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Conserved domains on  [gi|495596910|ref|WP_008321489|]
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MULTISPECIES: diaminopropionate ammonia-lyase [Citrobacter]

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) ...
 4-397 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: 626.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910    4 NLSFFINQTPF-TEHPNAPLapFSRQELVKALNFHRSIPGYAPTPLYTLPALAQKLGVKNIYLKDESQRFGLKAFKALGG 82
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSL--LSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   83 SYAMACHIAELVGKDISELPFDVMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNE 162
Cdd:TIGR03528  79 SYAIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  163 GATAEIVDMNYDDAVRMTAEQAEKYGWIVVQDTAWEGYEKIPQWIMQGYGTLMLEAIDQLHQVA---PTHIFVQAGVGSF 239
Cdd:TIGR03528 159 GAECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGvekPTHVFLQAGVGSF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  240 AGMVQGMVTAAWGENRPKVIVAEALIADCLYRSARSKEGDAIAVGGDLQTVMAGLACGEANSIGWKLLRDYANAFASCPD 319
Cdd:TIGR03528 239 AGAVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPD 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910  320 EVAALGMRMLGNPLAGDPQIISGESGAVTTGLLALLMTSPELAQTREQLGLDAHSRVLLVSTEGDTDPQQYLDIVWGG 397
Cdd:TIGR03528 319 WVAAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 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 ...
 4-397 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: 626.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910    4 NLSFFINQTPF-TEHPNAPLapFSRQELVKALNFHRSIPGYAPTPLYTLPALAQKLGVKNIYLKDESQRFGLKAFKALGG 82
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSL--LSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   83 SYAMACHIAELVGKDISELPFDVMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNE 162
Cdd:TIGR03528  79 SYAIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  163 GATAEIVDMNYDDAVRMTAEQAEKYGWIVVQDTAWEGYEKIPQWIMQGYGTLMLEAIDQLHQVA---PTHIFVQAGVGSF 239
Cdd:TIGR03528 159 GAECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGvekPTHVFLQAGVGSF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  240 AGMVQGMVTAAWGENRPKVIVAEALIADCLYRSARSKEGDAIAVGGDLQTVMAGLACGEANSIGWKLLRDYANAFASCPD 319
Cdd:TIGR03528 239 AGAVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPD 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910  320 EVAALGMRMLGNPLAGDPQIISGESGAVTTGLLALLMTSPELAQTREQLGLDAHSRVLLVSTEGDTDPQQYLDIVWGG 397
Cdd:TIGR03528 319 WVAAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 9-400 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 621.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   9 INQTPFTEHPNAPLapFSRQELVKALNFHRSIPGYAPTPLYTLPALAQKLGVKNIYLKDESQRFGLKAFKALGGSYAMAC 88
Cdd:PRK08206  10 IADNKPYDGADLPL--LSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALGGAYAVAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  89 HIAELVGKDISELPFDVMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEI 168
Cdd:PRK08206  88 LLAEKLGLDISELSFEELTSGEVREKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECII 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 169 VDMNYDDAVRMTAEQAEKYGWIVVQDTAWEGYEKIPQWIMQGYGTLMLEAIDQLHQ--VAPTHIFVQAGVGSFAGMVQGM 246
Cdd:PRK08206 168 TDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEmgVPPTHVFLQAGVGSLAGAVLGY 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 247 VTAAWGENRPKVIVAEALIADCLYRSARskEGDAIAVGGDLQTVMAGLACGEANSIGWKLLRDYANAFASCPDEVAALGM 326
Cdd:PRK08206 248 FAEVYGEQRPHFVVVEPDQADCLYQSAV--DGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGM 325

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495596910 327 RMLGNPLAGDPQIISGESGAVTTGLLALLMTSPELAQTREQLGLDAHSRVLLVSTEGDTDPQQYLDIVWGGQYP 400
Cdd:PRK08206 326 RILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA 399
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 21-397 2.89e-85

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: 262.67  E-value: 2.89e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  21 PLAPFSRQELVKALNFHRSIpgYAPTPLYTLPALAQKLGVkNIYLKDESQRFgLKAFKALGGSYAMACHiaelvgkdise 100
Cdd:COG1171    2 TALMPTLADIEAAAARIAGV--VRRTPLLRSPTLSERLGA-EVYLKLENLQP-TGSFKLRGAYNALASL----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 101 lpfdvmtSEEVRhdlqTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMT 180
Cdd:COG1171   67 -------SEEER----ARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 181 AEQAEKYGWIVVQDTAwegyekiPQWIMQGYGTLMLEAIDQLHQVapTHIFVQAGVGSFAGmvqGMVTAAWGEN-RPKVI 259
Cdd:COG1171  136 AELAEEEGATFVHPFD-------DPDVIAGQGTIALEILEQLPDL--DAVFVPVGGGGLIA---GVAAALKALSpDIRVI 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 260 VAEALIADCLYRSARSkeGDAIAVGGdLQTVMAGLACGEANSIGWKLLRDYANAFASCPDEVAALGMRMLGNPLAgdpqI 339
Cdd:COG1171  204 GVEPEGAAAMYRSLAA--GEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTK----I 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910 340 ISGESGAVTtglLALLMTSpelaqtREQLgldAHSRVLLVSTEGDTDPQQYLDIVWGG 397
Cdd:COG1171  277 VVEPAGAAA---LAALLAG------KERL---KGKRVVVVLSGGNIDPDRLAEILERG 322
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 41-382 4.21e-43

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: 152.46  E-value: 4.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   41 PGYAPTPLYTLPALAQKLGVkNIYLKDES-QRFGlkAFKALGGSYAMACHIAELvgkdiselpfdvmtseevrhdlQTVT 119
Cdd:pfam00291   3 LGIGPTPLVRLPRLSKELGV-DVYLKLESlNPTG--SFKDRGALNLLLRLKEGE----------------------GGKT 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  120 FATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKygwivvqdtaWEG 199
Cdd:pfam00291  58 VVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAE----------GPG 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  200 YEKIPQW----IMQGYGTLMLEAIDQLhQVAPTHIFVQAGVGS-FAGMVQGMvtaAWGENRPKVIVAEALIADCLYRSAR 274
Cdd:pfam00291 128 AYYINQYdnplNIEGYGTIGLEILEQL-GGDPDAVVVPVGGGGlIAGIARGL---KELGPDVRVIGVEPEGAPALARSLA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  275 SKEGDAIAVggdLQTVMAGLACGEANSIG-WKLLRDYANAFASCPDEVAALGMRMLGNpLAGdpqIISGESGAvtTGLLA 353
Cdd:pfam00291 204 AGRPVPVPV---ADTIADGLGVGDEPGALaLDLLDEYVGEVVTVSDEEALEAMRLLAR-REG---IVVEPSSA--AALAA 274

                         330       340
                  ....*....|....*....|....*....
gi 495596910  354 LLMtspelaqtREQLGLDAHSRVLLVSTE 382
Cdd:pfam00291 275 LKL--------ALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 46-268 2.05e-31

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: 119.54  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVkNIYLKDESQRFGLkAFKALGGSYAMACHIAELVGKDiselpfdvmtseevrhdlqtVTFATTTD 125
Cdd:cd00640    1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTG-SFKDRGALNLILLAEEEGKLPK--------------------GVIIESTG 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVqdtawegyekIPQ 205
Cdd:cd00640   59 GNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYY----------VNQ 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910 206 ----WIMQGYGTLMLEAIDQLHQVAPTHIFVQAGVGS-FAGMVQGMVTaawGENRPKVIVAEALIADC 268
Cdd:cd00640  129 fdnpANIAGQGTIGLEILEQLGGQKPDAVVVPVGGGGnIAGIARALKE---LLPNVKVIGVEPEVVTV 193
 
Name Accession Description Interval E-value
2_3_DAP_am_ly TIGR03528
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ...
 4-397 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: 626.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910    4 NLSFFINQTPF-TEHPNAPLapFSRQELVKALNFHRSIPGYAPTPLYTLPALAQKLGVKNIYLKDESQRFGLKAFKALGG 82
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSL--LSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   83 SYAMACHIAELVGKDISELPFDVMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNE 162
Cdd:TIGR03528  79 SYAIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  163 GATAEIVDMNYDDAVRMTAEQAEKYGWIVVQDTAWEGYEKIPQWIMQGYGTLMLEAIDQLHQVA---PTHIFVQAGVGSF 239
Cdd:TIGR03528 159 GAECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGvekPTHVFLQAGVGSF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  240 AGMVQGMVTAAWGENRPKVIVAEALIADCLYRSARSKEGDAIAVGGDLQTVMAGLACGEANSIGWKLLRDYANAFASCPD 319
Cdd:TIGR03528 239 AGAVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPD 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910  320 EVAALGMRMLGNPLAGDPQIISGESGAVTTGLLALLMTSPELAQTREQLGLDAHSRVLLVSTEGDTDPQQYLDIVWGG 397
Cdd:TIGR03528 319 WVAAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 9-400 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 621.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   9 INQTPFTEHPNAPLapFSRQELVKALNFHRSIPGYAPTPLYTLPALAQKLGVKNIYLKDESQRFGLKAFKALGGSYAMAC 88
Cdd:PRK08206  10 IADNKPYDGADLPL--LSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALGGAYAVAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  89 HIAELVGKDISELPFDVMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEI 168
Cdd:PRK08206  88 LLAEKLGLDISELSFEELTSGEVREKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECII 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 169 VDMNYDDAVRMTAEQAEKYGWIVVQDTAWEGYEKIPQWIMQGYGTLMLEAIDQLHQ--VAPTHIFVQAGVGSFAGMVQGM 246
Cdd:PRK08206 168 TDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEmgVPPTHVFLQAGVGSLAGAVLGY 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 247 VTAAWGENRPKVIVAEALIADCLYRSARskEGDAIAVGGDLQTVMAGLACGEANSIGWKLLRDYANAFASCPDEVAALGM 326
Cdd:PRK08206 248 FAEVYGEQRPHFVVVEPDQADCLYQSAV--DGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGM 325

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495596910 327 RMLGNPLAGDPQIISGESGAVTTGLLALLMTSPELAQTREQLGLDAHSRVLLVSTEGDTDPQQYLDIVWGGQYP 400
Cdd:PRK08206 326 RILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA 399
diampropi_NH3ly TIGR01747
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ...
 25-395 1.00e-178

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: 502.50  E-value: 1.00e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   25 FSRQELVKALNFHRSIPGYAPTPLYTLPALAQKLGVKNIYLKDESQRFGLKAFKALGGSYAMACHIAELVGKDISELPFD 104
Cdd:TIGR01747   2 FSQSQAKLALAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDIETLSFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  105 VMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQA 184
Cdd:TIGR01747  82 HLKNDAIGEKMGQATFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQMA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  185 EKYGWIVVQDTAWEGYEKIPQWIMQGYGTLMLEAIDQLHQ---VAPTHIFVQAGVGSFAGMVQGMVTAAWGENRPKVIVA 261
Cdd:TIGR01747 162 QQHGWVVVQDTAWEGYEKIPTWIMQGYATLADEAVEQLREmgsVTPTHVLLQAGVGSMAGGVLGYFVDVYSENNPHSIVV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  262 EALIADCLYRSARSKEGDAIAVGGDLQTVMAGLACGEANSIGWKLLRDYANAFASCPDEVAALGMRMLGNPLAGDPQIIS 341
Cdd:TIGR01747 242 EPDKADCLYQSAVKKDGDIVNVGGDMATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGGDPRIIS 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495596910  342 GESGAVTTGLLALLMTSPELAQTREQLGLDAHSRVLLVSTEGDTDPQQYLDIVW 395
Cdd:TIGR01747 322 GESGAVGLGLLAAVMYHPQYQSLMEKLQLDKDAVVLVISTEGDTDPDHYREIVW 375
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 21-397 2.89e-85

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: 262.67  E-value: 2.89e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  21 PLAPFSRQELVKALNFHRSIpgYAPTPLYTLPALAQKLGVkNIYLKDESQRFgLKAFKALGGSYAMACHiaelvgkdise 100
Cdd:COG1171    2 TALMPTLADIEAAAARIAGV--VRRTPLLRSPTLSERLGA-EVYLKLENLQP-TGSFKLRGAYNALASL----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 101 lpfdvmtSEEVRhdlqTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMT 180
Cdd:COG1171   67 -------SEEER----ARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 181 AEQAEKYGWIVVQDTAwegyekiPQWIMQGYGTLMLEAIDQLHQVapTHIFVQAGVGSFAGmvqGMVTAAWGEN-RPKVI 259
Cdd:COG1171  136 AELAEEEGATFVHPFD-------DPDVIAGQGTIALEILEQLPDL--DAVFVPVGGGGLIA---GVAAALKALSpDIRVI 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 260 VAEALIADCLYRSARSkeGDAIAVGGdLQTVMAGLACGEANSIGWKLLRDYANAFASCPDEVAALGMRMLGNPLAgdpqI 339
Cdd:COG1171  204 GVEPEGAAAMYRSLAA--GEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTK----I 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910 340 ISGESGAVTtglLALLMTSpelaqtREQLgldAHSRVLLVSTEGDTDPQQYLDIVWGG 397
Cdd:COG1171  277 VVEPAGAAA---LAALLAG------KERL---KGKRVVVVLSGGNIDPDRLAEILERG 322
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 41-382 4.21e-43

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: 152.46  E-value: 4.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   41 PGYAPTPLYTLPALAQKLGVkNIYLKDES-QRFGlkAFKALGGSYAMACHIAELvgkdiselpfdvmtseevrhdlQTVT 119
Cdd:pfam00291   3 LGIGPTPLVRLPRLSKELGV-DVYLKLESlNPTG--SFKDRGALNLLLRLKEGE----------------------GGKT 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  120 FATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKygwivvqdtaWEG 199
Cdd:pfam00291  58 VVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAE----------GPG 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  200 YEKIPQW----IMQGYGTLMLEAIDQLhQVAPTHIFVQAGVGS-FAGMVQGMvtaAWGENRPKVIVAEALIADCLYRSAR 274
Cdd:pfam00291 128 AYYINQYdnplNIEGYGTIGLEILEQL-GGDPDAVVVPVGGGGlIAGIARGL---KELGPDVRVIGVEPEGAPALARSLA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  275 SKEGDAIAVggdLQTVMAGLACGEANSIG-WKLLRDYANAFASCPDEVAALGMRMLGNpLAGdpqIISGESGAvtTGLLA 353
Cdd:pfam00291 204 AGRPVPVPV---ADTIADGLGVGDEPGALaLDLLDEYVGEVVTVSDEEALEAMRLLAR-REG---IVVEPSSA--AALAA 274

                         330       340
                  ....*....|....*....|....*....
gi 495596910  354 LLMtspelaqtREQLGLDAHSRVLLVSTE 382
Cdd:pfam00291 275 LKL--------ALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 46-268 2.05e-31

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: 119.54  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVkNIYLKDESQRFGLkAFKALGGSYAMACHIAELVGKDiselpfdvmtseevrhdlqtVTFATTTD 125
Cdd:cd00640    1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTG-SFKDRGALNLILLAEEEGKLPK--------------------GVIIESTG 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVqdtawegyekIPQ 205
Cdd:cd00640   59 GNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYY----------VNQ 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495596910 206 ----WIMQGYGTLMLEAIDQLHQVAPTHIFVQAGVGS-FAGMVQGMVTaawGENRPKVIVAEALIADC 268
Cdd:cd00640  129 fdnpANIAGQGTIGLEILEQLGGQKPDAVVVPVGGGGnIAGIARALKE---LLPNVKVIGVEPEVVTV 193
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 45-329 3.49e-24

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: 101.41  E-value: 3.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  45 PTPLYTLPALAQKLGVkNIYLKDES-QRFGlkAFKALGGSYAMAChiaelvgkdiselpfdvMTSEEVRHDLqtVTFatt 123
Cdd:cd01562   17 RTPLLTSPTLSELLGA-EVYLKCENlQKTG--SFKIRGAYNKLLS-----------------LSEEERAKGV--VAA--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 124 TDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVqdtawEGYEKi 203
Cdd:cd01562   72 SAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFI-----HPFDD- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 204 pQWIMQGYGTLMLEAIDQLhqVAPTHIFVQAGVGsfaGMVQGmVTAAWGENRP--KVIVAEALIADCLYRSARS------ 275
Cdd:cd01562  146 -PDVIAGQGTIGLEILEQV--PDLDAVFVPVGGG---GLIAG-IATAVKALSPntKVIGVEPEGAPAMAQSLAAgkpvtl 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495596910 276 KEGDAIAvggDlqtvmaGLACGEANSIGWKLLRDYANAFASCPDEVAALGMRML 329
Cdd:cd01562  219 PEVDTIA---D------GLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLL 263
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 46-381 7.12e-20

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: 89.57  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVKNIYLKDESQRFGLkAFKALGgsyaMACHIaelvgkdiselpfdvmtSEEVRHDLQTVTFATTtd 125
Cdd:cd01563   23 TPLVRAPRLGERLGGKNLYVKDEGLNPTG-SFKDRG----MTVAV-----------------SKAKELGVKAVACAST-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVqdTAWEGYEkipq 205
Cdd:cd01563   79 GNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS--NSLNPYR---- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 206 wiMQGYGTLMLEAIDQLHQVAPTHIFVQAGVGS-FAGMVQG---MVTAAWGENRPKVIVAEALIADCLYRSARSKEGDAI 281
Cdd:cd01563  153 --LEGQKTIAFEIAEQLGWEVPDYVVVPVGNGGnITAIWKGfkeLKELGLIDRLPRMVGVQAEGAAPIVRAFKEGKDDIE 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 282 AVgGDLQTVMAGLACGEANSI--GWKLLRDYANAFASCPDEVAALGMRMlgnpLAGDPQIISGESGAVT-TGLLALlmts 358
Cdd:cd01563  231 PV-ENPETIATAIRIGNPASGpkALRAVRESGGTAVAVSDEEILEAQKL----LARTEGIFVEPASAASlAGLKKL---- 301

                        330       340
                 ....*....|....*....|...
gi 495596910 359 pelaqtREQLGLDAHSRVLLVST 381
Cdd:cd01563  302 ------REEGIIDKGERVVVVLT 318
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 46-381 4.29e-16

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: 79.09  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGvKNIYLKDESQRFGLkAFKALGgsYAMACHIAelvgkdiselpfdvmtseeVRHDLQTVTFATTtd 125
Cdd:COG0498   67 TPLVKAPRLADELG-KNLYVKEEGHNPTG-SFKDRA--MQVAVSLA-------------------LERGAKTIVCASS-- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKG--SSQQRLTsIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVQDTAWegyeki 203
Cdd:COG0498  122 GNGSAALAAYAARAGIEVFVFVPEGkvSPGQLAQ-MLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINP------ 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 204 pqWIMQGYGTLMLEAIDQLHQVaPTHIFVqaGVGSFagmvqGMVTAAW-----------GENRPKVIVAEALIADCLYRS 272
Cdd:COG0498  195 --ARLEGQKTYAFEIAEQLGRV-PDWVVV--PTGNG-----GNILAGYkafkelkelglIDRLPRLIAVQATGCNPILTA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 273 ARSKEGDAIAVGGDlqTVMAGLACGeaNSIGW----KLLRDYANAFASCPDEVAALGMRMLGNpLAG---DPqiisgESG 345
Cdd:COG0498  265 FETGRDEYEPERPE--TIAPSMDIG--NPSNGeralFALRESGGTAVAVSDEEILEAIRLLAR-REGifvEP-----ATA 334

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 495596910 346 AVTTGLLALlmtspelaqtREQLGLDAHSRVLLVST 381
Cdd:COG0498  335 VAVAGLRKL----------REEGEIDPDEPVVVLST 360
eutB PRK07476
threonine dehydratase; Provisional
 38-261 1.23e-13

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 71.15  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  38 RSIPGYAP-TPLYTLPALAQKLGVKnIYLKDES-QRFGlkAFKALGGSYAMAChiaelvgkdiselpfdvMTSEEVRHDL 115
Cdd:PRK07476  11 RRIAGRVRrTPLVASASLSARAGVP-VWLKLETlQPTG--SFKLRGATNALLS-----------------LSAQERARGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 116 qtVTFATttdGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAvrmtaeQAEkygwiVVQDT 195
Cdd:PRK07476  71 --VTAST---GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDA------QAE-----VERLV 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495596910 196 AWEGYEKIPQW----IMQGYGTLMLEAIDQLHQVAptHIFVQ-AGVGSFAGmvqgmVTAAWGENRPKVIVA 261
Cdd:PRK07476 135 REEGLTMVPPFddprIIAGQGTIGLEILEALPDVA--TVLVPlSGGGLASG-----VAAAVKAIRPAIRVI 198
PRK06608 PRK06608
serine/threonine dehydratase;
19-274 2.44e-13

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 70.57  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  19 NAPLAPFsrQELVKAlnfHRSIPGYA-PTPLYTLPALAQKLGVKnIYLKDES-QRFGlkAFKALGgsyamAC-HIAELVg 95
Cdd:PRK06608   1 NLLLQNP--QNIAAA---HNRIKQYLhLTPIVHSESLNEMLGHE-IFFKVESlQKTG--AFKVRG-----VLnHLLELK- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  96 kdiselpfdvmtsEEVRHDLQTVTFATttdGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDmnydd 175
Cdd:PRK06608  67 -------------EQGKLPDKIVAYST---GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTN----- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 176 aVRMTAEQAEKYGwiVVQDTAWegyekIPQW----IMQGYGTLMLEAIDQLHqVAPTHIFVQAGVGsfaGMVQGMVTAAW 251
Cdd:PRK06608 126 -TRQEAEEKAKED--EEQGFYY-----IHPSdsdsTIAGAGTLCYEALQQLG-FSPDAIFASCGGG---GLISGTYLAKE 193

                        250       260
                 ....*....|....*....|....
gi 495596910 252 G-ENRPKVIVAEALIADCLYRSAR 274
Cdd:PRK06608 194 LiSPTSLLIGSEPLNANDAYLSLK 217
PRK08197 PRK08197
threonine synthase; Validated
 46-263 3.53e-12

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 67.33  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVKNIYLKDESqRFGLKAFKALGGsyAMACHIAELVGkdiselpfdvmtseeVRHdlqtvtFATTTD 125
Cdd:PRK08197  80 TPLLPLPRLGKALGIGRLWVKDEG-LNPTGSFKARGL--AVGVSRAKELG---------------VKH------LAMPTN 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVQdTAWEGYEkipq 205
Cdd:PRK08197 136 GNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVS-TLKEPYR---- 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495596910 206 wiMQGYGTLMLEAIDQLHQVAPTHIFVQAGVGSfaGMVqGMVTA-------AW-GENRPKVIVAEA 263
Cdd:PRK08197 211 --IEGKKTMGLELAEQLGWRLPDVILYPTGGGV--GLI-GIWKAfdelealGWiGGKRPRLVAVQA 271
PRK06381 PRK06381
threonine synthase; Validated
 46-261 1.74e-11

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 64.73  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVKNIYLKDEsqrfglkafkalgGSYAMACHiaelvgKD-ISElpfdVMTSEEVRHDLQTVTFATTt 124
Cdd:PRK06381  16 TPLLRARKLEEELGLRKIYLKFE-------------GANPTGTQ------KDrIAE----AHVRRAMRLGYSGITVGTC- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 125 dGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWivvqdtawegYEKIP 204
Cdd:PRK06381  72 -GNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI----------YDANP 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495596910 205 ----QWI-MQGYGTLMLEAIDQLHQVaPTHIFVQAGVGS-FAGMVQG---MVTAAWGENRPKVIVA 261
Cdd:PRK06381 141 gsvnSVVdIEAYSAIAYEIYEALGDV-PDAVAVPVGNGTtLAGIYHGfrrLYDRGKTSRMPRMIGV 205
PRK06815 PRK06815
threonine/serine dehydratase;
37-354 1.14e-10

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 62.40  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  37 HRSI-PGYAPTPLYTLPALAQKLGVkNIYLKDES-QRFGlkAFKALGGSYAMachiaelvgkdiselpfdVMTSEEVRHd 114
Cdd:PRK06815  11 HQRLrPQVRVTPLEHSPLLSQHTGC-EVYLKCEHlQHTG--SFKFRGASNKL------------------RLLNEAQRQ- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 115 lQTVtfATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVQD 194
Cdd:PRK06815  69 -QGV--ITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 195 tawegYEKiPQwIMQGYGTLMLEAIDQLHQvaPTHIFVQAGVGsfaGMVQGMVTA------------AWGENRPkvivae 262
Cdd:PRK06815 146 -----YND-PQ-VIAGQGTIGMELVEQQPD--LDAVFVAVGGG---GLISGIATYlktlspkteiigCWPANSP------ 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 263 aliadCLYRSArsKEGDAIAVgGDLQTVMAGLACG-EANSIGWKLLRDYANAFASCPDEVAALGMRMLgnpLAGDPQIIS 341
Cdd:PRK06815 208 -----SLYTSL--EAGEIVEV-AEQPTLSDGTAGGvEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLI---AETDRWLIE 276

                        330
                 ....*....|...
gi 495596910 342 GESGAVTTGLLAL 354
Cdd:PRK06815 277 GAAGVALAAALKL 289
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
46-277 2.38e-10

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 62.08  E-value: 2.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGvKNIYLKDESQR--FglkAFKaLGGSYAMachIAELvgkdiselpfdvmtSEEVRHdlQTVTFATT 123
Cdd:PRK09224  21 TPLEKAPKLSARLG-NQVLLKREDLQpvF---SFK-LRGAYNK---MAQL--------------TEEQLA--RGVITASA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 124 tdGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKygwivvqdtawEGYEKI 203
Cdd:PRK09224  77 --GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEE-----------EGLTFI 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 204 PQW----IMQGYGTLMLEaIDQLHQVAPTHIFVQAGVGsfaGMVQGmVTAAWGENRP--KVIVAEALIADCLYRSARSKE 277
Cdd:PRK09224 144 HPFddpdVIAGQGTIAME-ILQQHPHPLDAVFVPVGGG---GLIAG-VAAYIKQLRPeiKVIGVEPEDSACLKAALEAGE 218
PLN02550 PLN02550
threonine dehydratase
 46-258 2.56e-10

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 62.25  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVKnIYLKDESQR--FGLKafkaLGGSYAMachiaelvgkdISELPfdvmtseevRHDLQTVTFATT 123
Cdd:PLN02550 110 SPLQLAKKLSERLGVK-VLLKREDLQpvFSFK----LRGAYNM-----------MAKLP---------KEQLDKGVICSS 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 124 TdGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKygwivvqdtawEGYEKI 203
Cdd:PLN02550 165 A-GNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALE-----------EGRTFI 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 204 PQW----IMQGYGTLMLEAIDQLHqvAPTH-IFVQAGVGsfaGMVQGmVTAAWGENRPKV 258
Cdd:PLN02550 233 PPFdhpdVIAGQGTVGMEIVRQHQ--GPLHaIFVPVGGG---GLIAG-IAAYVKRVRPEV 286
PRK08246 PRK08246
serine/threonine dehydratase;
126-324 3.27e-10

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 60.74  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVQdtaweGYEKIPq 205
Cdd:PRK08246  77 GNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCH-----AYDQPE- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 206 wIMQGYGTLMLEAIDQLHQVAPthIFVQAGVGSFAGMVqgmvtAAWGENRPKVIVAEALIADCLYRsarskegdAIAVGG 285
Cdd:PRK08246 151 -VLAGAGTLGLEIEEQAPGVDT--VLVAVGGGGLIAGI-----AAWFEGRARVVAVEPEGAPTLHA--------ALAAGE 214

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495596910 286 DLQTVMAGLAcgeANSIGWKLLRDYANAFASCPDEVAAL 324
Cdd:PRK08246 215 PVDVPVSGIA---ADSLGARRVGEIAFALARAHVVTSVL 250
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 46-252 3.90e-10

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: 60.86  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   46 TPLYTLPALAQKLGVKNIYLKDESQRFGLkAFKALGGSYAMAcHIAELvGKDiselpfdvmtseevrhdlqTVTFATTtd 125
Cdd:TIGR00260  23 TPLFRAPALAANVGIKNLYVKELGHNPTL-SFKDRGMAVALT-KALEL-GND-------------------TVLCAST-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  126 GNHGRGVAWMARQLKQNAVVYMPKGS-SQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAE-KYGWIVVQDTAWEGYeki 203
Cdd:TIGR00260  79 GNTGAAAAAYAGKAGLKVVVLYPAGKiSLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEdKPALGLNSANSIPYR--- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 495596910  204 pqwiMQGYGTLMLEAIDQLHQVAPTHIFVQAGVGsfagmvqGMVTAAWG 252
Cdd:TIGR00260 156 ----LEGQKTYAFEAVEQLGWEAPDKVVVPVPNS-------GNFGAIWK 193
PRK08639 PRK08639
threonine dehydratase; Validated
 44-248 4.84e-10

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 60.98  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  44 APTPLYTLPALAQKLGVkNIYLKDES-QRfgLKAFKALGGSYAMachiaelvgkdiSELpfdvmtSEEVRHDlqtvTFAT 122
Cdd:PRK08639  24 PETPLQRNDYLSEKYGA-NVYLKREDlQP--VRSYKLRGAYNAI------------SQL------SDEELAA----GVVC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 123 TTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATA-EIV---DmNYDDAvrmtAEQAEKYgwivvqdTAWE 198
Cdd:PRK08639  79 ASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFvEIVlvgD-TFDDS----AAAAQEY-------AEET 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495596910 199 GYEKIPQW----IMQGYGTLMLEAIDQL-HQVAPTHIFVQAGVGsfaGMVQGMVT 248
Cdd:PRK08639 147 GATFIPPFddpdVIAGQGTVAVEILEQLeKEGSPDYVFVPVGGG---GLISGVTT 198
PRK08813 PRK08813
threonine dehydratase; Provisional
 12-274 2.16e-09

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 58.48  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  12 TPFTEHPNAPLAPFSRQELVKA-LNFHRSIPgyaPTPLYtlpaLAQKLGVkniYLKDES-QRFGlkAFKALGGSYAMach 89
Cdd:PRK08813   8 RPTVQEPDVGDVAVSVADVLAAqARLRRYLS---PTPLH----YAERFGV---WLKLENlQRTG--SYKVRGALNAL--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  90 iaeLVGKDiselpfdvmtseevRHDLQTVTFATTtdGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIV 169
Cdd:PRK08813  73 ---LAGLE--------------RGDERPVICASA--GNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQH 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 170 DMNYDDAVRMTAEQAEKYGWIVVqdTAWEGYEkipqwIMQGYGTLMLEaidqLHQVAPTHIFVQAGVGsfaGMVQGmVTA 249
Cdd:PRK08813 134 GNSYDEAYAFARELADQNGYRFL--SAFDDPD-----VIAGQGTVGIE----LAAHAPDVVIVPIGGG---GLASG-VAL 198

                        250       260
                 ....*....|....*....|....*
gi 495596910 250 AWGENRPKVIVAEALIADCLYRSAR 274
Cdd:PRK08813 199 ALKSQGVRVVGAQVEGVDSMARAIR 223
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 46-277 6.94e-09

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: 56.92  E-value: 6.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVkNIYLKDES-QRFGlkAFKALGgsyamachIAELVGKDISelpfdvmtseevRHDLQTVTFATTT 124
Cdd:cd06448    2 TPLIESTALSKTAGC-NVFLKLENlQPSG--SFKIRG--------IGHLCQKSAK------------QGLNECVHVVCSS 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 125 DGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQ--AEKYGWIVVQ----DTAWE 198
Cdd:cd06448   59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREElaENDPGPVYVHpfddPLIWE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 199 gyekipqwimqGYGTLMLEAIDQLH-QVAPTHIFVQAGVGS-FAGMVQGMVTAAWGenRPKVIVAEALIADCLYRSARSK 276
Cdd:cd06448  139 -----------GHSSMVDEIAQQLQsQEKVDAIVCSVGGGGlLNGIVQGLERNGWG--DIPVVAVETEGAHSLNASLKAG 205


                 .
gi 495596910 277 E 277
Cdd:cd06448  206 K 206
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
62-249 9.22e-08

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 53.59  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  62 NIYLKDES-QRFGlkAFKaLGGSYAMACHiaelvgkdiselpfdvMTSEEVRHDLqtvtfATTTDGNHGRGVAWMARQLK 140
Cdd:PRK08638  43 EIFLKLENmQRTG--SFK-IRGAFNKLSS----------------LTDAEKRKGV-----VACSAGNHAQGVALSCALLG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 141 QNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVQDtawegYEKiPQwIMQGYGTLMLEAID 220
Cdd:PRK08638  99 IDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPP-----YDD-PK-VIAGQGTIGLEILE 171

                        170       180
                 ....*....|....*....|....*....
gi 495596910 221 QLHQVapTHIFVQAGVGsfaGMVQGMVTA 249
Cdd:PRK08638 172 DLWDV--DTVIVPIGGG---GLIAGIAVA 195
PRK12483 PRK12483
threonine dehydratase; Reviewed
 46-277 1.16e-07

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 53.65  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGvKNIYLKDESQR--FGLKafkaLGGSYAMACHIaelvgkDISELPFDVMTSeevrhdlqtvtfatt 123
Cdd:PRK12483  38 TPLQRAPNLSARLG-NQVLLKREDLQpvFSFK----IRGAYNKMARL------PAEQLARGVITA--------------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 124 TDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKygwivvqdtawEGYEKI 203
Cdd:PRK12483  92 SAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEE-----------EGLTFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 204 PQW----IMQGYGTLMLEAIDQlHQVAPTHIFVQAGVGSFAGMVQGMVTAAwgenRP--KVIVAEALIADCLYRSARSKE 277
Cdd:PRK12483 161 PPFddpdVIAGQGTVAMEILRQ-HPGPLDAIFVPVGGGGLIAGIAAYVKYV----RPeiKVIGVEPDDSNCLQAALAAGE 235
PRK06110 PRK06110
threonine dehydratase;
25-192 4.05e-07

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 51.53  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  25 FSRQELVKALNF-HRSIPgyaPTPLYTLPALAQKLGVkNIYLKDESQRfGLKAFKALGGsyamachiaeLVgkdiselPF 103
Cdd:PRK06110   3 FTLAELEAAAAVvYAAMP---PTPQYRWPLLAERLGC-EVWVKHENHT-PTGAFKVRGG----------LV-------YF 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 104 DVMtseeVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGatAEIVDMNYD-DAVRMTAE 182
Cdd:PRK06110  61 DRL----ARRGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALG--AELIEHGEDfQAAREEAA 134

                        170
                 ....*....|.
gi 495596910 183 Q-AEKYGWIVV 192
Cdd:PRK06110 135 RlAAERGLHMV 145
THD1 TIGR02079
threonine dehydratase; This model represents threonine dehydratase, the first step in the ...
 45-248 1.10e-06

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: 50.52  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910   45 PTPLYTLPALAQKLGVkNIYLKDES-QRfgLKAFKALGGSYAMachiaelvgKDISElpfdvmtseevrHDLQTVtFATT 123
Cdd:TIGR02079  16 HTPLQLNERLSEKYGA-NIYLKREDlQP--VRSYKIRGAYNFL---------KQLSD------------AQLAKG-VVCA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  124 TDGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGatAEIVDM-----NYDDAVRMTAEQAEKygwivvqdtawE 198
Cdd:TIGR02079  71 SAGNHAQGFAYACRHLGVHGTVFMPATTPKQKIDRVKIFG--GEFIEIilvgdTFDQCAAAAREHVED-----------H 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495596910  199 GYEKIPQW----IMQGYGTLMLEAIDQLHQvAPTHIFVQAGVGsfaGMVQGMVT 248
Cdd:TIGR02079 138 GGTFIPPFddprIIEGQGTVAAEILDQLPE-KPDYVVVPVGGG---GLISGLTT 187
PRK07334 PRK07334
threonine dehydratase; Provisional
 126-387 4.04e-06

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 48.74  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 126 GNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAvRMTAEQ-AEKYGWIVVQ--DTAwegyek 202
Cdd:PRK07334  80 GNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEA-RAHARElAEEEGLTFVHpyDDP------ 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 203 ipqWIMQGYGTL---MLEA---IDQLhqVAPThifvqaGVGsfaGMVQGMVTAAWGENRP-KVIVAEALIADCLYRSARs 275
Cdd:PRK07334 153 ---AVIAGQGTValeMLEDapdLDTL--VVPI------GGG---GLISGMATAAKALKPDiEIIGVQTELYPSMYAAIK- 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 276 keGDAIAVGGDlqTVMAGLACGEANSIGWKLLRDYAnafascpDEVAALGMRMLGNPLAgdpQIISGE----SGAVTTGL 351
Cdd:PRK07334 218 --GVALPCGGS--TIAEGIAVKQPGQLTLEIVRRLV-------DDILLVSEADIEQAVS---LLLEIEktvvEGAGAAGL 283

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495596910 352 LALLmTSPELAQTReqlgldahsRVLLVSTEGDTDP 387
Cdd:PRK07334 284 AALL-AYPERFRGR---------KVGLVLSGGNIDT 309
D-Ser-dehyd cd06447
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 11-320 1.67e-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: 46.57  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  11 QTPFTEHPNAPLAPFSRQELVKAlnfHRSIPGYAP-----------------TPLYTLPALAQKLGVKN-------IYLK 66
Cdd:cd06447    4 KNPNYGKPAEALAPLSREDIFDA---EARLKRFAPyiakvfpetaashgiieSPLLPIPRMKQALEKLYhqpikgrLLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  67 DESQRFGLKAFKALGGSYAMACHIAELV---GKDISELPFDVMTSEEVRHDLQTVTFATTTDGNHGRGVAWMARQLKQNA 143
Cdd:cd06447   81 ADSHLPISGSIKARGGIYEVLKHAEKLAlehGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFKV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 144 VVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEK--YGWIVvQDtawegyEKIPQWIMqGYGTLMLEAIDQ 221
Cdd:cd06447  161 TVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAAdpMCYFV-DD------ENSRDLFL-GYAVAASRLKAQ 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 222 LHQVA-------PTHIFVQAGVGSFAGMVQGMVTAAWGENrPKVIVAEALIADCLYRSARSKEGDAIAV---GGDLQTVM 291
Cdd:cd06447  233 LAELGikvdaehPLFVYLPCGVGGAPGGVAFGLKLIFGDN-VHCFFAEPTHSPCMLLGMATGLHDKISVqdiGIDNRTAA 311

                        330       340
                 ....*....|....*....|....*....
gi 495596910 292 AGLACGEANSIGWKLLRDYANAFASCPDE 320
Cdd:cd06447  312 DGLAVGRPSGLVGKLMEPLLSGIYTVEDD 340
PLN02970 PLN02970
serine racemase
 46-392 1.94e-05

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 46.21  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910  46 TPLYTLPALAQKLGVKnIYLKDES-QRFGlkAFKALGGSYAMACHIAElvgkdisELPFDVMTseevrHdlqtvtfattT 124
Cdd:PLN02970  28 TPVLTSSSLDALAGRS-LFFKCECfQKGG--AFKFRGACNAIFSLSDD-------QAEKGVVT-----H----------S 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 125 DGNHGRGVAWMARQLKQNAVVYMPKGSSQQRLTSIRNEGATAEIVDMNYDDAVRMTAEQAEKYGWIVVQDtawegYEKIP 204
Cdd:PLN02970  83 SGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHP-----YNDGR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 205 qwIMQGYGTLMLEAIDQLHQVAPTHIFVQAGvgsfaGMVQGMVTAAWGENrP--KVIVAEALIADclyRSARSKEGDAIA 282
Cdd:PLN02970 158 --VISGQGTIALEFLEQVPELDVIIVPISGG-----GLISGIALAAKAIK-PsiKIIAAEPKGAD---DAAQSKAAGEII 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495596910 283 VGGDLQTVMAGLAcGEANSIGWKLLRDYANAFASCPDEVAALGMRMLGNPLagdpQIISGESGAVttGLLALLMTSPELA 362
Cdd:PLN02970 227 TLPVTNTIADGLR-ASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERL----KVVVEPSGAI--GLAAALSDSFRSN 299

                        330       340       350
                 ....*....|....*....|....*....|
gi 495596910 363 QTREqlgldAHSRVLLVSTEGDTDPQQYLD 392
Cdd:PLN02970 300 PAWK-----GCKNVGIVLSGGNVDLGVLWE 324
 
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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