIGLEILEQLG----GDPDAVVVPVGGGGLIAGIARGLKELGPDVRV--IGVEPEGAPALARSLAAGR 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  276 IVNVGGdMATIMAGLACG-EPNPLGWEILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGESGAVGLGTLAAVhfh 354
Cdd:pfam00291 207 PVPVPV-ADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLL----ARREGIVVEPSSAAALAALKLA--- 278

                         330       340
                  ....*....|....*....|....
gi 505807461  355 pqrqalmNKLGLDSHSVVLVISTE 378
Cdd:pfam00291 279 -------LAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 45-262 5.77e-32

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: 121.08  E-value: 5.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGVkNILVKDESQRFGLnAFKMLGGAYAIAQLLCEKyhldinafsfetlkstIKEKMTFATTTDGNHG 124
Cdd:cd00640    1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTG-SFKDRGALNLILLAEEEG----------------KLPKGVIIESTGGNTG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 125 RGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKN-GWEVVQDTawegytkIPTWIM 203
Cdd:cd00640   63 IALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQF-------DNPANI 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505807461 204 QGYATLADEAVEQMAAMgiaRPTHVFLQAGVGAMAGGVLGYLVDvfGARDLHSVIVEPE 262
Cdd:cd00640  136 AGQGTIGLEILEQLGGQ---KPDAVVVPVGGGGNIAGIARALKE--LLPNVKVIGVEPE 189
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 36-376 2.11e-28

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: 112.97  E-value: 2.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  36 HQKIAGY-QPTPLYALKELATLFGVkNILVKDES-QRFGlnAFKMLGGAYAIAQLLCEKYHLDINAFSfetlkstikekm 113
Cdd:cd01562    8 AARIKPVvRRTPLLTSPTLSELLGA-EVYLKCENlQKTG--SFKIRGAYNKLLSLSEEERAKGVVAAS------------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 114 tfatttDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtawE 193
Cdd:cd01562   73 ------AGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEE-----------E 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 194 GYTKIPT----WIMQGYATLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYL------VDVFGardlhsviVEPEL 263
Cdd:cd01562  136 GLTFIHPfddpDVIAGQGTIGLEILEQVPD-----LDAVFVPVGGGGLIAGIATAVkalspnTKVIG--------VEPEG 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 264 ADCIYRSGLKGDIVNVgGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGESGAV 343
Cdd:cd01562  203 APAMAQSLAAGKPVTL-PEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLL----FEREKLVAEPAGAL 277

                        330       340       350
                 ....*....|....*....|....*....|...
gi 505807461 344 GlgtLAAvhfhpqrqALMNKLGLDSHSVVLVIS 376
Cdd:cd01562  278 A---LAA--------LLSGKLDLKGKKVVVVLS 299
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
43-277 1.91e-14

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 74.79  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  43 QPTPLYALKELATLFGvKNILVKDESQR--FglnAFKmLGGAYA-IAQLlcekyhldinafSFETLKSTIkekmtfATTT 119
Cdd:PRK09224  19 QETPLEKAPKLSARLG-NQVLLKREDLQpvF---SFK-LRGAYNkMAQL------------TEEQLARGV------ITAS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 120 DGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtawEGYTKIP 199
Cdd:PRK09224  76 AGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEE-----------EGLTFIH 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 200 TW----IMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYL------VDVFGardlhsviVEPELADCIYR 269
Cdd:PRK09224 145 PFddpdVIAGQGTIAMEILQQHP----HPLDAVFVPVGGGGLIAGVAAYIkqlrpeIKVIG--------VEPEDSACLKA 212


                 ....*...
gi 505807461 270 SGLKGDIV 277
Cdd:PRK09224 213 ALEAGERV 220
PRK08639 PRK08639
threonine dehydratase; Validated
 121-277 1.29e-13

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 71.76  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 121 GNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGA---ECIVTDMNYDDtvrfTMQTAQkngwevvQDTAWEGYTK 197
Cdd:PRK08639  82 GNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDD----SAAAAQ-------EYAEETGATF 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 198 IPTW----IMQGYATLADEAVEQMAAMGiaRPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPELADCIYRSGLK 273
Cdd:PRK08639 151 IPPFddpdVIAGQGTVAVEILEQLEKEG--SPDYVFVPVGGGGLISGVTTYLKER--SPKTKIIGVEPAGAASMKAALEA 226


                 ....
gi 505807461 274 GDIV 277
Cdd:PRK08639 227 GKPV 230
PRK06815 PRK06815
threonine/serine dehydratase;
116-341 1.45e-13

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 70.88  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 116 ATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtawEGY 195
Cdd:PRK06815  72 ITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQ-----------QGK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 196 TKIPTW----IMQGYATLADEAVEQmaamgIARPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPELADCIYRSG 271
Cdd:PRK06815 141 VYISPYndpqVIAGQGTIGMELVEQ-----QPDLDAVFVAVGGGGLISGIATYLKTL--SPKTEIIGCWPANSPSLYTSL 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505807461 272 LKGDIVNVgGDMATIMAGLACG-EPNPLGWEILRNCATQFISCQDAVAALGMRVLGNpvgNDHRVISGESG 341
Cdd:PRK06815 214 EAGEIVEV-AEQPTLSDGTAGGvEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAE---TDRWLIEGAAG 280
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 45-316 1.89e-13

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: 70.70  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGVKNILVKDEsqrfGLN---AFKMLGGAYAIAQLLcekyHLDINafsfetlkstikekmTFATTTDG 121
Cdd:cd01563   23 TPLVRAPRLGERLGGKNLYVKDE----GLNptgSFKDRGMTVAVSKAK----ELGVK---------------AVACASTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 122 NHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGWEVVqdtawegyTKIPTW 201
Cdd:cd01563   80 NTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS--------NSLNPY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 202 IMQGYATLADEAVEQmaaMGIARPTHVFLQAGVGamaGGVLGYLVdvfGARDLHS----------VIVEPELADCIYRSG 271
Cdd:cd01563  152 RLEGQKTIAFEIAEQ---LGWEVPDYVVVPVGNG---GNITAIWK---GFKELKElglidrlprmVGVQAEGAAPIVRAF 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 505807461 272 LKG-DIVNVGGDMATIMAGLACGepNPLGW----EILRNCATQFISCQDA 316
Cdd:cd01563  223 KEGkDDIEPVENPETIATAIRIG--NPASGpkalRAVRESGGTAVAVSDE 270
PRK06110 PRK06110
threonine dehydratase;
22-325 2.98e-13

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 70.02  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  22 PLFSRQQAQQARHF-HQKIAgyqPTPLYALKELATLFGVkNILVKDESQRfGLNAFKMLGG-AYaiaqllcekyhldina 99
Cdd:PRK06110   1 MMFTLAELEAAAAVvYAAMP---PTPQYRWPLLAERLGC-EVWVKHENHT-PTGAFKVRGGlVY---------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 100 fsFETLKSTIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTA 179
Cdd:PRK06110  60 --FDRLARRGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 180 QKNGWEVVqdtawegytkiPT---WIMQGYATLADEAVEQMAAMGIarpthVFLQAGVGAmagGVLGylvdVFGARDL-- 254
Cdd:PRK06110 138 AERGLHMV-----------PSfhpDLVRGVATYALELFRAVPDLDV-----VYVPIGMGS---GICG----AIAARDAlg 194

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807461 255 ---HSVIVEPELADCIYRSGLKGDIVNVggDMATIMA-GLACGEPNPLGWEILRNCATQFISCQDAVAALGMRVL 325
Cdd:PRK06110 195 lktRIVGVVSAHAPAYALSFEAGRVVTT--PVATTLAdGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAY 267
eutB PRK07476
threonine dehydratase; Provisional
 31-241 8.80e-13

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 68.45  E-value: 8.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  31 QARhfhQKIAGYQP-TPLYALKELATLFGVKNILVKDESQRFGlnAFKMLGGAYAIAQLLCEKYHLDINAFSfetlksti 109
Cdd:PRK07476   8 RAR---RRIAGRVRrTPLVASASLSARAGVPVWLKLETLQPTG--SFKLRGATNALLSLSAQERARGVVTAS-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 110 kekmtfatttDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDtvrftmqtAQKngwEVVQD 189
Cdd:PRK07476  75 ----------TGNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDD--------AQA---EVERL 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505807461 190 TAWEGYTKIPTW----IMQGYATLADEAVEQMAAMGIarpthVFLQAGVGAMAGGV 241
Cdd:PRK07476 134 VREEGLTMVPPFddprIIAGQGTIGLEILEALPDVAT-----VLVPLSGGGLASGV 184
THD1 TIGR02079
threonine dehydratase; This model represents threonine dehydratase, the first step in the ...
 44-245 2.69e-11

threonine dehydratase; This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 273957 [Multi-domain]  Cd Length: 409  Bit Score: 64.77  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461   44 PTPLYALKELATLFGVkNILVKDES-QRfgLNAFKMLGGAYAIAQLlcekyhldinafSFETLKSTikekmtFATTTDGN 122
Cdd:TIGR02079  16 HTPLQLNERLSEKYGA-NIYLKREDlQP--VRSYKIRGAYNFLKQL------------SDAQLAKG------VVCASAGN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  123 HGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIvtdmnyddTVRFTMQTAQKNGWEVVQDTAWEGYTKIPTW- 201
Cdd:TIGR02079  75 HAQGFAYACRHLGVHGTVFMPATTPKQKIDRVKIFGGEFI--------EIILVGDTFDQCAAAAREHVEDHGGTFIPPFd 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 505807461  202 ---IMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYL 245
Cdd:TIGR02079 147 dprIIEGQGTVAAEILDQLP----EKPDYVVVPVGGGGLISGLTTYL 189
PLN02550 PLN02550
threonine dehydratase
 45-281 4.45e-11

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 64.56  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGVKNILVKDESQRfgLNAFKMLGGAYAIAQLLCEKYHldinafsfetlKSTIkekmtfaTTTDGNHG 124
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQP--VFSFKLRGAYNMMAKLPKEQLD-----------KGVI-------CSSAGNHA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 125 RGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtawEGYTKIPTW--- 201
Cdd:PLN02550 170 QGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALE-----------EGRTFIPPFdhp 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 202 -IMQGYATLADEAVEQMAAmgiarPTH-VFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPELADCIYRSGLKGDIV-- 277
Cdd:PLN02550 239 dVIAGQGTVGMEIVRQHQG-----PLHaIFVPVGGGGLIAGIAAYVKRV--RPEVKIIGVEPSDANAMALSLHHGERVml 311


                 ....*
gi 505807461 278 -NVGG 281
Cdd:PLN02550 312 dQVGG 316
PRK06381 PRK06381
threonine synthase; Validated
 114-241 6.40e-11

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 62.80  E-value: 6.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 114 TFATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGWevvqdtawe 193
Cdd:PRK06381  65 GITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI--------- 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505807461 194 gYTKIP----TWI-MQGYATLADEAVEQMAAMgiarPTHVFLQAGVGAMAGGV 241
Cdd:PRK06381 136 -YDANPgsvnSVVdIEAYSAIAYEIYEALGDV----PDAVAVPVGNGTTLAGI 183
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 121-388 4.17e-10

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: 60.39  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 121 GNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNY---DDTVRFTMqTAQKNGWEVVQ----DTAWE 193
Cdd:cd06448   60 GNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWweaDNYLREEL-AENDPGPVYVHpfddPLIWE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 194 gytkiptwimqGYATLADEAVEQMAAMGiaRPTHVFLQAGVGAMAGGVLGYLVDVfGARDLHSVIVEPELADCIYRSGLK 273
Cdd:cd06448  139 -----------GHSSMVDEIAQQLQSQE--KVDAIVCSVGGGGLLNGIVQGLERN-GWGDIPVVAVETEGAHSLNASLKA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 274 GDIVNVgGDMATIMAGLACGEPNPLGWEILRNCATQ--FISCQDAVAALgMRVLgnpvgNDHRVISGES-GAvglgTLAA 350
Cdd:cd06448  205 GKLVTL-PKITSVATSLGAKTVSSQALEYAQEHNIKseVVSDRDAVQAC-LRFA-----DDERILVEPAcGA----ALAV 273

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 505807461 351 VhFHPQRQALMNKLGLDSHSVVLVI----STEGDTDVQHYRE 388
Cdd:cd06448  274 V-YSGKILDLQLEVLLTPLDNVVVVvcggSNITLEQLKEYKK 314
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 45-262 8.75e-10

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: 59.06  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGVkNILVKDESQRFG-----LNAFKMLGGAYAiaqllcekyhldinafsfetlKSTIKEKMTFATTT 119
Cdd:cd01561    3 TPLVRLNRLSPGTGA-EIYAKLEFFNPGgsvkdRIALYMIEDAEK---------------------RGLLKPGTTIIEPT 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 120 DGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTD-MNYDDtvrftMQTAQKNGWEVVQDT--AWegyt 196
Cdd:cd01561   61 SGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPeAEADG-----MKGAIAKARELAAETpnAF---- 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505807461 197 kiptWIMQ---------GYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFgaRDLHSVIVEPE 262
Cdd:cd01561  132 ----WLNQfenpanpeaHYETTAPEIWEQLD----GKVDAFVAGVGTGGTITGVARYLKEKN--PNVRIVGVDPV 196
PRK12483 PRK12483
threonine dehydratase; Reviewed
 117-280 5.24e-09

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 57.88  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 117 TTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtawEGYT 196
Cdd:PRK12483  90 TASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEE-----------EGLT 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 197 KIPTW----IMQGYATLADEAVEQMAAmgiarPTH-VFLQAGVGAMAGGVLGYLVDVfgaRDLHSVI-VEPELADCIYRS 270
Cdd:PRK12483 159 FVPPFddpdVIAGQGTVAMEILRQHPG-----PLDaIFVPVGGGGLIAGIAAYVKYV---RPEIKVIgVEPDDSNCLQAA 230

                        170
                 ....*....|
gi 505807461 271 GLKGDIVNVG 280
Cdd:PRK12483 231 LAAGERVVLG 240
PRK06608 PRK06608
serine/threonine dehydratase;
36-242 5.83e-09

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 57.09  E-value: 5.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  36 HQKIAGY-QPTPLYALKELATLFGVKnILVKDES-QRFGlnAFKMLGGAYAIAQLLcEKYHLdinafsfetlkstIKEKM 113
Cdd:PRK06608  14 HNRIKQYlHLTPIVHSESLNEMLGHE-IFFKVESlQKTG--AFKVRGVLNHLLELK-EQGKL-------------PDKIV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 114 TFATttdGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDmnyddtvrfTMQTAQKngwEVVQDTAwE 193
Cdd:PRK06608  77 AYST---GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTN---------TRQEAEE---KAKEDEE-Q 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505807461 194 GYTKIPTW----IMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVL 242
Cdd:PRK06608 141 GFYYIHPSdsdsTIAGAGTLCYEALQQLG----FSPDAIFASCGGGGLISGTY 189
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 45-271 8.94e-09

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: 56.21  E-value: 8.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGVkNILVKDESqrfgLN---------AFKMLggAYAIAqllcekyhldinafsfetlKSTIKEKMTF 115
Cdd:COG0031   14 TPLVRLNRLSPGPGA-EIYAKLES----FNpggsvkdriALSMI--EDAEK-------------------RGLLKPGGTI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 116 ATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDdtvrftMQTAQKNGWEVVQDTawEGY 195
Cdd:COG0031   68 VEATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEG------MKGAIDKAEELAAET--PGA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 196 tkipTWIMQG---------YATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFgaRDLHSVIVEPElaDC 266
Cdd:COG0031  140 ----FWPNQFenpanpeahYETTGPEIWEQTD----GKVDAFVAGVGTGGTITGVGRYLKERN--PDIKIVAVEPE--GS 207


                 ....*
gi 505807461 267 IYRSG 271
Cdd:COG0031  208 PLLSG 212
PRK08813 PRK08813
threonine dehydratase; Provisional
 121-184 9.88e-09

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 56.56  E-value: 9.88e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505807461 121 GNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGW 184
Cdd:PRK08813  90 GNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGY 153
PLN02970 PLN02970
serine racemase
 36-392 1.17e-08

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 56.23  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  36 HQKIAGY-QPTPLYALKELATLFGVKnILVKDES-QRFGlnAFKMLGGAYAIAQLlcekyhldinafSFETLKSTIkekm 113
Cdd:PLN02970  18 RKRIAPFiHRTPVLTSSSLDALAGRS-LFFKCECfQKGG--AFKFRGACNAIFSL------------SDDQAEKGV---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 114 tfATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMnyddtvrfTMQTAQKNGWEVVQDTawe 193
Cdd:PLN02970  79 --VTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEP--------TVESREAVAARVQQET--- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 194 GYTKIPTW----IMQGYATLADEAVEQMAAMGIarpthVFLQAGVGAMAGGVlgylvdVFGARDLHSVI----VEPELAD 265
Cdd:PLN02970 146 GAVLIHPYndgrVISGQGTIALEFLEQVPELDV-----IIVPISGGGLISGI------ALAAKAIKPSIkiiaAEPKGAD 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 266 CIYRSGLKGDIVNVgGDMATIMAGLAcGEPNPLGWEILRNCATQFISCQDAVAALGMRVLGNPVgndhRVISGESGAVGL 345
Cdd:PLN02970 215 DAAQSKAAGEIITL-PVTNTIADGLR-ASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERL----KVVVEPSGAIGL 288

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 505807461 346 gtlaAVHFHPQRQalMNKLGLDSHSVVLVISTeGDTDVQhyreVVWE 392
Cdd:PLN02970 289 ----AAALSDSFR--SNPAWKGCKNVGIVLSG-GNVDLG----VLWE 324
PRK08246 PRK08246
serine/threonine dehydratase;
121-356 8.41e-08

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 53.42  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 121 GNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGweVVQDTAwegYTKIPT 200
Cdd:PRK08246  77 GNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETG--ALLCHA---YDQPEV 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 201 WIMQGyaTLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYlvdVFGARDLhsVIVEPELADCIYRSGLKGDIVNV- 279
Cdd:PRK08246 152 LAGAG--TLGLEIEEQAPG-----VDTVLVAVGGGGLIAGIAAW---FEGRARV--VAVEPEGAPTLHAALAAGEPVDVp 219

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505807461 280 -GGDMATIMAGLACGEpnpLGWEILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGESGAVGLGTLAAVHFHPQ 356
Cdd:PRK08246 220 vSGIAADSLGARRVGE---IAFALARAHVVTSVLVSDEAIIAARRAL----WEELRLAVEPGAATALAALLSGAYVPA 290
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
36-279 9.88e-08

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 53.10  E-value: 9.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  36 HQKIAGY-QPTPLYALKELATLFGVKnILVKDES-QRFGlnAFKMLGGAYAIAQLLCEKYHLDINAFSfetlkstikekm 113
Cdd:PRK07048  15 AARLAGVaHRTPVLTSRTADARTGAQ-VFFKCENfQRMG--AFKFRGAYNALSQFSPEQRRAGVVTFS------------ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 114 tfatttDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNgwevvqdtawe 193
Cdd:PRK07048  80 ------SGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER----------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 194 GYTKIPTW----IMQGYATLADEAVEQMAAMGIarpthVFLQAGVG------AMAGGVLGYLVDVFGardlhsviVEPEL 263
Cdd:PRK07048 143 GLTLIPPYdhphVIAGQGTAAKELFEEVGPLDA-----LFVCLGGGgllsgcALAARALSPGCKVYG--------VEPEA 209

                        250
                 ....*....|....*.
gi 505807461 264 ADCIYRSGLKGDIVNV 279
Cdd:PRK07048 210 GNDGQQSFRSGEIVHI 225
PRK07334 PRK07334
threonine dehydratase; Provisional
 121-305 1.70e-07

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 52.97  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 121 GNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGWEVVQ--DTAwegytki 198
Cdd:PRK07334  80 GNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHpyDDP------- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 199 ptWIMQGYATLADEAVEqmaamgiARPThvfLQAGVGAMAGGVL--GYLVDVFGAR-DLHSVIVEPELADCIYrSGLKGD 275
Cdd:PRK07334 153 --AVIAGQGTVALEMLE-------DAPD---LDTLVVPIGGGGLisGMATAAKALKpDIEIIGVQTELYPSMY-AAIKGV 219

                        170       180       190
                 ....*....|....*....|....*....|
gi 505807461 276 IVNVGGDmaTIMAGLACGEPNPLGWEILRN 305
Cdd:PRK07334 220 ALPCGGS--TIAEGIAVKQPGQLTLEIVRR 247
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
117-217 3.25e-07

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 51.66  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 117 TTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKngwevvqdtawEGYT 196
Cdd:PRK08638  80 ACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEE-----------EGRT 148

                         90       100
                 ....*....|....*....|....*
gi 505807461 197 KIPTW----IMQGYATLADEAVEQM 217
Cdd:PRK08638 149 FIPPYddpkVIAGQGTIGLEILEDL 173
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 45-377 8.84e-06

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: 47.50  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461  45 TPLYALKELATLFGvKNILVKDEsqrfGLN---AFKMLGgayaiAQLLCEKyhldinafsfetlkstIKE--KMTFATTT 119
Cdd:COG0498   67 TPLVKAPRLADELG-KNLYVKEE----GHNptgSFKDRA-----MQVAVSL----------------ALErgAKTIVCAS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 120 DGNHGRGVAWAAQQLGQNAVVYMPKGS-AQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGWEVVQDTAWegytki 198
Cdd:COG0498  121 SGNGSAALAAYAARAGIEVFVFVPEGKvSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINP------ 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 199 ptWIMQGYATLADEAVEQMAAMgiarPTHVFLqaGVGAmAGGVLGYLVdvfGARDLHS----------VIVEPELADCIY 268
Cdd:COG0498  195 --ARLEGQKTYAFEIAEQLGRV----PDWVVV--PTGN-GGNILAGYK---AFKELKElglidrlprlIAVQATGCNPIL 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 269 RSGLKGDIVNVGGDMATIMAGLACGepNPLGWE----ILRNCATQFISCQDAVAALGMRVLgnpvGNDHRVISGESGAVG 344
Cdd:COG0498  263 TAFETGRDEYEPERPETIAPSMDIG--NPSNGEralfALRESGGTAVAVSDEEILEAIRLL----ARREGIFVEPATAVA 336

                        330       340       350
                 ....*....|....*....|....*....|...
gi 505807461 345 lgtLAAVhfhpqrQALMNKLGLDSHSVVLVIST 377
Cdd:COG0498  337 ---VAGL------RKLREEGEIDPDEPVVVLST 360
D-Ser-dehyd cd06447
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 121-305 1.46e-05

D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.


Pssm-ID: 107208  Cd Length: 404  Bit Score: 46.96  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 121 GNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTV-RFTMQTAQKNGWEVVQDtawEGYTKIp 199
Cdd:cd06447  143 GNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVeEGRKQAAADPMCYFVDD---ENSRDL- 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 200 twiMQGYATLADEAVEQMAAMGI----ARPTHVFLQAGVGAMAGGVLGYLVDVFGArDLHSVIVEPELADCI---YRSGL 272
Cdd:cd06447  219 ---FLGYAVAASRLKAQLAELGIkvdaEHPLFVYLPCGVGGAPGGVAFGLKLIFGD-NVHCFFAEPTHSPCMllgMATGL 294

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 505807461 273 KGDI--VNVGGDMATIMAGLACGEPNPLGWEILRN 305
Cdd:cd06447  295 HDKIsvQDIGIDNRTAADGLAVGRPSGLVGKLMEP 329
PRK05638 PRK05638
threonine synthase; Validated
 115-267 9.82e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 44.42  E-value: 9.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 115 FATTTDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTDMNYDDTVRFTMQTAQKNGWevvqdtaweg 194
Cdd:PRK05638 115 FIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGL---------- 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505807461 195 YTKIPTW---IMQGYATLADEAVEQMAamgiarPTHVFLQAGVGAmaggvlgYLVDVF-GARDLHSVIVEPELADCI 267
Cdd:PRK05638 185 YNVTPEYniiGLEGQKTIAFELWEEIN------PTHVIVPTGSGS-------YLYSIYkGFKELLEIGVIEEIPKLI 248
PRK02991 PRK02991
D-serine dehydratase; Provisional
 205-298 1.20e-03

D-serine dehydratase; Provisional


Pssm-ID: 235096  Cd Length: 441  Bit Score: 40.64  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505807461 205 GYATLADEAVEQMAAMGIA----RPTHVFLQAGVGAMAGGVLGYLVDVFGArDLHSVIVEPELADCIY---RSGLKGDIV 277
Cdd:PRK02991 244 GYAVAGLRLKAQLAEQGIVvdadHPLFVYLPCGVGGGPGGVAFGLKLAFGD-HVHCFFAEPTHSPCMLlglMTGLHDQIS 322

                         90       100
                 ....*....|....*....|...
gi 505807461 278 --NVGGDMATIMAGLACGEPNPL 298
Cdd:PRK02991 323 vqDIGIDNLTAADGLAVGRASGF 345
PRK10717 PRK10717
cysteine synthase A; Provisional
 119-165 3.32e-03

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 39.07  E-value: 3.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 505807461 119 TDGNHGRGVAWAAQQLGQNAVVYMPKGSAQERVDAILRLGAECIVTD 165
Cdd:PRK10717  71 TAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVP 117
 
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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