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Conserved domains on  [gi|490304197|ref|WP_004199498|]
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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) ...
 4-400 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: 694.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197    4 IKFQLNARRQPYgQGADLSLLNESVGNEVLAFHQKFPDYRVTPLRKLEFLSQRLGLGSIHIKDEAQRFGLNAFKGLGGSY 83
Cdd:TIGR03528   2 IKIIINDNKKAT-NGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   84 AMGKYLAALLERDINTLSFAELNSPVIKARIKDIVFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGA 163
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  164 ECTITELNYDDTVRLAAKTAREQGWVLLQDTAWQGYEQIPTWIMQGYMTLAVEIWQQLAESGAPMPTHLFLQAGVGSFAG 243
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  244 SIMGYFIEKMQQQAPTIIIVEPHKANCLYRSATINDGLPHSVGGDMSTLMAGLACGEPNITSWPMLRDHATCFISADDCL 323
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304197  324 AANGMRLLAAPRPGtDEPFVSGESGAIGTGVLYALMTQPAYRELAESLRLNADAQVLLISTEGDTSPDVYEDIVWFG 400
Cdd:TIGR03528 321 AAKGMRILGNPLKG-DPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 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 ...
 4-400 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: 694.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197    4 IKFQLNARRQPYgQGADLSLLNESVGNEVLAFHQKFPDYRVTPLRKLEFLSQRLGLGSIHIKDEAQRFGLNAFKGLGGSY 83
Cdd:TIGR03528   2 IKIIINDNKKAT-NGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   84 AMGKYLAALLERDINTLSFAELNSPVIKARIKDIVFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGA 163
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  164 ECTITELNYDDTVRLAAKTAREQGWVLLQDTAWQGYEQIPTWIMQGYMTLAVEIWQQLAESGAPMPTHLFLQAGVGSFAG 243
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  244 SIMGYFIEKMQQQAPTIIIVEPHKANCLYRSATINDGLPHSVGGDMSTLMAGLACGEPNITSWPMLRDHATCFISADDCL 323
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304197  324 AANGMRLLAAPRPGtDEPFVSGESGAIGTGVLYALMTQPAYRELAESLRLNADAQVLLISTEGDTSPDVYEDIVWFG 400
Cdd:TIGR03528 321 AAKGMRILGNPLKG-DPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-401 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 680.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   1 MDTIKFQLNARRQPYGQGADLSLLNESVGNEVLAFHQKFPDYRVTPLRKLEFLSQRLGLGSIHIKDEAQRFGLNAFKGLG 80
Cdd:PRK08206   1 MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  81 GSYAMGKYLAALLERDINTLSFAELNSPVIKARIKDIVFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRR 160
Cdd:PRK08206  81 GAYAVARLLAEKLGLDISELSFEELTSGEVREKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 161 HGAECTITELNYDDTVRLAAKTAREQGWVLLQDTAWQGYEQIPTWIMQGYMTLAVEIWQQLAESGAPmPTHLFLQAGVGS 240
Cdd:PRK08206 161 LGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMGVP-PTHVFLQAGVGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 241 FAGSIMGYFIEKMQQQAPTIIIVEPHKANCLYRSATinDGLPHSVGGDMSTLMAGLACGEPNITSWPMLRDHATCFISAD 320
Cdd:PRK08206 240 LAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAV--DGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 321 DCLAANGMRLLAAPRPGtDEPFVSGESGAIGTGVLYALMTQPAYRELAESLRLNADAQVLLISTEGDTSPDVYEDIVWFG 400
Cdd:PRK08206 318 DEVAALGMRILANPLGG-DPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEG 396


                 .
gi 490304197 401 R 401
Cdd:PRK08206 397 K 397
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 42-398 4.30e-87

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: 267.29  E-value: 4.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  42 YRVTPLRKLEFLSQRLGlGSIHIKDEAQRFgLNAFKGLGGSYAMGKYLAALLERdintlsfaelnspvikarikdiVFVT 121
Cdd:COG1171   22 VRRTPLLRSPTLSERLG-AEVYLKLENLQP-TGSFKLRGAYNALASLSEEERAR----------------------GVVA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLQDTAwqgyeq 201
Cdd:COG1171   78 ASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFD------ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 202 iPTWIMQGYMTLAVEIWQQLAEsgapmPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPHKANCLYRSatINDGL 281
Cdd:COG1171  152 -DPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAAL--KALSPDIRVIGVEPEGAAAMYRS--LAAGE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 282 PHSVGGdMSTLMAGLACGEPNITSWPMLRDHATCFISADDCLAANGMRLLAaprpgTDEPFVSGESGAIGTGVLYalmtq 361
Cdd:COG1171  222 PVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLL-----ERTKIVVEPAGAAALAALL----- 290

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 490304197 362 pAYRELAeslrlnADAQVLLISTEGDTSPDVYEDIVW 398
Cdd:COG1171  291 -AGKERL------KGKRVVVVLSGGNIDPDRLAEILE 320
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 39-385 1.21e-46

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: 161.71  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   39 FPDYRVTPLRKLEFLSQRLGlGSIHIKDE-AQRFGlnAFKGLGGSYAMGKylaallerdintlsfaelnspvIKARIKDI 117
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELG-VDVYLKLEsLNPTG--SFKDRGALNLLLR----------------------LKEGEGGK 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  118 VFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTARE-QGWVLLQDTAw 196
Cdd:pfam00291  57 TVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYD- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  197 qgyeqiPTWIMQGYMTLAVEIWQQLaesgAPMPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPHKANCLYRSAT 276
Cdd:pfam00291 136 ------NPLNIEGYGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGL--KELGPDVRVIGVEPEGAPALARSLA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  277 INDGLPHSVggdMSTLMAGLACG-EPNITSWPMLRDHATCFISADDCLAANGMRLLAaprpgTDEPFVSGESGAIGtgvL 355
Cdd:pfam00291 204 AGRPVPVPV---ADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLA-----RREGIVVEPSSAAA---L 272

                         330       340       350
                  ....*....|....*....|....*....|
gi 490304197  356 YALmtqpayrELAESLRLNADAQVLLISTE 385
Cdd:pfam00291 273 AAL-------KLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 45-266 8.48e-35

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: 128.79  E-value: 8.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  45 TPLRKLEFLSQRLGlGSIHIKDEaqrfGLN---AFKGLGGSYAMGKYLAallerdintlsfaelnspviKARIKDIVFVT 121
Cdd:cd00640    1 TPLVRLKRLSKLGG-ANIYLKLE----FLNptgSFKDRGALNLILLAEE--------------------EGKLPKGVIIE 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQ-GWVLLQDTawqgye 200
Cdd:cd00640   56 STGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQF------ 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304197 201 qIPTWIMQGYMTLAVEIWQQLAEsgaPMPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPH 266
Cdd:cd00640  130 -DNPANIAGQGTIGLEILEQLGG---QKPDAVVVPVGGGGNIAGIARAL--KELLPNVKVIGVEPE 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 ...
 4-400 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: 694.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197    4 IKFQLNARRQPYgQGADLSLLNESVGNEVLAFHQKFPDYRVTPLRKLEFLSQRLGLGSIHIKDEAQRFGLNAFKGLGGSY 83
Cdd:TIGR03528   2 IKIIINDNKKAT-NGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   84 AMGKYLAALLERDINTLSFAELNSPVIKARIKDIVFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGA 163
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNEIREKLGDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  164 ECTITELNYDDTVRLAAKTAREQGWVLLQDTAWQGYEQIPTWIMQGYMTLAVEIWQQLAESGAPMPTHLFLQAGVGSFAG 243
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  244 SIMGYFIEKMQQQAPTIIIVEPHKANCLYRSATINDGLPHSVGGDMSTLMAGLACGEPNITSWPMLRDHATCFISADDCL 323
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIADDGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304197  324 AANGMRLLAAPRPGtDEPFVSGESGAIGTGVLYALMTQPAYRELAESLRLNADAQVLLISTEGDTSPDVYEDIVWFG 400
Cdd:TIGR03528 321 AAKGMRILGNPLKG-DPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-401 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 680.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   1 MDTIKFQLNARRQPYGQGADLSLLNESVGNEVLAFHQKFPDYRVTPLRKLEFLSQRLGLGSIHIKDEAQRFGLNAFKGLG 80
Cdd:PRK08206   1 MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  81 GSYAMGKYLAALLERDINTLSFAELNSPVIKARIKDIVFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRR 160
Cdd:PRK08206  81 GAYAVARLLAEKLGLDISELSFEELTSGEVREKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 161 HGAECTITELNYDDTVRLAAKTAREQGWVLLQDTAWQGYEQIPTWIMQGYMTLAVEIWQQLAESGAPmPTHLFLQAGVGS 240
Cdd:PRK08206 161 LGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMGVP-PTHVFLQAGVGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 241 FAGSIMGYFIEKMQQQAPTIIIVEPHKANCLYRSATinDGLPHSVGGDMSTLMAGLACGEPNITSWPMLRDHATCFISAD 320
Cdd:PRK08206 240 LAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAV--DGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 321 DCLAANGMRLLAAPRPGtDEPFVSGESGAIGTGVLYALMTQPAYRELAESLRLNADAQVLLISTEGDTSPDVYEDIVWFG 400
Cdd:PRK08206 318 DEVAALGMRILANPLGG-DPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEG 396


                 .
gi 490304197 401 R 401
Cdd:PRK08206 397 K 397
diampropi_NH3ly TIGR01747
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ...
 23-398 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: 620.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   23 LLNESVGNEVLAFHQKFPDYRVTPLRKLEFLSQRLGLGSIHIKDEAQRFGLNAFKGLGGSYAMGKYLAALLERDINTLSF 102
Cdd:TIGR01747   1 LFSQSQAKLALAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDIETLSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  103 AELNSPVIKARIKDIVFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKT 182
Cdd:TIGR01747  81 EHLKNDAIGEKMGQATFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  183 AREQGWVLLQDTAWQGYEQIPTWIMQGYMTLAVEIWQQLAESGAPMPTHLFLQAGVGSFAGSIMGYFIEKMQQQAPTIII 262
Cdd:TIGR01747 161 AQQHGWVVVQDTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHVLLQAGVGSMAGGVLGYFVDVYSENNPHSIV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  263 VEPHKANCLYRSATINDGLPHSVGGDMSTLMAGLACGEPNITSWPMLRDHATCFISADDCLAANGMRLLAAPRPGtDEPF 342
Cdd:TIGR01747 241 VEPDKADCLYQSAVKKDGDIVNVGGDMATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGG-DPRI 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490304197  343 VSGESGAIGTGVLYALMTQPAYRELAESLRLNADAQVLLISTEGDTSPDVYEDIVW 398
Cdd:TIGR01747 320 ISGESGAVGLGLLAAVMYHPQYQSLMEKLQLDKDAVVLVISTEGDTDPDHYREIVW 375
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 42-398 4.30e-87

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: 267.29  E-value: 4.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  42 YRVTPLRKLEFLSQRLGlGSIHIKDEAQRFgLNAFKGLGGSYAMGKYLAALLERdintlsfaelnspvikarikdiVFVT 121
Cdd:COG1171   22 VRRTPLLRSPTLSERLG-AEVYLKLENLQP-TGSFKLRGAYNALASLSEEERAR----------------------GVVA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLQDTAwqgyeq 201
Cdd:COG1171   78 ASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFD------ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 202 iPTWIMQGYMTLAVEIWQQLAEsgapmPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPHKANCLYRSatINDGL 281
Cdd:COG1171  152 -DPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAAL--KALSPDIRVIGVEPEGAAAMYRS--LAAGE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 282 PHSVGGdMSTLMAGLACGEPNITSWPMLRDHATCFISADDCLAANGMRLLAaprpgTDEPFVSGESGAIGTGVLYalmtq 361
Cdd:COG1171  222 PVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLL-----ERTKIVVEPAGAAALAALL----- 290

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 490304197 362 pAYRELAeslrlnADAQVLLISTEGDTSPDVYEDIVW 398
Cdd:COG1171  291 -AGKERL------KGKRVVVVLSGGNIDPDRLAEILE 320
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 39-385 1.21e-46

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: 161.71  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   39 FPDYRVTPLRKLEFLSQRLGlGSIHIKDE-AQRFGlnAFKGLGGSYAMGKylaallerdintlsfaelnspvIKARIKDI 117
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELG-VDVYLKLEsLNPTG--SFKDRGALNLLLR----------------------LKEGEGGK 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  118 VFVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTARE-QGWVLLQDTAw 196
Cdd:pfam00291  57 TVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYD- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  197 qgyeqiPTWIMQGYMTLAVEIWQQLaesgAPMPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPHKANCLYRSAT 276
Cdd:pfam00291 136 ------NPLNIEGYGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGL--KELGPDVRVIGVEPEGAPALARSLA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  277 INDGLPHSVggdMSTLMAGLACG-EPNITSWPMLRDHATCFISADDCLAANGMRLLAaprpgTDEPFVSGESGAIGtgvL 355
Cdd:pfam00291 204 AGRPVPVPV---ADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLA-----RREGIVVEPSSAAA---L 272

                         330       340       350
                  ....*....|....*....|....*....|
gi 490304197  356 YALmtqpayrELAESLRLNADAQVLLISTE 385
Cdd:pfam00291 273 AAL-------KLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 45-266 8.48e-35

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: 128.79  E-value: 8.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  45 TPLRKLEFLSQRLGlGSIHIKDEaqrfGLN---AFKGLGGSYAMGKYLAallerdintlsfaelnspviKARIKDIVFVT 121
Cdd:cd00640    1 TPLVRLKRLSKLGG-ANIYLKLE----FLNptgSFKDRGALNLILLAEE--------------------EGKLPKGVIIE 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQ-GWVLLQDTawqgye 200
Cdd:cd00640   56 STGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQF------ 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304197 201 qIPTWIMQGYMTLAVEIWQQLAEsgaPMPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPH 266
Cdd:cd00640  130 -DNPANIAGQGTIGLEILEQLGG---QKPDAVVVPVGGGGNIAGIARAL--KELLPNVKVIGVEPE 189
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 43-332 4.29e-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: 112.20  E-value: 4.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  43 RVTPLRKLEFLSQRLGlGSIHIKDEA-QRFGlnAFKGLGGSYAMgkylAALLErdintlsfAELNSPVIkarikdivfvT 121
Cdd:cd01562   16 RRTPLLTSPTLSELLG-AEVYLKCENlQKTG--SFKIRGAYNKL----LSLSE--------EERAKGVV----------A 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLqdtawQGYEQ 201
Cdd:cd01562   71 ASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFI-----HPFDD 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 202 IptWIMQGYMTLAVEIWQQlaesgAPMPTHLFLQAGVGSFAGSIMGYFiekmQQQAPTI-II-VEPHKANCLYRSatIND 279
Cdd:cd01562  146 P--DVIAGQGTIGLEILEQ-----VPDLDAVFVPVGGGGLIAGIATAV----KALSPNTkVIgVEPEGAPAMAQS--LAA 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490304197 280 GLPHSVgGDMSTLMAGLACGEPNITSWPMLRDHATCFISADDCLAANGMRLLA 332
Cdd:cd01562  213 GKPVTL-PEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLF 264
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 45-384 1.17e-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: 91.89  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  45 TPLRKLEFLSQRLGLGSIHIKDEaqrfGLN---AFKGLGGSYAMGKylaaLLERDINTlsfaelnspvikarikdivFVT 121
Cdd:cd01563   23 TPLVRAPRLGERLGGKNLYVKDE----GLNptgSFKDRGMTVAVSK----AKELGVKA-------------------VAC 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLQdtawqgyeQ 201
Cdd:cd01563   76 ASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSN--------S 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 202 IPTWIMQGYMTLAVEIWQQLaesGAPMPTHLFLQAGVGS-FAGSIMGY-------FIEKMqqqaPTIIIVEPHKANCLYR 273
Cdd:cd01563  148 LNPYRLEGQKTIAFEIAEQL---GWEVPDYVVVPVGNGGnITAIWKGFkelkelgLIDRL----PRMVGVQAEGAAPIVR 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 274 SATINDGLPHSVgGDMSTLMAGLACGEPniTSWP----MLRDHATCFISADD--CLAAngMRLLAaprpGTDEPFVSGES 347
Cdd:cd01563  221 AFKEGKDDIEPV-ENPETIATAIRIGNP--ASGPkalrAVRESGGTAVAVSDeeILEA--QKLLA----RTEGIFVEPAS 291

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 490304197 348 GAigtgvlyalmTQPAYRELAESLRLNADAQVLLIST 384
Cdd:cd01563  292 AA----------SLAGLKKLREEGIIDKGERVVVVLT 318
PRK06815 PRK06815
threonine/serine dehydratase;
30-365 1.89e-20

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 90.91  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  30 NEVLAFHQKF-PDYRVTPLRKLEFLSQRLGlGSIHIKDE-AQRFGlnAFKGLGGSYAMGKYLAALLERDIntlsfaelns 107
Cdd:PRK06815   5 DAILEAHQRLrPQVRVTPLEHSPLLSQHTG-CEVYLKCEhLQHTG--SFKFRGASNKLRLLNEAQRQQGV---------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 108 pvikarikdivfVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQG 187
Cdd:PRK06815  72 ------------ITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 188 WVL------LQDTAWQGyeqiptwimqgymTLAVEIWQQlaesgAPMPTHLFLQAGVGSFAGSIMGYFieKMQQQAPTII 261
Cdd:PRK06815 140 KVYispyndPQVIAGQG-------------TIGMELVEQ-----QPDLDAVFVAVGGGGLISGIATYL--KTLSPKTEII 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 262 IVEPHKANCLYRSATINDGLPHSVggdMSTLMAGLACG-EPNITSWPMLRD--HATCFISADDCLAAngMRLLAAprpgT 338
Cdd:PRK06815 200 GCWPANSPSLYTSLEAGEIVEVAE---QPTLSDGTAGGvEPGAITFPLCQQliDQKVLVSEEEIKEA--MRLIAE----T 270

                        330       340
                 ....*....|....*....|....*..
gi 490304197 339 DEPFVsgeSGAIGTGVLYALMTQPAYR 365
Cdd:PRK06815 271 DRWLI---EGAAGVALAAALKLAPRYQ 294
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
43-274 1.57e-17

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 84.03  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  43 RVTPLRKLEFLSQRLGlGSIHIKDEAQR--FglnAFKgLGGSYAMgkylaallerdINTLSFAELNSPVIkarikdivfv 120
Cdd:PRK09224  19 QETPLEKAPKLSARLG-NQVLLKREDLQpvF---SFK-LRGAYNK-----------MAQLTEEQLARGVI---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 121 TATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLQ--D----T 194
Cdd:PRK09224  73 TASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHpfDdpdvI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 195 AWQGyeqiptwimqgymTLAVEIWQQLAESgapmPTHLFLQAGVGSFAGSIMGYfiekMQQQAPTI-II-VEPHKANCLY 272
Cdd:PRK09224 153 AGQG-------------TIAMEILQQHPHP----LDAVFVPVGGGGLIAGVAAY----IKQLRPEIkVIgVEPEDSACLK 211


                 ..
gi 490304197 273 RS 274
Cdd:PRK09224 212 AA 213
PRK06608 PRK06608
serine/threonine dehydratase;
31-281 3.44e-16

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 79.04  E-value: 3.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  31 EVLAFHQKFPDY-RVTPLRKLEFLSQRLGlGSIHIKDEA-QRFGlnAFKGLGGsyamgkylaallerdINTLSFAELNsp 108
Cdd:PRK06608   9 NIAAAHNRIKQYlHLTPIVHSESLNEMLG-HEIFFKVESlQKTG--AFKVRGV---------------LNHLLELKEQ-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 109 viKARIKDIVfvTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITelNYDDTVRLAAKTAREQGw 188
Cdd:PRK06608  69 --GKLPDKIV--AYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT--NTRQEAEEKAKEDEEQG- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 189 vllqdTAWqgyeqIPTW----IMQGYMTLAVEIWQQLAESgapmPTHLFLQAGVGsfaGSIMGYFIEKMQQQAPTIII-V 263
Cdd:PRK06608 142 -----FYY-----IHPSdsdsTIAGAGTLCYEALQQLGFS----PDAIFASCGGG---GLISGTYLAKELISPTSLLIgS 204

                        250       260       270
                 ....*....|....*....|....*....|.
gi 490304197 264 EPHKANCLYRSA-------------TINDGL 281
Cdd:PRK06608 205 EPLNANDAYLSLknnkiyrlnyspnTIADGL 235
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 44-384 1.09e-15

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: 77.93  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  44 VTPLRKLEFLSQRLGlGSIHIKDEaqrfGLN---AFKglggsyAMGKYLA--ALLERDINTLsfaelnspvikarikdiv 118
Cdd:COG0498   66 GTPLVKAPRLADELG-KNLYVKEE----GHNptgSFK------DRAMQVAvsLALERGAKTI------------------ 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 119 fVTATDGNHGRGVAWAAEQLGLRAVVYMPKGS-SPV-RAQnIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLQDTAW 196
Cdd:COG0498  117 -VCASSGNGSAALAAYAARAGIEVFVFVPEGKvSPGqLAQ-MLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINP 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 197 qgyeqiptWIMQGYMTLAVEIWQQLAEsgapMPTHLFLqaGVGSFAGSIMGY----------FIEKMqqqaPTIIIVEPH 266
Cdd:COG0498  195 --------ARLEGQKTYAFEIAEQLGR----VPDWVVV--PTGNGGNILAGYkafkelkelgLIDRL----PRLIAVQAT 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 267 KANCLYRSATINDGLPHSVGGDmsTLMAGLACGEPniTSWPMLRDHAT----CFISADDCLAANGMRLLAApRPGTD-EP 341
Cdd:COG0498  257 GCNPILTAFETGRDEYEPERPE--TIAPSMDIGNP--SNGERALFALResggTAVAVSDEEILEAIRLLAR-REGIFvEP 331

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 490304197 342 fvsgeSGAIGtgvlYAlmtqpAYRELAESLRLNADAQVLLIST 384
Cdd:COG0498  332 -----ATAVA----VA-----GLRKLREEGEIDPDEPVVVLST 360
PRK08246 PRK08246
serine/threonine dehydratase;
120-274 9.73e-15

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 74.22  E-value: 9.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 120 VTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLqdtawQGY 199
Cdd:PRK08246  72 VAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLC-----HAY 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304197 200 EQIPTWIMQGymTLAVEIWQQlaesgAPMPTHLFLQAGVGSFAGSIMGYFiekmqQQAPTIIIVEPHKANCLYRS 274
Cdd:PRK08246 147 DQPEVLAGAG--TLGLEIEEQ-----APGVDTVLVAVGGGGLIAGIAAWF-----EGRARVVAVEPEGAPTLHAA 209
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 122-284 7.67e-14

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: 71.62  E-value: 7.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTIT--ELNYDDTVRLAAKTAREQ-GWVLLQD----- 193
Cdd:COG0031   70 ATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTpgAEGMKGAIDKAEELAAETpGAFWPNQfenpa 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 194 --TAWqgyeqiptwimqgYMTLAVEIWQQLAESgapmPTHLFlqAGVGSfAGSIMG---YFieKMQQQAPTIIIVEPhka 268
Cdd:COG0031  150 npEAH-------------YETTGPEIWEQTDGK----VDAFV--AGVGT-GGTITGvgrYL--KERNPDIKIVAVEP--- 204

                        170
                 ....*....|....*.
gi 490304197 269 nclYRSATINDGLPHS 284
Cdd:COG0031  205 ---EGSPLLSGGEPGP 217
PRK08639 PRK08639
threonine dehydratase; Validated
 45-274 1.58e-12

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 68.68  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  45 TPLRKLEFLSQRLGLgSIHIKDE-AQRfgLNAFKGLGGSYAMGKylaallerdintLSFAELNSpvikarikdiVFVTAT 123
Cdd:PRK08639  26 TPLQRNDYLSEKYGA-NVYLKREdLQP--VRSYKLRGAYNAISQ------------LSDEELAA----------GVVCAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 124 DGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITEL---NYDDtvrlAAKTAREqgwvllqDTAWQGYE 200
Cdd:PRK08639  81 AGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVEIVLvgdTFDD----SAAAAQE-------YAEETGAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 201 QIPTW----IMQGYMTLAVEIWQQLAEsgAPMPTHLFLQAGVGSFAGSIMGYFiekmQQQAPT--IIIVEPHKANCLYRS 274
Cdd:PRK08639 150 FIPPFddpdVIAGQGTVAVEILEQLEK--EGSPDYVFVPVGGGGLISGVTTYL----KERSPKtkIIGVEPAGAASMKAA 223
PRK12483 PRK12483
threonine dehydratase; Reviewed
 43-274 2.19e-12

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 68.28  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  43 RVTPLRKLEFLSQRLGlGSIHIKDEAQRfGLNAFKGLGGSYAMGKYLAALLERDIntlsfaelnspvikarikdivfVTA 122
Cdd:PRK12483  36 RETPLQRAPNLSARLG-NQVLLKREDLQ-PVFSFKIRGAYNKMARLPAEQLARGV----------------------ITA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 123 TDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLlqdtawqgyeqI 202
Cdd:PRK12483  92 SAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTF-----------V 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304197 203 PTW----IMQGYMTLAVEIWQQlaesgAPMPTH-LFLQAGVGSFAGSIMGYFieKMQQQAPTIIIVEPHKANCLYRS 274
Cdd:PRK12483 161 PPFddpdVIAGQGTVAMEILRQ-----HPGPLDaIFVPVGGGGLIAGIAAYV--KYVRPEIKVIGVEPDDSNCLQAA 230
THD1 TIGR02079
threonine dehydratase; This model represents threonine dehydratase, the first step in the ...
 45-274 2.43e-12

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: 67.85  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197   45 TPLRKLEFLSQRLGlGSIHIKDE-AQRfgLNAFKGLGGSYAMgkylaallerdiNTLSFAELnspvikarikDIVFVTAT 123
Cdd:TIGR02079  17 TPLQLNERLSEKYG-ANIYLKREdLQP--VRSYKIRGAYNFL------------KQLSDAQL----------AKGVVCAS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  124 DGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAEcTITELNYDDTVRLAAKTAREqgwvllqDTAWQGYEQIP 203
Cdd:TIGR02079  72 AGNHAQGFAYACRHLGVHGTVFMPATTPKQKIDRVKIFGGE-FIEIILVGDTFDQCAAAARE-------HVEDHGGTFIP 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304197  204 TW----IMQGYMTLAVEIWQQLAESgapmPTHLFLQAGVGSFAGSIMGYFIEKMQQQAptIIIVEPHKANCLYRS 274
Cdd:TIGR02079 144 PFddprIIEGQGTVAAEILDQLPEK----PDYVVVPVGGGGLISGLTTYLAGTSPKTK--IIGVEPEGAPSMKAS 212
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 120-284 5.78e-12

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: 66.00  E-value: 5.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 120 VTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITE----LNYDDTVRLAAKTAREQ-GWVLLQ-- 192
Cdd:cd01561   57 IEPTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPeaeaDGMKGAIAKARELAAETpNAFWLNqf 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 193 -DTA-WQGYeqiptwimqgYMTLAVEIWQQLAEsgapMPTHLFlqAGVGSfAGSIMGyFIEKMQQQAP--TIIIVEPhka 268
Cdd:cd01561  137 eNPAnPEAH----------YETTAPEIWEQLDG----KVDAFV--AGVGT-GGTITG-VARYLKEKNPnvRIVGVDP--- 195

                        170
                 ....*....|....*.
gi 490304197 269 nclYRSATINDGLPHS 284
Cdd:cd01561  196 ---VGSVLFSGGPPGP 208
PRK06381 PRK06381
threonine synthase; Validated
 121-248 9.47e-12

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 65.50  E-value: 9.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 121 TATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWvllqdtawqgYE 200
Cdd:PRK06381  68 VGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI----------YD 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490304197 201 QIP----TWI-MQGYMTLAVEIWQQLAESgapmPTHLFLQAGVGS-FAGSIMGY 248
Cdd:PRK06381 138 ANPgsvnSVVdIEAYSAIAYEIYEALGDV----PDAVAVPVGNGTtLAGIYHGF 187
eutB PRK07476
threonine dehydratase; Provisional
 43-223 1.36e-11

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 64.99  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  43 RVTPLRKLEFLSQRLGLgSIHIKDEA-QRFGlnAFKGLGGSYAMGKYLAALLERDIntlsfaelnspvikarikdivfVT 121
Cdd:PRK07476  18 RRTPLVASASLSARAGV-PVWLKLETlQPTG--SFKLRGATNALLSLSAQERARGV----------------------VT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMpkgSSPV---RAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLlqdtawqg 198
Cdd:PRK07476  73 ASTGNHGRALAYAARALGIRATICM---SRLVpanKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTM-------- 141

                        170       180
                 ....*....|....*....|....*....
gi 490304197 199 yeqIPTW----IMQGYMTLAVEIWQQLAE 223
Cdd:PRK07476 142 ---VPPFddprIIAGQGTIGLEILEALPD 167
PLN02550 PLN02550
threonine dehydratase
 45-274 1.06e-10

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 63.40  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  45 TPLRKLEFLSQRLGLGSIHIKDEAQRfgLNAFKgLGGSYAMgkylAALLERDintlsfaELNSPVIkarikdivfvTATD 124
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQP--VFSFK-LRGAYNM----MAKLPKE-------QLDKGVI----------CSSA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 125 GNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLlqdtawqgyeqIPT 204
Cdd:PLN02550 166 GNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTF-----------IPP 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304197 205 W----IMQGYMTLAVEIWQQLaesgaPMPTH-LFLQAGVGSFAGSIMGYfiekMQQQAP--TIIIVEPHKANCLYRS 274
Cdd:PLN02550 235 FdhpdVIAGQGTVGMEIVRQH-----QGPLHaIFVPVGGGGLIAGIAAY----VKRVRPevKIIGVEPSDANAMALS 302
PLN02970 PLN02970
serine racemase
 10-351 3.59e-10

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 60.85  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  10 ARRQPYGqgADLSLLNESvgnevlafHQKFPDY-RVTPLRKLEFLSQRLGLgSIHIKDEA-QRFGlnAFKGLGGSYAmgk 87
Cdd:PLN02970   2 AASEKYA--ADLSSIREA--------RKRIAPFiHRTPVLTSSSLDALAGR-SLFFKCECfQKGG--AFKFRGACNA--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  88 ylaallerdINTLSFAELNSPVikarikdivfVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTI 167
Cdd:PLN02970  66 ---------IFSLSDDQAEKGV----------VTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITW 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 168 TELNYDDTVRLAAKTAREQGWVLLQDtawqgYEQIPtwIMQGYMTLAVEIWQQLAE--------SGAPMpthlflQAGVG 239
Cdd:PLN02970 127 CEPTVESREAVAARVQQETGAVLIHP-----YNDGR--VISGQGTIALEFLEQVPEldviivpiSGGGL------ISGIA 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 240 SFAGSImgyfiekmqqqAPTIIIV--EPHKANCLYRSA------------TINDGLPHSVgGDMstlmaglacgepnitS 305
Cdd:PLN02970 194 LAAKAI-----------KPSIKIIaaEPKGADDAAQSKaageiitlpvtnTIADGLRASL-GDL---------------T 246

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 490304197 306 WPMLRDHATCFISADDCLAANGMRLLAAPRPGTDEPfvsgeSGAIG 351
Cdd:PLN02970 247 WPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEP-----SGAIG 287
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
43-221 3.78e-10

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 60.90  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  43 RVTPLRKLEFLSQRLGlGSIHIKDE-AQRFGLNAFKGlggsyAMGKylaallerdINTLSFAELNSPVIkarikdivfvT 121
Cdd:PRK08638  26 RKTPLPRSNYLSERCK-GEIFLKLEnMQRTGSFKIRG-----AFNK---------LSSLTDAEKRKGVV----------A 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLlqdtawqgyeq 201
Cdd:PRK08638  81 CSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTF----------- 149

                        170       180
                 ....*....|....*....|....
gi 490304197 202 IPTW----IMQGYMTLAVEIWQQL 221
Cdd:PRK08638 150 IPPYddpkVIAGQGTIGLEILEDL 173
PRK06110 PRK06110
threonine dehydratase;
120-331 5.52e-10

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 60.01  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 120 VTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLlqdtawqgy 199
Cdd:PRK06110  74 ISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHM--------- 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 200 eqIPT---WIMQGYMTLAVEiwqqLAESGAPMPThLFLQAGVGS-FAGSI-----MGYFIEkmqqqaptIIIVEPHKANC 270
Cdd:PRK06110 145 --VPSfhpDLVRGVATYALE----LFRAVPDLDV-VYVPIGMGSgICGAIaardaLGLKTR--------IVGVVSAHAPA 209

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304197 271 LYRSATINdglpHSVGGDMSTLMA-GLACGEPNITSWPMLRDHATCFISADDCLAANGMRLL 331
Cdd:PRK06110 210 YALSFEAG----RVVTTPVATTLAdGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAY 267
PRK05638 PRK05638
threonine synthase; Validated
 119-274 9.52e-10

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 60.21  E-value: 9.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 119 FVTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWvllqdtawqg 198
Cdd:PRK05638 115 FIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGL---------- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 199 YEQIPTW---IMQGYMTLAVEIWQQLAesgapmPTHLFLQAGVGSFAGSIMGYFIEKMQ----QQAPTIIIVEPHKANCL 271
Cdd:PRK05638 185 YNVTPEYniiGLEGQKTIAFELWEEIN------PTHVIVPTGSGSYLYSIYKGFKELLEigviEEIPKLIAVQTERCNPI 258


                 ...
gi 490304197 272 YRS 274
Cdd:PRK05638 259 ASE 261
PRK07334 PRK07334
threonine dehydratase; Provisional
 120-190 9.32e-09

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 56.83  E-value: 9.32e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304197 120 VTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVL 190
Cdd:PRK07334  75 IAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTF 145
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 44-274 1.69e-07

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: 52.69  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  44 VTPLRKLEFLSQRLGLgSIHIKDEA-QRFGlnAFKGLGGSYAMGKYLAallerdintlsfaelnspviKARIKDIVFVTA 122
Cdd:cd06448    1 KTPLIESTALSKTAGC-NVFLKLENlQPSG--SFKIRGIGHLCQKSAK--------------------QGLNECVHVVCS 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 123 TDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKT--AREQGWVllqdtawqgYe 200
Cdd:cd06448   58 SGGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREElaENDPGPV---------Y- 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490304197 201 qIPTW----IMQGYMTLAVEIWQQLAESgaPMPTHLFLQAGVGS-FAGSIMGyfIEKMQQQAPTIIIVEPHKANCLYRS 274
Cdd:cd06448  128 -VHPFddplIWEGHSSMVDEIAQQLQSQ--EKVDAIVCSVGGGGlLNGIVQG--LERNGWGDIPVVAVETEGAHSLNAS 201
PRK08197 PRK08197
threonine synthase; Validated
 45-189 1.83e-07

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 52.70  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  45 TPLRKLEFLSQRLGLGSIHIKDEaqrfGLN---AFK--GLGGSYAMGKYLaallerdintlsfaelnspvikaRIKDIVF 119
Cdd:PRK08197  80 TPLLPLPRLGKALGIGRLWVKDE----GLNptgSFKarGLAVGVSRAKEL-----------------------GVKHLAM 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304197 120 VTAtdGNhgRGVAWA--AEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWV 189
Cdd:PRK08197 133 PTN--GN--AGAAWAayAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWF 200
PRK08813 PRK08813
threonine dehydratase; Provisional
 13-191 2.13e-07

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 52.32  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  13 QPYGQGADLSLLNESVGnEVLAFHQKFPDYRV-TPLRKLEFLSQRLGLGSIhikdeaQRFGLNAFKGlggsyAMGKYLAA 91
Cdd:PRK08813   8 RPTVQEPDVGDVAVSVA-DVLAAQARLRRYLSpTPLHYAERFGVWLKLENL------QRTGSYKVRG-----ALNALLAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197  92 LLERDintlsfaelNSPVIkarikdivfvTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELN 171
Cdd:PRK08813  76 LERGD---------ERPVI----------CASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNS 136

                        170       180
                 ....*....|....*....|
gi 490304197 172 YDDTVRLAAKTAREQGWVLL 191
Cdd:PRK08813 137 YDEAYAFARELADQNGYRFL 156
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
120-332 1.50e-04

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 43.47  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 120 VTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLlqdtawqgy 199
Cdd:PRK07048  76 VTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTL--------- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 200 eqIPTW----IMQGYMTLAVEIWQQLAESGApmpthLFLQAGVGSF-AGSIMGyfiekMQQQAP--TIIIVEPHKAN--- 269
Cdd:PRK07048 147 --IPPYdhphVIAGQGTAAKELFEEVGPLDA-----LFVCLGGGGLlSGCALA-----ARALSPgcKVYGVEPEAGNdgq 214

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304197 270 -CLYRSATINDGLPHSVGGDMSTLMAGlacgepNITsWPMLRDHATCFISADDCLAANGMRLLA 332
Cdd:PRK07048 215 qSFRSGEIVHIDTPRTIADGAQTQHLG------NYT-FPIIRRLVDDIVTVSDAELVDAMRFFA 271
cysM PRK11761
cysteine synthase CysM;
122-265 7.32e-04

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 41.01  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 122 ATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTIT------ELNYDdtvrLA-AKTAREQGWVLLQ-- 192
Cdd:PRK11761  69 ATSGNTGIALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVpkeqgmEGARD----LAlQMQAEGEGKVLDQfa 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304197 193 --DTAWQGYEqiptwimqgymTLAVEIWQQLAESgapmPTHlFLQAgVGSfAGSIMG---YFieKMQQQAPTIIIVEP 265
Cdd:PRK11761 145 npDNPLAHYE-----------TTGPEIWRQTEGR----ITH-FVSS-MGT-TGTIMGvsrYL--KEQNPAVQIVGLQP 202
PRK06450 PRK06450
threonine synthase; Validated
 125-265 1.71e-03

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 40.10  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 125 GNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITELNYDDTVRLAAKTAREQGWVLLQDTAWQGYEqipt 204
Cdd:PRK06450 106 GNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGSREDVAKAAENSGYYYASHVLQPQFRDGIR---- 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304197 205 wimqgymTLAVEIWQQLaesGAPMPTHLFLQAGVGSFagsIMGYF-----------IEKMqqqaPTIIIVEP 265
Cdd:PRK06450 182 -------TLAYEIAKDL---DWKIPNYVFIPVSAGTL---LLGVYsgfkhlldsgvISEM----PKIVAVQT 236
PRK10717 PRK10717
cysteine synthase A; Provisional
 120-220 2.92e-03

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 39.46  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304197 120 VTATDGNHGRGVAWAAEQLGLRAVVYMPKGSSPVRAQNIRRHGAECTITE----LNYDDTVRLAAKTAREqgwvlLQDTA 195
Cdd:PRK10717  68 VEGTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaapyANPNNYVKGAGRLAEE-----LVASE 142

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490304197 196 WQGYeqipTWIMQ---------GYMTLAVEIWQQ 220
Cdd:PRK10717 143 PNGA----IWANQfdnpanreaHYETTGPEIWEQ 172
 
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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