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Conserved domains on  [gi|114793663]
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Chain A, Threonine synthase

Protein Classification

threonine synthase( domain architecture ID 10107605)

threonine synthase catalyzes the final step of threonine biosynthesis, the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine

CATH:  3.40.50.1100
EC:  4.2.3.1
Gene Ontology:  GO:0004795|GO:0030170|GO:0009088
PubMed:  11933250
SCOP:  4000798

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
16-332 3.45e-159

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: 448.97  E-value: 3.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  16 IAAYRDRLPVgDDWTPVTLLEGGTPLIAATNLSK-QTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTG 94
Cdd:cd01563    1 LWRYRELLPV-TEDDIVSLGEGNTPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  95 NTSASAAAYAARAGITCAVLIPQGKiAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVNPVRIEGQK 174
Cdd:cd01563   80 NTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENW-IYLSNSLNPYRLEGQK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 175 TAAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLVLG--------EPVSHPET 245
Cdd:cd01563  158 TIAFEIAEQLGwEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAfkegkddiEPVENPET 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 246 IATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTV 325
Cdd:cd01563  238 IATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVL 317

                 ....*..
gi 114793663 326 TGNGLKD 332
Cdd:cd01563  318 TGHGLKD 324
 
Name Accession Description Interval E-value
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
16-332 3.45e-159

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: 448.97  E-value: 3.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  16 IAAYRDRLPVgDDWTPVTLLEGGTPLIAATNLSK-QTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTG 94
Cdd:cd01563    1 LWRYRELLPV-TEDDIVSLGEGNTPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  95 NTSASAAAYAARAGITCAVLIPQGKiAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVNPVRIEGQK 174
Cdd:cd01563   80 NTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENW-IYLSNSLNPYRLEGQK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 175 TAAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLVLG--------EPVSHPET 245
Cdd:cd01563  158 TIAFEIAEQLGwEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAfkegkddiEPVENPET 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 246 IATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTV 325
Cdd:cd01563  238 IATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVL 317

                 ....*..
gi 114793663 326 TGNGLKD 332
Cdd:cd01563  318 TGHGLKD 324
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
12-338 4.55e-138

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: 398.03  E-value: 4.55e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  12 WPGvIAAYRDRLPVGDDWTPVTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCA 91
Cdd:COG0498   41 RRG-LWRYRELLPFDDEEKAVSLGEGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  92 STGNTSASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVNPVRIE 171
Cdd:COG0498  120 SSGNGSAALAAYAARAGIEVFVFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEG-LYAVNSINPARLE 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 172 GQKTAAFEIVDVLGTAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLVL----GEPV---SHPE 244
Cdd:COG0498  199 GQKTYAFEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKELGLIDRLPRLIAVQATGCNPILTafetGRDEyepERPE 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 245 TIATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCT 324
Cdd:COG0498  279 TIAPSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPDEPVVVL 358
                        330
                 ....*....|....
gi 114793663 325 VTGNGLKDPDTALK 338
Cdd:COG0498  359 STGHGLKFPDAVRE 372
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
19-334 3.29e-118

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: 345.14  E-value: 3.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   19 YRDRLPVGDDwTPVTLLEGGTPLIAATNLSKQTGCT-IHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTS 97
Cdd:TIGR00260   4 YREFLPVTEK-DLVDLGEGVTPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   98 ASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVN--PVRIEGQKT 175
Cdd:TIGR00260  83 AAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKP-ALGLNSANsiPYRLEGQKT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  176 AAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLiDKLPRMLGTQAAGAAPLVLG-------EPVSHPETIA 247
Cdd:TIGR00260 162 YAFEAVEQLGwEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGL-DSLPVKRGIQAEGAADIVRAfleggqwEPIETPETLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  248 TAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTVTG 327
Cdd:TIGR00260 241 TAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADPAERVVCALTG 320

                  ....*..
gi 114793663  328 NGLKDPD 334
Cdd:TIGR00260 321 NGLKDPE 327
PLN02569 PLN02569
threonine synthase
4-331 3.56e-73

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 235.09  E-value: 3.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   4 PPTATHQPWPGVIAAYRDRLPVGDDWTPVTLLEGGTPLIAATNLSKQTGCTIHL--KVEGLNPTGSFKDRGMTMAVTDA- 80
Cdd:PLN02569  99 VGKTTWPYGSGVWSKKEWVLPEIDDDDIVSLFEGNSNLFWAERLGKEFLGMNDLwvKHCGISHTGSFKDLGMTVLVSQVn 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  81 ----LAHGQRAVLCASTGNTSASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADF 156
Cdd:PLN02569 179 rlrkMAKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSIDTDFDGCMRLIREVTAEL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 157 PtISLVNSVNPVRIEGQKTAAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLV 235
Cdd:PLN02569 259 P-IYLANSLNSLRLEGQKTAAIEILQQFDwEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVDRLPRLVCAQAANANPLY 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 236 LG--------EPVSHPETIATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLvARVEGVFVEPASAASIAGLL 307
Cdd:PLN02569 338 RAyksgweefKPVKANPTFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDAQAE-ADKTGMFLCPHTGVALAALK 416
                        330       340
                 ....*....|....*....|....
gi 114793663 308 KAIDDGWVARGSTVVCTVTGNGLK 331
Cdd:PLN02569 417 KLRASGVIGPTDRTVVVSTAHGLK 440
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
32-327 1.01e-66

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: 212.56  E-value: 1.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   32 VTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAH-GQRAVLCASTGNTSASAAAYAARAGIT 110
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGeGGKTVVEASSGNHGRALAAAAARLGLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  111 CAVLIPQGKIAmGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSV-NPVRIEGQKTAAFEIVDVLGTAPD 189
Cdd:pfam00291  81 VTIVVPEDAPP-GKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYdNPLNIEGYGTIGLEILEQLGGDPD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  190 VHALPVGNAGNITAYWKGyteyhqLGLIDKLPRMLGTQAAGAAPLVLG------EPVSHPETIATAIRIGSPASwTSAVE 263
Cdd:pfam00291 160 AVVVPVGGGGLIAGIARG------LKELGPDVRVIGVEPEGAPALARSlaagrpVPVPVADTIADGLGVGDEPG-ALALD 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663  264 AQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGlLKAIDDGWVARGSTVVCTVTG 327
Cdd:pfam00291 233 LLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAA-LKLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
16-332 3.45e-159

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: 448.97  E-value: 3.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  16 IAAYRDRLPVgDDWTPVTLLEGGTPLIAATNLSK-QTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTG 94
Cdd:cd01563    1 LWRYRELLPV-TEDDIVSLGEGNTPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  95 NTSASAAAYAARAGITCAVLIPQGKiAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVNPVRIEGQK 174
Cdd:cd01563   80 NTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENW-IYLSNSLNPYRLEGQK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 175 TAAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLVLG--------EPVSHPET 245
Cdd:cd01563  158 TIAFEIAEQLGwEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAfkegkddiEPVENPET 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 246 IATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTV 325
Cdd:cd01563  238 IATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVL 317

                 ....*..
gi 114793663 326 TGNGLKD 332
Cdd:cd01563  318 TGHGLKD 324
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
12-338 4.55e-138

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: 398.03  E-value: 4.55e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  12 WPGvIAAYRDRLPVGDDWTPVTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCA 91
Cdd:COG0498   41 RRG-LWRYRELLPFDDEEKAVSLGEGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  92 STGNTSASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVNPVRIE 171
Cdd:COG0498  120 SSGNGSAALAAYAARAGIEVFVFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEG-LYAVNSINPARLE 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 172 GQKTAAFEIVDVLGTAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLVL----GEPV---SHPE 244
Cdd:COG0498  199 GQKTYAFEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKELGLIDRLPRLIAVQATGCNPILTafetGRDEyepERPE 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 245 TIATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCT 324
Cdd:COG0498  279 TIAPSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPDEPVVVL 358
                        330
                 ....*....|....
gi 114793663 325 VTGNGLKDPDTALK 338
Cdd:COG0498  359 STGHGLKFPDAVRE 372
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
19-334 3.29e-118

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: 345.14  E-value: 3.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   19 YRDRLPVGDDwTPVTLLEGGTPLIAATNLSKQTGCT-IHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTS 97
Cdd:TIGR00260   4 YREFLPVTEK-DLVDLGEGVTPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   98 ASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPtISLVNSVN--PVRIEGQKT 175
Cdd:TIGR00260  83 AAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKP-ALGLNSANsiPYRLEGQKT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  176 AAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLiDKLPRMLGTQAAGAAPLVLG-------EPVSHPETIA 247
Cdd:TIGR00260 162 YAFEAVEQLGwEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGL-DSLPVKRGIQAEGAADIVRAfleggqwEPIETPETLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  248 TAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTVTG 327
Cdd:TIGR00260 241 TAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADPAERVVCALTG 320

                  ....*..
gi 114793663  328 NGLKDPD 334
Cdd:TIGR00260 321 NGLKDPE 327
PLN02569 PLN02569
threonine synthase
4-331 3.56e-73

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 235.09  E-value: 3.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   4 PPTATHQPWPGVIAAYRDRLPVGDDWTPVTLLEGGTPLIAATNLSKQTGCTIHL--KVEGLNPTGSFKDRGMTMAVTDA- 80
Cdd:PLN02569  99 VGKTTWPYGSGVWSKKEWVLPEIDDDDIVSLFEGNSNLFWAERLGKEFLGMNDLwvKHCGISHTGSFKDLGMTVLVSQVn 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  81 ----LAHGQRAVLCASTGNTSASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADF 156
Cdd:PLN02569 179 rlrkMAKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSIDTDFDGCMRLIREVTAEL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 157 PtISLVNSVNPVRIEGQKTAAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLV 235
Cdd:PLN02569 259 P-IYLANSLNSLRLEGQKTAAIEILQQFDwEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVDRLPRLVCAQAANANPLY 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 236 LG--------EPVSHPETIATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLvARVEGVFVEPASAASIAGLL 307
Cdd:PLN02569 338 RAyksgweefKPVKANPTFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDAQAE-ADKTGMFLCPHTGVALAALK 416
                        330       340
                 ....*....|....*....|....
gi 114793663 308 KAIDDGWVARGSTVVCTVTGNGLK 331
Cdd:PLN02569 417 KLRASGVIGPTDRTVVVSTAHGLK 440
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
32-327 1.01e-66

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: 212.56  E-value: 1.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   32 VTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAH-GQRAVLCASTGNTSASAAAYAARAGIT 110
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGeGGKTVVEASSGNHGRALAAAAARLGLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  111 CAVLIPQGKIAmGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSV-NPVRIEGQKTAAFEIVDVLGTAPD 189
Cdd:pfam00291  81 VTIVVPEDAPP-GKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYdNPLNIEGYGTIGLEILEQLGGDPD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  190 VHALPVGNAGNITAYWKGyteyhqLGLIDKLPRMLGTQAAGAAPLVLG------EPVSHPETIATAIRIGSPASwTSAVE 263
Cdd:pfam00291 160 AVVVPVGGGGLIAGIARG------LKELGPDVRVIGVEPEGAPALARSlaagrpVPVPVADTIADGLGVGDEPG-ALALD 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663  264 AQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGlLKAIDDGWVARGSTVVCTVTG 327
Cdd:pfam00291 233 LLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAA-LKLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
39-327 1.21e-62

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: 200.05  E-value: 1.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRA---VLCASTGNTSASAAAYAARAGITCAVLI 115
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPkgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 116 PQGKiAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNS-VNPVRIEGQKTAAFEIV-DVLGTAPDVHAL 193
Cdd:cd00640   81 PEGA-SPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQfDNPANIAGQGTIGLEILeQLGGQKPDAVVV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 194 PVGNAGNITAYWKGYTEYHqlglidKLPRMLGTQAagaaplvlgepvshpetiatairigspaswtsaveaqqqskgRFL 273
Cdd:cd00640  160 PVGGGGNIAGIARALKELL------PNVKVIGVEP------------------------------------------EVV 191
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 114793663 274 AASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGwvARGSTVVCTVTG 327
Cdd:cd00640  192 TVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL--GKGKTVVVILTG 243
PRK08197 PRK08197
threonine synthase; Validated
19-335 1.21e-60

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 199.84  E-value: 1.21e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  19 YRDRLPVGDDWTPVTLLEGGTPLIAATNLSKQTGC-TIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTS 97
Cdd:PRK08197  60 YHELLPVRDPEHIVSLGEGMTPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAG 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  98 ASAAAYAARAGITCAVLIPQGKIAMGKLAQAVMhGAKIIQIDGNFDDCLELARKMAAD---FPTISLVNsvnPVRIEGQK 174
Cdd:PRK08197 140 AAWAAYAARAGIRATIFMPADAPEITRLECALA-GAELYLVDGLISDAGKIVAEAVAEygwFDVSTLKE---PYRIEGKK 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 175 TAAFEIVDVLG-TAPDVHALPVGNAGNITAYWKGYTEYHQLGLID-KLPRMLGTQAAGAAPLV--------LGEPVSHPE 244
Cdd:PRK08197 216 TMGLELAEQLGwRLPDVILYPTGGGVGLIGIWKAFDELEALGWIGgKRPRLVAVQAEGCAPIVkaweegkeESEFWEDAH 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 245 TIATAIRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCT 324
Cdd:PRK08197 296 TVAFGIRVPKALGDFLVLDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWLKGDERVVLF 375
                        330
                 ....*....|.
gi 114793663 325 VTGNGLKDPDT 335
Cdd:PRK08197 376 NTGSGLKYPDT 386
PRK05638 PRK05638
threonine synthase; Validated
32-333 1.48e-58

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 195.80  E-value: 1.48e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  32 VTLLEGGTPLIAATNLSKqTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTSASAAAYAARAGITC 111
Cdd:PRK05638  60 ISLGEGGTPLIRARISEK-LGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 112 AVLIPQgKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLGtaPDVH 191
Cdd:PRK05638 139 FVVVPR-KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHV 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 192 ALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPL---VLGEPVSHPETIATAIRIGSPASWTSAVEAQQQS 268
Cdd:PRK05638 216 IVPTGSGSYLYSIYKGFKELLEIGVIEEIPKLIAVQTERCNPIaseILGNKTKCNETKALGLYVKNPVMKEYVSEAIKES 295
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114793663 269 KGRFLAASDEEILAAYHLVARvEGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTVTGNGLKDP 333
Cdd:PRK05638 296 GGTAVVVNEEEIMAGEKLLAK-EGIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTGSGLKGY 359
PRK06381 PRK06381
threonine synthase; Validated
37-327 1.62e-41

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 147.54  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  37 GGTPLIAATNLSKQTGCT-IHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTSASAAAYAARAGITCAVLI 115
Cdd:PRK06381  14 GGTPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 116 PQGkIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADF------PtislvNSVNP-VRIEGQKTAAFEIVDVLGTAP 188
Cdd:PRK06381  94 PRS-YSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENgiydanP-----GSVNSvVDIEAYSAIAYEIYEALGDVP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 189 DVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLV------LGEPVS-HPETIA-TAirIGSP-ASWT 259
Cdd:PRK06381 168 DAVAVPVGNGTTLAGIYHGFRRLYDRGKTSRMPRMIGVSTSGGNQIVesfkrgSSEVVDlEVDEIReTA--VNEPlVSYR 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114793663 260 S-----AVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVARgsTVVCTVTG 327
Cdd:PRK06381 246 SfdgdnALEAIYDSHGYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVND--NVVAVITG 316
PRK08329 PRK08329
threonine synthase; Validated
19-331 1.09e-40

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 146.12  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  19 YRDRLPVGDDWTPvTLLEGGTPLIaatnlskQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTSA 98
Cdd:PRK08329  46 YIDYLPVDEEFLP-HLTPPITPTV-------KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAAL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  99 SAAAYAARAGITCAVLIP----QGKIAMGKLAQAVMHgakiiQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQK 174
Cdd:PRK08329 118 SLALYSLSEGIKVHVFVSynasKEKISLLSRLGAELH-----FVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTK 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 175 TAAFEIVDVLGTaPDVHALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPLVlgePVSHPE-TIATAIRIG 253
Cdd:PRK08329 193 TIAYEIYEQIGV-PDYAFVPVGSGTLFLGIWKGFKELHEMGEISKMPKLVAVQAEGYESLC---KRSKSEnKLADGIAIP 268
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114793663 254 SPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVeGVFVEPASAASIAGLLKAIDDGWVARGSTVVCTVTGNGLK 331
Cdd:PRK08329 269 EPPRKEEMLRALEESNGFCISVGEEETRAALHWLRRM-GFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLK 345
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
39-327 2.82e-31

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: 119.90  E-value: 2.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTdALAHGQRA--VLCASTGNTSASAAAYAARAGITCAVLIP 116
Cdd:cd01562   18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLL-SLSEEERAkgVVAASAGNHAQGVAYAAKLLGIPATIVMP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 117 QGKIAMgKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDvlgTAPDVHAL--P 194
Cdd:cd01562   97 ETAPAA-KVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILE---QVPDLDAVfvP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 195 VGNAG---NITAYWKgyteyHQLGLIdklpRMLGTQAAGAAPLVL----GEPVSHPE--TIATAIRIGSPASWTSAVeaQ 265
Cdd:cd01562  173 VGGGGliaGIATAVK-----ALSPNT----KVIGVEPEGAPAMAQslaaGKPVTLPEvdTIADGLAVKRPGELTFEI--I 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114793663 266 QQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDgwvARGSTVVCTVTG 327
Cdd:cd01562  242 RKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSG 300
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
39-327 7.10e-30

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: 116.67  E-value: 7.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVtDALAHGQRA--VLCASTGNTSASAAAYAARAGITCAVLIP 116
Cdd:COG1171   25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNAL-ASLSEEERArgVVAASAGNHAQGVAYAARLLGIPATIVMP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 117 QGkIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAA--------DF--PTIslvnsvnpvrIEGQKTAAFEIVDvlgT 186
Cdd:COG1171  104 ET-APAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEeegatfvhPFddPDV----------IAGQGTIALEILE---Q 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 187 APDVHAL--PVGN----AGnITAYWKGyteyhqlglIDKLPRMLGTQAAGAAPLVL----GEPVSHPE--TIATAIRIGS 254
Cdd:COG1171  170 LPDLDAVfvPVGGggliAG-VAAALKA---------LSPDIRVIGVEPEGAAAMYRslaaGEPVTLPGvdTIADGLAVGR 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114793663 255 PASWTSAVeAQQQSkGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDgwvARGSTVVCTVTG 327
Cdd:COG1171  240 PGELTFEI-LRDLV-DDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSG 307
PRK06450 PRK06450
threonine synthase; Validated
32-331 5.83e-23

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 97.88  E-value: 5.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  32 VTLLEGGTPLIAATNlskqtgctIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRAVLCASTGNTSASAAAYAARAGITC 111
Cdd:PRK06450  52 ISLGEGRTPLIKKGN--------IWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 112 AVLIPQgKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLvnsvNPVRIEGQKTAAFEIVDVLGT-APDV 190
Cdd:PRK06450 124 KIFVPE-TASGGKLKQIESYGAEVVRVRGSREDVAKAAENSGYYYASHVL----QPQFRDGIRTLAYEIAKDLDWkIPNY 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 191 HALPVGNAGNITAYWKGYTEYHQLGLIDKLPRMLGTQAAGAAPL---VLGEPVSHPE---TIATAIRIGSPASWTSAVEA 264
Cdd:PRK06450 199 VFIPVSAGTLLLGVYSGFKHLLDSGVISEMPKIVAVQTEQVSPLcakFKGISYTPPDkvtSIADALVSTRPFLLDYMVKA 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114793663 265 QQQSkGRFLAASDEEILAAYHLVARvEGVFVEPASAASIAGLLKaiddgWVARGSTVVctVTGNGLK 331
Cdd:PRK06450 279 LSEY-GECIVVSDNEIVEAWKELAK-KGLLVEYSSATVYAAYKK-----YSVNDSVLV--LTGSGLK 336
PRK08639 PRK08639
threonine dehydratase; Validated
39-327 2.16e-20

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 91.41  E-value: 2.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVtDALAHGQRA--VLCASTGNtsasaaayaARAGI--TCAVL 114
Cdd:PRK08639  26 TPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAI-SQLSDEELAagVVCASAGN---------HAQGVayACRHL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 115 IPQGKIAM------GKLAQAVMHGAK---IIQIDGNFDDCLELARKMAAD--------FPtislvnsvNPVRIEGQKTAA 177
Cdd:PRK08639  96 GIPGVIFMpvttpqQKIDQVRFFGGEfveIVLVGDTFDDSAAAAQEYAEEtgatfippFD--------DPDVIAGQGTVA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 178 FEIVDVLGTA--PDVHALPVGNAG---NITAYWKGYTeyhqlglidklP--RMLGTQAAGA----APLVLGEPVSHPET- 245
Cdd:PRK08639 168 VEILEQLEKEgsPDYVFVPVGGGGlisGVTTYLKERS-----------PktKIIGVEPAGAasmkAALEAGKPVTLEKId 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 246 -----IATAiRIGS-PASWTSAVEAQqqskgrfLAASDE-----EILAAYHlvarVEGVFVEPASAASIAGLLKAIDDgw 314
Cdd:PRK08639 237 kfvdgAAVA-RVGDlTFEILKDVVDD-------VVLVPEgavctTILELYN----KEGIVAEPAGALSIAALELYKDE-- 302
                        330
                 ....*....|...
gi 114793663 315 vARGSTVVCTVTG 327
Cdd:PRK08639 303 -IKGKTVVCVISG 314
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
37-340 1.46e-19

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: 87.57  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  37 GGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQ----RAVLCASTGNTSASAAAYAARAGITCA 112
Cdd:cd01561    1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 113 VLIPqGKIAMGKLAQAVMHGAKIIQIDGNFDD----CLELARKMAADFPtislvNSV------NPVRIEG-QKTAAFEIV 181
Cdd:cd01561   81 IVMP-ETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETP-----NAFwlnqfeNPANPEAhYETTAPEIW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 182 DVLGTAPDVHALPVGNAGNITaywkGYTEYhqlgLIDKLP--RMLGTQAAGAAPLVLGEPVSHpetIATAIRIGS-PASW 258
Cdd:cd01561  155 EQLDGKVDAFVAGVGTGGTIT----GVARY----LKEKNPnvRIVGVDPVGSVLFSGGPPGPH---KIEGIGAGFiPENL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 259 -TSAVEaqqqskgRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDgwVARGSTVVCTVtgnglkdPDTAL 337
Cdd:cd01561  224 dRSLID-------EVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKR--LGPGKTIVTIL-------PDSGE 287

                 ...
gi 114793663 338 KDM 340
Cdd:cd01561  288 RYL 290
PRK06815 PRK06815
threonine/serine dehydratase;
39-327 9.36e-19

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 85.51  E-value: 9.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTdALAHGQR--AVLCASTGNTSASAAAYAARAGITCAVLIP 116
Cdd:PRK06815  21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLR-LLNEAQRqqGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 117 QGKIAMgKLAQAVMHGAKIIQIDgnfDDCLEL---ARKMAAD--FPTISLVNsvNPVRIEGQKTAAFEIVDvlgTAPDVH 191
Cdd:PRK06815 100 EQASAI-KLDAIRALGAEVRLYG---GDALNAelaARRAAEQqgKVYISPYN--DPQVIAGQGTIGMELVE---QQPDLD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 192 AL--PVGNAGNITaywkGYTEYhqLGLIDKLPRMLGTQAAGAA----PLVLGEPVSHPE--TIATAIRIG-SPASWTsaV 262
Cdd:PRK06815 171 AVfvAVGGGGLIS----GIATY--LKTLSPKTEIIGCWPANSPslytSLEAGEIVEVAEqpTLSDGTAGGvEPGAIT--F 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114793663 263 EAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDgwvARGSTVVCTVTG 327
Cdd:PRK06815 243 PLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPR---YQGKKVAVVLCG 304
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
39-304 2.05e-18

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: 84.66  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQ---RAVLCASTGNTSASAAAYAARAGITCAVLI 115
Cdd:cd06448    2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLnecVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 116 PQ--GKIAMGKLAQAvmhGAKIIQIDGNFDDCLELARK--MAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLGTA--PD 189
Cdd:cd06448   82 PEstKPRVVEKLRDE---GATVVVHGKVWWEADNYLREelAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQekVD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 190 VHALPVGNAGNITAYWKGYTEYHQlgliDKLPrMLGTQAAGA----APLVLGEPVSHPETIATAIRIGSPASWTSAVEAQ 265
Cdd:cd06448  159 AIVCSVGGGGLLNGIVQGLERNGW----GDIP-VVAVETEGAhslnASLKAGKLVTLPKITSVATSLGAKTVSSQALEYA 233
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 114793663 266 QQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIA 304
Cdd:cd06448  234 QEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALA 272
eutB PRK07476
threonine dehydratase; Provisional
39-335 1.20e-14

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 73.85  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTdALAHGQRA--VLCASTGNTSASAAAYAARAGITCAV--- 113
Cdd:PRK07476  20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALL-SLSAQERArgVVTASTGNHGRALAYAARALGIRATIcms 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 114 -LIPQGKIAmgklaqAV-MHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLgtaPDVH 191
Cdd:PRK07476  99 rLVPANKVD------AIrALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEAL---PDVA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 192 ALPV-----GNAGNITAYWKGyteyhqlglIDKLPRMLGTQ----AAGAAPLVLGEPVSHPE--TIATAIR--IGSPASW 258
Cdd:PRK07476 170 TVLVplsggGLASGVAAAVKA---------IRPAIRVIGVSmergAAMHASLAAGRPVQVEEvpTLADSLGggIGLDNRY 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114793663 259 TSAVeAQQQSKGRFLaASDEEILAAYHLVARVEGVFVEPASAASIAGLLkaiDDGWVARGSTVVCTVTGNGLkDPDT 335
Cdd:PRK07476 241 TFAM-CRALLDDVVL-LDEAEIAAGIRHAYREERLVVEGAGAVGIAALL---AGKIAARDGPIVVVVSGANI-DMEL 311
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
37-323 2.94e-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: 72.39  E-value: 2.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  37 GGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDR-GMTMaVTDALAHGQ----RAVLCASTGNTsasaaayaaraGI-- 109
Cdd:COG0031   12 GNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRiALSM-IEDAEKRGLlkpgGTIVEATSGNT-----------GIgl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 110 --TCAVL-------IPQgKIAMGKLAQAVMHGAKIIQIDG--NFDDCLELARKMAADFPtislvNSV------NPVRIEG 172
Cdd:COG0031   80 amVAAAKgyrlilvMPE-TMSKERRALLRAYGAEVVLTPGaeGMKGAIDKAEELAAETP-----GAFwpnqfeNPANPEA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 173 -QKTAAFEIVDVLGTAPDVHALPVGNAGNITaywkGYTEYhqlgLIDKLP--RMLGTQAAGAAPLVLGEPVSHPetiata 249
Cdd:COG0031  154 hYETTGPEIWEQTDGKVDAFVAGVGTGGTIT----GVGRY----LKERNPdiKIVAVEPEGSPLLSGGEPGPHK------ 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114793663 250 IR-IGS---PASW-TSAVEaqqqskgRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDgwVARGSTVVC 323
Cdd:COG0031  220 IEgIGAgfvPKILdPSLID-------EVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR--LGPGKTIVT 289
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
39-327 1.90e-13

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 70.53  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGM---TMAVTDalAHGQRAVLCASTGNTSASAAAYAARAGITCAVLI 115
Cdd:PRK08638  28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTD--AEKRKGVVACSAGNHAQGVALSCALLGIDGKVVM 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 116 PQGKIAMgKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLGTAPDVhALPV 195
Cdd:PRK08638 106 PKGAPKS-KVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTV-IVPI 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 196 GNAGNITAYWKGyteyhqLGLIDKLPRMLGTQAAG----AAPLVLGEPVSHPE--TIATAIRIGSPASWTsaVEAQQQSK 269
Cdd:PRK08638 184 GGGGLIAGIAVA------LKSINPTIHIIGVQSENvhgmAASFYAGEITTHRTtgTLADGCDVSRPGNLT--YEIVRELV 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 114793663 270 GRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDGWVaRGSTVVCTVTG 327
Cdd:PRK08638 256 DDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYI-QNKKVVAIISG 312
PRK07334 PRK07334
threonine dehydratase; Provisional
39-308 2.16e-11

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 64.53  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMT---MAVTDalAHGQRAVLCASTGNTSASAAAYAARAGITCAVLI 115
Cdd:PRK07334  24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALnklLLLTE--EERARGVIAMSAGNHAQGVAYHAQRLGIPATIVM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 116 PQGKiAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADfPTISLVNSVN-PVRIEGQKTAAFEIvdvLGTAPDVHAL- 193
Cdd:PRK07334 102 PRFT-PTVKVERTRGFGAEVVLHGETLDEARAHARELAEE-EGLTFVHPYDdPAVIAGQGTVALEM---LEDAPDLDTLv 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 194 -PVGNAGNI----TAYwKGyteyhqlglIDKLPRMLGTQAAG-----AAPLVLGEPVSHpETIATAIRIGSPASWTSAVE 263
Cdd:PRK07334 177 vPIGGGGLIsgmaTAA-KA---------LKPDIEIIGVQTELypsmyAAIKGVALPCGG-STIAEGIAVKQPGQLTLEIV 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 114793663 264 AQQQSkgRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLK 308
Cdd:PRK07334 246 RRLVD--DILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLA 288
PRK12483 PRK12483
threonine dehydratase; Reviewed
39-206 5.28e-11

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 63.66  E-value: 5.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRG----MTMAVTDALAhgqRAVLCASTGNTSASAAAYAARAGITCAVL 114
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLA---RGVITASAGNHAQGVALAAARLGVKAVIV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 115 IPQGKIAMgKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLGTAPDVHALP 194
Cdd:PRK12483 115 MPRTTPQL-KVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPLDAIFVP 193
                        170
                 ....*....|....*
gi 114793663 195 VGNAG---NITAYWK 206
Cdd:PRK12483 194 VGGGGliaGIAAYVK 208
PRK08813 PRK08813
threonine dehydratase; Provisional
57-199 1.06e-10

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 62.34  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  57 LKVEGLNPTGSFKDRGMTMAVTDALAHG-QRAVLCASTGNTSASAAAYAARAGITCAVLIPQGKIAMgKLAQAVMHGAKI 135
Cdd:PRK08813  52 LKLENLQRTGSYKVRGALNALLAGLERGdERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQT-KIAGVAHWGATV 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663 136 IQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVdvlGTAPDVHALPVGNAG 199
Cdd:PRK08813 131 RQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELA---AHAPDVVIVPIGGGG 191
PLN02356 PLN02356
phosphateglycerate kinase
37-116 4.48e-09

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 57.69  E-value: 4.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  37 GGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRA----VLCASTGNTSASAAAYAARAGITCA 112
Cdd:PLN02356  52 GNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFpggvVTEGSAGSTAISLATVAPAYGCKCH 131

                 ....
gi 114793663 113 VLIP 116
Cdd:PLN02356 132 VVIP 135
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
64-203 4.52e-09

Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.


Pssm-ID: 107203 [Multi-domain]  Cd Length: 460  Bit Score: 57.63  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  64 PTGSFKDRGM--TMAVTDALAHGQR---AVLCASTGNT-SASAAAYAARAGITCAVLIPQGKIAmgKLAQAVMHGA---- 133
Cdd:cd01560  106 PTLAFKDMALqfLGRLLEYFLKRRNeriTILVATSGDTgSAAIEGFRGKPNVDVVVLYPKGGVS--PIQELQMTTLpadn 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 134 -KIIQIDGNFDDCLELARKMAADFP-----TISLVNSVNPVRIEGQKT----AAFEiVDVLGTAPDVH-ALPVGNAGNIT 202
Cdd:cd01560  184 vHVVAVEGDFDDCQSLVKALFADEDfnkklKLSSANSINWARILAQIVyyfyAYLQ-LLKRGEGEKVEfSVPTGNFGNIL 262

                 .
gi 114793663 203 A 203
Cdd:cd01560  263 A 263
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
39-308 5.13e-09

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 57.46  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRG----MTMAVTDALAHGqraVLCASTGNTSASAAAYAARAGITcAVL 114
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARG---VITASAGNHAQGVALSAARLGIK-AVI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 115 I-----PQGKI----AMGklAQAVMHGAkiiqidgNFDDCLELARKMAA----------DFPTIslvnsvnpvrIEGQKT 175
Cdd:PRK09224  97 VmpvttPDIKVdavrAFG--GEVVLHGD-------SFDEAYAHAIELAEeegltfihpfDDPDV----------IAGQGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 176 AAFEIVDVLGTAPDVHALPVGNAG---NITAYWKgyteyhQLglidkLP--RMLGTQAAGAAPLVL----GEPVSHPET- 245
Cdd:PRK09224 158 IAMEILQQHPHPLDAVFVPVGGGGliaGVAAYIK------QL-----RPeiKVIGVEPEDSACLKAaleaGERVDLPQVg 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663 246 -----IATAiRIGspaswTSAVEAQQQSKGRFLAASDEEILAAyhlvarVEGVF------VEPASAASIAGLLK 308
Cdd:PRK09224 227 lfadgVAVK-RIG-----EETFRLCQEYVDDVITVDTDEICAA------IKDVFedtrsiAEPAGALALAGLKK 288
PRK08246 PRK08246
serine/threonine dehydratase;
57-307 5.26e-09

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 56.89  E-value: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  57 LKVEGLNPTGSFKDRGmtmAVTDALAHGQRA--VLCASTGNTSASAAAYAARAGITCAVLIP----QGKIAmgKLAQavm 130
Cdd:PRK08246  41 LKLEHLQHTGSFKARG---AFNRLLAAPVPAagVVAASGGNAGLAVAYAAAALGVPATVFVPetapPAKVA--RLRA--- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 131 HGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLGtAPDVHALPVGNAG---NITAYWKG 207
Cdd:PRK08246 113 LGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAP-GVDTVLVAVGGGGliaGIAAWFEG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 208 YTeyhqlglidklpRMLGTQAAGA----APLVLGEPVSHP-ETIAT----AIRIGSPAsWTSAVEAQQQSkgrfLAASDE 278
Cdd:PRK08246 192 RA------------RVVAVEPEGAptlhAALAAGEPVDVPvSGIAAdslgARRVGEIA-FALARAHVVTS----VLVSDE 254
                        250       260
                 ....*....|....*....|....*....
gi 114793663 279 EILAAYHLVARVEGVFVEPASAASIAGLL 307
Cdd:PRK08246 255 AIIAARRALWEELRLAVEPGAATALAALL 283
PRK06608 PRK06608
serine/threonine dehydratase;
39-199 4.95e-08

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 54.01  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRA--VLCASTGNTSASAAAYAARAGITCAVLIP 116
Cdd:PRK06608  24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPdkIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 117 QgKIAMGKLAQAVMHGAKIIQIdgNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLGTAPDVHALPVG 196
Cdd:PRK06608 104 L-NTSKVKQQAALYYGGEVILT--NTRQEAEEKAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFASCG 180

                 ...
gi 114793663 197 NAG 199
Cdd:PRK06608 181 GGG 183
PRK10717 PRK10717
cysteine synthase A; Provisional
32-140 1.35e-07

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 52.56  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  32 VTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQ----RAVLCASTGNTSASAAAYAARA 107
Cdd:PRK10717   7 VSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLlkpgGTIVEGTAGNTGIGLALVAAAR 86
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 114793663 108 GITCAVLIP----QGKIAMGKLaqavmHGAKIIQIDG 140
Cdd:PRK10717  87 GYKTVIVMPetqsQEKKDLLRA-----LGAELVLVPA 118
PLN02550 PLN02550
threonine dehydratase
39-206 2.26e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 52.62  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGM-TMAVTDALAHGQRAVLCASTGNTSASAAAYAARAGITCAVLIPq 117
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMP- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 118 gkIAMGKLA-QAVMH-GAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPVRIEGQKTAAFEIVDVLgTAPdVHAL-- 193
Cdd:PLN02550 189 --VTTPEIKwQSVERlGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQH-QGP-LHAIfv 264
                        170
                 ....*....|....*.
gi 114793663 194 PVGNAG---NITAYWK 206
Cdd:PLN02550 265 PVGGGGliaGIAAYVK 280
PRK06110 PRK06110
threonine dehydratase;
39-308 8.22e-07

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 49.99  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGmTMAVTDALAHGQ---RAVLCASTGNTSASAAAYAARAGITCAVLI 115
Cdd:PRK06110  22 TPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRG-GLVYFDRLARRGprvRGVISATRGNHGQSVAFAARRHGLAATIVV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 116 PQG-----KIAMGKLaqavmhGAKIIQIDGNFDDCLELARKMAAdFPTISLVNSVNPVRIEGQKTAAFEIvdvLGTAPDV 190
Cdd:PRK06110 101 PHGnsvekNAAMRAL------GAELIEHGEDFQAAREEAARLAA-ERGLHMVPSFHPDLVRGVATYALEL---FRAVPDL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 191 HAL--PVGNAGNItaywkgyteyhqLGLI---DKL---PRMLGTQAAGAAPLVL----GEPVSHP--ETIA--TAIRIGS 254
Cdd:PRK06110 171 DVVyvPIGMGSGI------------CGAIaarDALglkTRIVGVVSAHAPAYALsfeaGRVVTTPvaTTLAdgMACRTPD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 114793663 255 PaswtSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLK 308
Cdd:PRK06110 239 P----EALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQ 288
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
39-340 1.30e-06

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 50.19  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKdrgmtmaVTDALahGQrAVLCASTGNTSASAAAYAARAGI----TCAVL 114
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHK-------INNAL--GQ-ALLAKRMGKTRIIAETGAGQHGVatatACALF 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 115 IPQGKIAMGKL-----AQAV----MHGAKIIQIDG------------------NFDDCLELARKMAADFPTISLVNSVNP 167
Cdd:PRK13803 342 GLKCTIFMGEEdikrqALNVermkLLGANVIPVLSgsktlkdavneairdwvaSVPDTHYLIGSAVGPHPYPEMVAYFQS 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 168 VRIEGQKTaafEIVDVLGTAPDVHALPVGNAGNITAYWKGYteyhqlgLIDKLPRMLGTQAAGaaplvLGepVSHPETIA 247
Cdd:PRK13803 422 VIGEEAKE---QLKEQTGKLPDAIIACVGGGSNAIGIFYHF-------LDDPSVKLIGVEAGG-----KG--VNTGEHAA 484
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 248 TaIRIGSPA----SWT----------------SA---------VEAQQQSKGR--FLAASDEEILAAYHLVARVEGVFVE 296
Cdd:PRK13803 485 T-IKKGRKGvlhgSMTylmqdengqilephsiSAgldypgigpMHANLFETGRaiYTSVTDEEALDAFKLLAKLEGIIPA 563
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 114793663 297 PASAASIAGLLKAidDGWVARGSTVVCTVTGNGLKDPDTALKDM 340
Cdd:PRK13803 564 LESSHALAYLKEG--RKKFKKKDIVIVNLSGRGDKDIPTLKEYF 605
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
39-327 2.43e-06

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 48.86  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRA-VLCASTGNTSASAAAYAARAGITCAVLIPQ 117
Cdd:PRK07048  25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAgVVTFSSGNHAQAIALSARLLGIPATIVMPQ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 118 GKIAMgKLAQAVMHGAKIIQIDGNFDDCLELARKMAADfPTISLVNSVN-PVRIEGQKTAAFEIVDVLGtAPDVHALPVG 196
Cdd:PRK07048 105 DAPAA-KVAATRGYGGEVVTYDRYTEDREEIGRRLAEE-RGLTLIPPYDhPHVIAGQGTAAKELFEEVG-PLDALFVCLG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 197 NAGNI--TAywkgyteyhqlglidklprmLGTQAAGAAPLVLG-EP-----------------VSHPETIATAIRIGSPA 256
Cdd:PRK07048 182 GGGLLsgCA--------------------LAARALSPGCKVYGvEPeagndgqqsfrsgeivhIDTPRTIADGAQTQHLG 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114793663 257 SWTSAVeaQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLKAIDDgwvARGSTVVCTVTG 327
Cdd:PRK07048 242 NYTFPI--IRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP---LKGKRVGVIISG 307
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
32-308 2.97e-06

cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273463  Cd Length: 299  Bit Score: 48.43  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663   32 VTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDR-GMTMaVTDALAHGQ----RAVLCASTGNTSASAAAYAAR 106
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRiALSM-ILDAEKRGLlkpgDTIIEATSGNTGIALAMVAAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  107 AGITCAVLIPQgkiAMGKLAQAVM--HGAKIIQIDGN--FDDCLELARKMAADFPTISLVNSV-NPVRIEG-QKTAAFEI 180
Cdd:TIGR01136  80 RGYKLILTMPE---TMSLERRKLLraYGAELILTPGEegMKGAIDKAEELAAETNKYVMLDQFeNPANPEAhYKTTGPEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  181 VDVLGTAPDVHALPVGNAGNITaywkGYTEYhqlgLIDKLP--RMLGTQAAGAAPLVLGEPVSHPetiataIRiGSPASW 258
Cdd:TIGR01136 157 WRDTDGRIDHFVAGVGTGGTIT----GVGRY----LKEQNPniQIVAVEPAESPVLSGGEPGPHK------IQ-GIGAGF 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 114793663  259 TSAVEAQQQSKGRFLAASDEEILAAYHLvARVEGVFVEPASAASIAGLLK 308
Cdd:TIGR01136 222 IPKILDLSLIDEVITVSDEDAIETARRL-AREEGILVGISSGAAVAAALK 270
PLN02970 PLN02970
serine racemase
39-307 2.23e-05

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 45.82  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALA-HGQRAVLCASTGNTSASAAAYAARAGITCAVLIPQ 117
Cdd:PLN02970  28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDdQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVVPK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 118 GKiAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADfPTISLVNSVNPVR-IEGQKTAAFEIVDvlgTAPDVHAL--P 194
Cdd:PLN02970 108 NA-PACKVDAVIRYGGIITWCEPTVESREAVAARVQQE-TGAVLIHPYNDGRvISGQGTIALEFLE---QVPELDVIivP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 195 VGNAGNIT---AYWKGyteyhqlglIDKLPRMLGTQAAG----AAPLVLGEPVS--HPETIATAIRiGSPASWTSAVEAQ 265
Cdd:PLN02970 183 ISGGGLISgiaLAAKA---------IKPSIKIIAAEPKGaddaAQSKAAGEIITlpVTNTIADGLR-ASLGDLTWPVVRD 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 114793663 266 QQSKgrFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLL 307
Cdd:PLN02970 253 LVDD--VITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAL 292
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
39-335 2.69e-05

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 45.60  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQT-GCTIHLKVEGLNPTGSFKdrgmtmaVTDALAH------------------GQRAVLCAstgntsas 99
Cdd:cd06446   35 TPLYRAKRLSEYLgGAKIYLKREDLNHTGAHK-------INNALGQallakrmgkkrviaetgaGQHGVATA-------- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 100 aaayaaragITCAVLIPQGKIAMGKL---AQAV------MHGAKIIQIDGNF-------DDCLELARKMAADfpTISLVN 163
Cdd:cd06446  100 ---------TACALFGLECEIYMGAVdveRQPLnvfrmeLLGAEVVPVPSGSgtlkdaiSEAIRDWVTNVED--THYLLG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 164 SV-------NPVR----IEGQKTAAfEIVDVLGTAPDVHALPVG---NAGNITaywkgyteYHQLGliDKLPRMLGTQAA 229
Cdd:cd06446  169 SVvgphpypNMVRdfqsVIGEEAKK-QILEKEGELPDVVIACVGggsNAAGLF--------YPFIN--DKDVKLIGVEAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 230 G--------AAPLVLGEP-VSH----------------PETIATAIR---IGSPASWTsaveaqqQSKGR--FLAASDEE 279
Cdd:cd06446  238 GcgletgghAAYLFGGTAgVLHglkmytlqdedgqivpPHSISAGLDypgVGPEHAYL-------KDSGRveYVAVTDEE 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 114793663 280 ILAAYHLVARVEGVFVEPASAASIAGLLK-AIDDGwvaRGSTVVCTVTGNGLKDPDT 335
Cdd:cd06446  311 ALEAFKLLARTEGIIPALESSHAIAYAIKlAKKLG---KEKVIVVNLSGRGDKDLQT 364
cysM PRK11761
cysteine synthase CysM;
37-96 6.83e-05

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 44.09  E-value: 6.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663  37 GGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDALAHGQRA---VLC-ASTGNT 96
Cdd:PRK11761  11 GNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKpgdTLIeATSGNT 74
PLN03013 PLN03013
cysteine synthase
21-308 1.14e-04

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 44.00  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  21 DRLPVGDDwtpVTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDA-----LAHGQRAVLCASTGN 95
Cdd:PLN03013 109 DGLNIADN---VSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAeqkgfISPGKSVLVEPTSGN 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  96 TSASAAAYAARAGITCAVLIPqGKIAMGKLAQAVMHGAKIIQID------GNFDDCLELARKMAADFPTISLVNSVNPvR 169
Cdd:PLN03013 186 TGIGLAFIAASRGYRLILTMP-ASMSMERRVLLKAFGAELVLTDpakgmtGAVQKAEEILKNTPDAYMLQQFDNPANP-K 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 170 IEGQKTAAfEIVDVLGTAPDVHALPVGNAGNITAYWKGYTEyhqlglidKLPRmlgTQAAGAAP-----LVLGEPVSHpe 244
Cdd:PLN03013 264 IHYETTGP-EIWDDTKGKVDIFVAGIGTGGTITGVGRFIKE--------KNPK---TQVIGVEPtesdiLSGGKPGPH-- 329
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663 245 tiataiRIGSPASWTSAVEAQQQSKGRFLAASDEEILAAYHLVARVEGVFVEPASAASIAGLLK 308
Cdd:PLN03013 330 ------KIQGIGAGFIPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIK 387
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
271-338 1.27e-04

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 43.52  E-value: 1.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 271 RFLAASDEEILAAYHLVARVEGVFvePA--SAASIAGLLKAIDDgwVARGSTVVCTVTGNGLKDPDTALK 338
Cdd:PRK04346 326 EYVSITDDEALEAFQLLSRLEGII--PAleSSHALAYALKLAPT--LGKDQIIVVNLSGRGDKDVFTVAK 391
PLN00011 PLN00011
cysteine synthase
21-308 2.50e-04

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 42.30  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  21 DRLPVGDDwtpVTLLEGGTPLIAATNLSKQTGCTIHLKVEGLNPTGSFKDRGMTMAVTDA-----LAHGQRAVLCASTGN 95
Cdd:PLN00011   3 DRCLIKND---VTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAedkglITPGKSTLIEATAGN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  96 TSASAAAYAARAGITCAVLIP-----QGKIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAADFPTISLVNSVNPvRI 170
Cdd:PLN00011  80 TGIGLACIGAARGYKVILVMPstmslERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANP-EI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 171 EGQKTAAFEIVDVLGTApDVHALPVGNAGNITAYWKGYTEYhqlgliDKLPRMLGTQAAGAAPLVLGEPVSH-PETIATA 249
Cdd:PLN00011 159 HYRTTGPEIWRDSAGKV-DILVAGVGTGGTATGVGKFLKEK------NKDIKVCVVEPVESAVLSGGQPGPHlIQGIGSG 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 114793663 250 IrIGSPASWTSAVEAQQqskgrflaASDEEILAAYHLVARVEGVFVEPASAASIAGLLK 308
Cdd:PLN00011 232 I-IPFNLDLTIVDEIIQ--------VTGEEAIETAKLLALKEGLLVGISSGAAAAAALK 281
PLN02618 PLN02618
tryptophan synthase, beta chain
185-338 5.43e-04

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 41.66  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 185 GTAPDVHALPVGNAGNITAYWKGYTEyhqlgliDKLPRMLGTQAAG--------AAPLVLGEP-VSH------------- 242
Cdd:PLN02618 237 GGKPDVLVACVGGGSNAMGLFHEFID-------DEDVRLIGVEAAGfgldsgkhAATLTKGEVgVLHgamsyllqdedgq 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663 243 ---PETIATAIR---IGSPASWTSAVEaqqqsKGRFLAASDEEILAAYHLVARVEGVFvePASAAS--IAGLLKAIDDgw 314
Cdd:PLN02618 310 iiePHSISAGLDypgVGPEHSFLKDTG-----RAEYYSVTDEEALEAFQRLSRLEGII--PALETShaLAYLEKLCPT-- 380
                        170       180
                 ....*....|....*....|....
gi 114793663 315 VARGSTVVCTVTGNGLKDPDTALK 338
Cdd:PLN02618 381 LPDGTKVVVNCSGRGDKDVNTAIK 404
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
39-154 1.93e-03

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 39.86  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114793663  39 TPLIAATNLSKQTGC-TIHLKVE----GLNptgSFKDRGMTMAVT----------------DALAHGQ-RAVL------C 90
Cdd:PRK08206  45 TPLVALPDLAAELGVgSILVKDEsyrfGLN---AFKALGGAYAVArllaeklgldiselsfEELTSGEvREKLgditfaT 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114793663  91 ASTGNTSASAAAYAARAGITCAVLIPQGkIAMGKLAQAVMHGAKIIQIDGNFDDCLELARKMAA 154
Cdd:PRK08206 122 ATDGNHGRGVAWAAQQLGQKAVIYMPKG-SSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQ 184
PRK12391 PRK12391
TrpB-like pyridoxal phosphate-dependent enzyme;
39-69 4.67e-03

TrpB-like pyridoxal phosphate-dependent enzyme;


Pssm-ID: 237087  Cd Length: 427  Bit Score: 38.62  E-value: 4.67e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 114793663  39 TPLIAATNLSK--QTGCTIHLKVEGLNPTGSFK 69
Cdd:PRK12391  78 TPLIRARRLEKalGTPAKIYYKYEGVSPTGSHK 110
 
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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