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Conserved domains on  [gi|446703728|ref|WP_000781074|]
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MULTISPECIES: threonine synthase [Enterobacteriaceae]

Protein Classification

threonine synthase( domain architecture ID 10107520)

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

EC:  4.2.3.1
Gene Ontology:  GO:0030170|GO:0004795

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
2-423 0e+00

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: 513.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   2 KLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEERVRAAFA 81
Cdd:cd01560    1 KYVSTRGGNPGVSFSEALLSGLAPDGGLYVPEELPKLSAEEIASWSGLSYQELAFEVLSLFIGDEIPEDDLKSLIDRAYS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  82 FPAPVA-----NVESDVGCLELFHGPTLAFKDFGGRFMAQMLTHIAGD--KPVTILTATSGDTGAAVAHAFYGLPNVKVV 154
Cdd:cd01560   81 FFRHPDiaplvQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrnERITILVATSGDTGSAAIEGFRGKPNVDVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 155 ILYPRGKISPLQEKLFCTLGG-NIETVAIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQL 233
Cdd:cd01560  161 VLYPKGGVSPIQELQMTTLPAdNVHVVAVEGDFDDCQSLVKALFADEDFNKKLKLSSANSINWARILAQIVYYFYAYLQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 234 PQE-TRNQLVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPK-ATQATLSNAMDVSQPNNWPR 311
Cdd:cd01560  241 LKRgEGEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGRYDRReSLKQTLSPAMDILKSSNFER 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 312 VEELFRRKIWQ-------------------------LKELGYAAVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQL 365
Cdd:cd01560  321 LLFLLAGRDRTkvkmlmeefeatgflslpkeelkklREDFSSGSVSDEETLETIREVyEETGYLIDPHTAVGVRAAERVR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 366 N-PGEYGLFLGTAHPAKFKESVEAILGETL-DLPKELAERADLPLLSHNLPADFAALRKL 423
Cdd:cd01560  401 KsPGTPGVVLSTAHPAKFPEAVKEALGEEPvELPEELEGLEDLEKRHEDLLADKELLKSH 460
 
Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
2-423 0e+00

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: 513.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   2 KLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEERVRAAFA 81
Cdd:cd01560    1 KYVSTRGGNPGVSFSEALLSGLAPDGGLYVPEELPKLSAEEIASWSGLSYQELAFEVLSLFIGDEIPEDDLKSLIDRAYS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  82 FPAPVA-----NVESDVGCLELFHGPTLAFKDFGGRFMAQMLTHIAGD--KPVTILTATSGDTGAAVAHAFYGLPNVKVV 154
Cdd:cd01560   81 FFRHPDiaplvQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrnERITILVATSGDTGSAAIEGFRGKPNVDVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 155 ILYPRGKISPLQEKLFCTLGG-NIETVAIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQL 233
Cdd:cd01560  161 VLYPKGGVSPIQELQMTTLPAdNVHVVAVEGDFDDCQSLVKALFADEDFNKKLKLSSANSINWARILAQIVYYFYAYLQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 234 PQE-TRNQLVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPK-ATQATLSNAMDVSQPNNWPR 311
Cdd:cd01560  241 LKRgEGEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGRYDRReSLKQTLSPAMDILKSSNFER 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 312 VEELFRRKIWQ-------------------------LKELGYAAVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQL 365
Cdd:cd01560  321 LLFLLAGRDRTkvkmlmeefeatgflslpkeelkklREDFSSGSVSDEETLETIREVyEETGYLIDPHTAVGVRAAERVR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 366 N-PGEYGLFLGTAHPAKFKESVEAILGETL-DLPKELAERADLPLLSHNLPADFAALRKL 423
Cdd:cd01560  401 KsPGTPGVVLSTAHPAKFPEAVKEALGEEPvELPEELEGLEDLEKRHEDLLADKELLKSH 460
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
52-398 6.47e-138

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: 397.91  E-value: 6.47e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   52 VTRSAKILSAFigdEIPQEILEERVRAAFAFPAPVANVESD-VGCLELFHGPTLAFKDFGgrfMAQMLTHIAGDKPVTIL 130
Cdd:TIGR00260   1 VWRYREFLPVT---EKDLVDLGEGVTPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRG---MAVALTKALELGNDTVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  131 TATSGDTGAAVAhAFYGLPNVKVVILYPRGKISplQEKLFCTLGGNIETVAIDGDFDACQALVKQAFDDeelKVALGLNS 210
Cdd:TIGR00260  75 CASTGNTGAAAA-AYAGKAGLKVVVLYPAGKIS--LGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFED---KPALGLNS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  211 ANSInISRLLAQICYYFEAVAQLPQETRNQLVVSVP-SGNFGDLTAGLLA-KSLG---LPVKRFIAATNVNDTVPRFLHD 285
Cdd:TIGR00260 149 ANSI-PYRLEGQKTYAFEAVEQLGWEAPDKVVVPVPnSGNFGAIWKGFKEkKMLGldsLPVKRGIQAEGAADIVRAFLEG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  286 GQWSPKATQATLSNAMDVSQPNNWPRVEELFRRKIWQLKELgyaaVDDETTQQTMRELKELGYTSEPHAAVAYRALRDQL 365
Cdd:TIGR00260 228 GQWEPIETPETLSTAMDIGNPANWPRALEAFRRSNGYAEDL----SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLV 303
                         330       340       350
                  ....*....|....*....|....*....|...
gi 446703728  366 NPgeyglflGTAHPAkfKESVEAILGETLDLPK 398
Cdd:TIGR00260 304 EK-------GTADPA--ERVVCALTGNGLKDPE 327
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
96-402 1.02e-69

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: 225.46  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  96 LELFHGPTLAFKDfggRFMAQMLTHIAGDKPVTILTATSGDTGAAVAhAFYGLPNVKVVILYPRGKISPLQEKLFCTLGg 175
Cdd:COG0498   86 KEEGHNPTGSFKD---RAMQVAVSLALERGAKTIVCASSGNGSAALA-AYAARAGIEVFVFVPEGKVSPGQLAQMLTYG- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 176 nIETVAIDGDFDACQALVKQAFDDEelkvalGLNSANSINISRLLAQICYYFEAVAQLpqeTRNQLVVSVPSGNFGDLTA 255
Cdd:COG0498  161 -AHVIAVDGNFDDAQRLVKELAADE------GLYAVNSINPARLEGQKTYAFEIAEQL---GRVPDWVVVPTGNGGNILA 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 256 GLLAK----SLGLPVK--RFIA--ATNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNWPRVeelfrrkiwqLKEL- 326
Cdd:COG0498  231 GYKAFkelkELGLIDRlpRLIAvqATGCNPILTAFETGRDEYEPERPETIAPSMDIGNPSNGERA----------LFALr 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 327 ---GYA-AVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQLNPGEYG-----LFLGTAHPAKFKESV-EAILGETLD 395
Cdd:COG0498  301 esgGTAvAVSDEEILEAIRLLaRREGIFVEPATAVAVAGLRKLREEGEIDpdepvVVLSTGHGLKFPDAVrEALGGEPLA 380

                 ....*..
gi 446703728 396 LPKELAE 402
Cdd:COG0498  381 VPPDLEA 387
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
96-365 8.38e-24

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: 100.46  E-value: 8.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   96 LELFHgPTLAFKDFGGRFMaqMLTHIAGDKPVTILTATSGDTGAAVAH--AFYGLpnvKVVILYPR----GKISPLQEkl 169
Cdd:pfam00291  28 LESLN-PTGSFKDRGALNL--LLRLKEGEGGKTVVEASSGNHGRALAAaaARLGL---KVTIVVPEdappGKLLLMRA-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  170 fctLGGNIetVAIDGDFDACQALVKQAFDDEElKVALGLNSANSINIsrlLAQICYYFEAVAQLPQETRnqlVVSVPSGN 249
Cdd:pfam00291 100 ---LGAEV--VLVGGDYDEAVAAARELAAEGP-GAYYINQYDNPLNI---EGYGTIGLEILEQLGGDPD---AVVVPVGG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  250 FGDLTAGLLAKSLGLPVKRFIAA-TNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNwPRVEELFRRKIWqlkelGY 328
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVePEGAPALARSLAAGRPVPVPVADTIADGLGVGDEPG-ALALDLLDEYVG-----EV 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 446703728  329 AAVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQL 365
Cdd:pfam00291 242 VTVSDEEALEAMRLLaRREGIVVEPSSAAALAALKLAL 279
PLN02569 PLN02569
threonine synthase
102-427 2.05e-16

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 81.01  E-value: 2.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 102 PTLAFKDFGGRFMAQMLTHIAG-DKPVT-ILTATSGDTGAAVAhAFYGLPNVKVVILYPRGKISPLQEKLFCTLGGNIet 179
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQVNRLRKmAKPVVgVGCASTGDTSAALS-AYCAAAGIPSIVFLPADKISIAQLVQPIANGALV-- 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 180 VAIDGDFDACQALVKQAfdDEELKVALglnsANSINISRLLAQICYYFEAVAQLPQETRNqlVVSVPSGNFGDLTA---G 256
Cdd:PLN02569 238 LSIDTDFDGCMRLIREV--TAELPIYL----ANSLNSLRLEGQKTAAIEILQQFDWEVPD--WVIVPGGNLGNIYAfykG 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 257 L-LAKSLGLpVKRF-----IAATNVNDTVpRFLHDG--QWSPKATQATLSNAMDVSQPNNwprveelFRRKIWQLKELG- 327
Cdd:PLN02569 310 FkMCKELGL-VDRLprlvcAQAANANPLY-RAYKSGweEFKPVKANPTFASAIQIGDPVS-------IDRAVYALKESNg 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 328 -YAAVDDETTQQTMRELKELGYTSEPHAAVAYRALRDQLNPGEYG-----LFLGTAHPAKFKESveAILGETLDLPKELA 401
Cdd:PLN02569 381 iVEEATEEELMDAQAEADKTGMFLCPHTGVALAALKKLRASGVIGptdrtVVVSTAHGLKFTQS--KIDYHSKEIPDMAC 458
                        330       340
                 ....*....|....*....|....*.
gi 446703728 402 ERADLPLlshNLPADFAALRKLMMNH 427
Cdd:PLN02569 459 RFANPPV---SVKADFGSVMDVLKKY 481
 
Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
2-423 0e+00

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: 513.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   2 KLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEERVRAAFA 81
Cdd:cd01560    1 KYVSTRGGNPGVSFSEALLSGLAPDGGLYVPEELPKLSAEEIASWSGLSYQELAFEVLSLFIGDEIPEDDLKSLIDRAYS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  82 FPAPVA-----NVESDVGCLELFHGPTLAFKDFGGRFMAQMLTHIAGD--KPVTILTATSGDTGAAVAHAFYGLPNVKVV 154
Cdd:cd01560   81 FFRHPDiaplvQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrnERITILVATSGDTGSAAIEGFRGKPNVDVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 155 ILYPRGKISPLQEKLFCTLGG-NIETVAIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQL 233
Cdd:cd01560  161 VLYPKGGVSPIQELQMTTLPAdNVHVVAVEGDFDDCQSLVKALFADEDFNKKLKLSSANSINWARILAQIVYYFYAYLQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 234 PQE-TRNQLVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPK-ATQATLSNAMDVSQPNNWPR 311
Cdd:cd01560  241 LKRgEGEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGRYDRReSLKQTLSPAMDILKSSNFER 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 312 VEELFRRKIWQ-------------------------LKELGYAAVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQL 365
Cdd:cd01560  321 LLFLLAGRDRTkvkmlmeefeatgflslpkeelkklREDFSSGSVSDEETLETIREVyEETGYLIDPHTAVGVRAAERVR 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 366 N-PGEYGLFLGTAHPAKFKESVEAILGETL-DLPKELAERADLPLLSHNLPADFAALRKL 423
Cdd:cd01560  401 KsPGTPGVVLSTAHPAKFPEAVKEALGEEPvELPEELEGLEDLEKRHEDLLADKELLKSH 460
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
52-398 6.47e-138

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: 397.91  E-value: 6.47e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   52 VTRSAKILSAFigdEIPQEILEERVRAAFAFPAPVANVESD-VGCLELFHGPTLAFKDFGgrfMAQMLTHIAGDKPVTIL 130
Cdd:TIGR00260   1 VWRYREFLPVT---EKDLVDLGEGVTPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRG---MAVALTKALELGNDTVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  131 TATSGDTGAAVAhAFYGLPNVKVVILYPRGKISplQEKLFCTLGGNIETVAIDGDFDACQALVKQAFDDeelKVALGLNS 210
Cdd:TIGR00260  75 CASTGNTGAAAA-AYAGKAGLKVVVLYPAGKIS--LGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFED---KPALGLNS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  211 ANSInISRLLAQICYYFEAVAQLPQETRNQLVVSVP-SGNFGDLTAGLLA-KSLG---LPVKRFIAATNVNDTVPRFLHD 285
Cdd:TIGR00260 149 ANSI-PYRLEGQKTYAFEAVEQLGWEAPDKVVVPVPnSGNFGAIWKGFKEkKMLGldsLPVKRGIQAEGAADIVRAFLEG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  286 GQWSPKATQATLSNAMDVSQPNNWPRVEELFRRKIWQLKELgyaaVDDETTQQTMRELKELGYTSEPHAAVAYRALRDQL 365
Cdd:TIGR00260 228 GQWEPIETPETLSTAMDIGNPANWPRALEAFRRSNGYAEDL----SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLV 303
                         330       340       350
                  ....*....|....*....|....*....|...
gi 446703728  366 NPgeyglflGTAHPAkfKESVEAILGETLDLPK 398
Cdd:TIGR00260 304 EK-------GTADPA--ERVVCALTGNGLKDPE 327
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
96-402 1.02e-69

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: 225.46  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  96 LELFHGPTLAFKDfggRFMAQMLTHIAGDKPVTILTATSGDTGAAVAhAFYGLPNVKVVILYPRGKISPLQEKLFCTLGg 175
Cdd:COG0498   86 KEEGHNPTGSFKD---RAMQVAVSLALERGAKTIVCASSGNGSAALA-AYAARAGIEVFVFVPEGKVSPGQLAQMLTYG- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 176 nIETVAIDGDFDACQALVKQAFDDEelkvalGLNSANSINISRLLAQICYYFEAVAQLpqeTRNQLVVSVPSGNFGDLTA 255
Cdd:COG0498  161 -AHVIAVDGNFDDAQRLVKELAADE------GLYAVNSINPARLEGQKTYAFEIAEQL---GRVPDWVVVPTGNGGNILA 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 256 GLLAK----SLGLPVK--RFIA--ATNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNWPRVeelfrrkiwqLKEL- 326
Cdd:COG0498  231 GYKAFkelkELGLIDRlpRLIAvqATGCNPILTAFETGRDEYEPERPETIAPSMDIGNPSNGERA----------LFALr 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 327 ---GYA-AVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQLNPGEYG-----LFLGTAHPAKFKESV-EAILGETLD 395
Cdd:COG0498  301 esgGTAvAVSDEEILEAIRLLaRREGIFVEPATAVAVAGLRKLREEGEIDpdepvVVLSTGHGLKFPDAVrEALGGEPLA 380

                 ....*..
gi 446703728 396 LPKELAE 402
Cdd:COG0498  381 VPPDLEA 387
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
96-378 5.03e-41

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: 145.74  E-value: 5.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  96 LELFHGPTLAFKDFGGRFMAQMLTHIAGDKPVTILTATSGDTGAAVAHAFYGLpNVKVVILYPRGKiSPLQEKLFCTLGG 175
Cdd:cd00640   20 KLEFLNPTGSFKDRGALNLILLAEEEGKLPKGVIIESTGGNTGIALAAAAARL-GLKCTIVMPEGA-SPEKVAQMRALGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 176 NIetVAIDGDFDACQALVKQAFDDEElkvalGLNSANS-INISRLLAQICYYFEAVAQLPQEtrNQLVVSVPSGNFGDLT 254
Cdd:cd00640   98 EV--VLVPGDFDDAIALAKELAEEDP-----GAYYVNQfDNPANIAGQGTIGLEILEQLGGQ--KPDAVVVPVGGGGNIA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 255 AGLLAKSLGLPVKRFIAATNvndtvprflhdgqwspkatqatlsnamdvsqpnnwprveelfrrkiwqlkelGYAAVDDE 334
Cdd:cd00640  169 GIARALKELLPNVKVIGVEP----------------------------------------------------EVVTVSDE 196
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446703728 335 TTQQTMREL-KELGYTSEPHAAVAYRA---LRDQLNPGEYGLFLGTAH 378
Cdd:cd00640  197 EALEAIRLLaREEGILVEPSSAAALAAalkLAKKLGKGKTVVVILTGG 244
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
96-365 8.38e-24

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: 100.46  E-value: 8.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728   96 LELFHgPTLAFKDFGGRFMaqMLTHIAGDKPVTILTATSGDTGAAVAH--AFYGLpnvKVVILYPR----GKISPLQEkl 169
Cdd:pfam00291  28 LESLN-PTGSFKDRGALNL--LLRLKEGEGGKTVVEASSGNHGRALAAaaARLGL---KVTIVVPEdappGKLLLMRA-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  170 fctLGGNIetVAIDGDFDACQALVKQAFDDEElKVALGLNSANSINIsrlLAQICYYFEAVAQLPQETRnqlVVSVPSGN 249
Cdd:pfam00291 100 ---LGAEV--VLVGGDYDEAVAAARELAAEGP-GAYYINQYDNPLNI---EGYGTIGLEILEQLGGDPD---AVVVPVGG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728  250 FGDLTAGLLAKSLGLPVKRFIAA-TNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNwPRVEELFRRKIWqlkelGY 328
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVePEGAPALARSLAAGRPVPVPVADTIADGLGVGDEPG-ALALDLLDEYVG-----EV 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 446703728  329 AAVDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQL 365
Cdd:pfam00291 242 VTVSDEEALEAMRLLaRREGIVVEPSSAAALAALKLAL 279
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
102-369 2.77e-17

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: 82.26  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 102 PTLAFKDfggRFMAQMLTHIAGDKPVTILTATSGDTGAAVAhAFYGLPNVKVVILYPRGKIsplQEKLFCTLGGNIETVA 181
Cdd:cd01563   49 PTGSFKD---RGMTVAVSKAKELGVKAVACASTGNTSASLA-AYAARAGIKCVVFLPAGKA---LGKLAQALAYGATVLA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 182 IDGDFDACQALVKQAFDDEelkvalGLNSANSINISRLLAQICYYFEAVAQLPQETRNQLVvsVPSGNFGDLTA---GLL 258
Cdd:cd01563  122 VEGNFDDALRLVRELAEEN------WIYLSNSLNPYRLEGQKTIAFEIAEQLGWEVPDYVV--VPVGNGGNITAiwkGFK 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 259 A-KSLGLPVK--RFIA--ATNVNDTVPRFL-HDGQWSPKATQATLSNAMDVSQPNNWPRVEELfrrkiwqLKEL-GYA-A 330
Cdd:cd01563  194 ElKELGLIDRlpRMVGvqAEGAAPIVRAFKeGKDDIEPVENPETIATAIRIGNPASGPKALRA-------VRESgGTAvA 266
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446703728 331 VDDETTQQTMREL-KELGYTSEPHAAVAYRALRDQLNPGE 369
Cdd:cd01563  267 VSDEEILEAQKLLaRTEGIFVEPASAASLAGLKKLREEGI 306
PLN02569 PLN02569
threonine synthase
102-427 2.05e-16

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 81.01  E-value: 2.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 102 PTLAFKDFGGRFMAQMLTHIAG-DKPVT-ILTATSGDTGAAVAhAFYGLPNVKVVILYPRGKISPLQEKLFCTLGGNIet 179
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQVNRLRKmAKPVVgVGCASTGDTSAALS-AYCAAAGIPSIVFLPADKISIAQLVQPIANGALV-- 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 180 VAIDGDFDACQALVKQAfdDEELKVALglnsANSINISRLLAQICYYFEAVAQLPQETRNqlVVSVPSGNFGDLTA---G 256
Cdd:PLN02569 238 LSIDTDFDGCMRLIREV--TAELPIYL----ANSLNSLRLEGQKTAAIEILQQFDWEVPD--WVIVPGGNLGNIYAfykG 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 257 L-LAKSLGLpVKRF-----IAATNVNDTVpRFLHDG--QWSPKATQATLSNAMDVSQPNNwprveelFRRKIWQLKELG- 327
Cdd:PLN02569 310 FkMCKELGL-VDRLprlvcAQAANANPLY-RAYKSGweEFKPVKANPTFASAIQIGDPVS-------IDRAVYALKESNg 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446703728 328 -YAAVDDETTQQTMRELKELGYTSEPHAAVAYRALRDQLNPGEYG-----LFLGTAHPAKFKESveAILGETLDLPKELA 401
Cdd:PLN02569 381 iVEEATEEELMDAQAEADKTGMFLCPHTGVALAALKKLRASGVIGptdrtVVVSTAHGLKFTQS--KIDYHSKEIPDMAC 458
                        330       340
                 ....*....|....*....|....*.
gi 446703728 402 ERADLPLlshNLPADFAALRKLMMNH 427
Cdd:PLN02569 459 RFANPPV---SVKADFGSVMDVLKKY 481
Thr_synth_N pfam14821
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ...
8-74 8.54e-13

Threonine synthase N terminus; This domain is found at the N-terminus of many threonine synthase enzymes.


Pssm-ID: 464335 [Multi-domain]  Cd Length: 79  Bit Score: 63.59  E-value: 8.54e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446703728    8 DHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEE 74
Cdd:pfam14821   7 GGAPPLSFEDALLKGLAPDGGLYVPEEIPQLSAEELASWRGLSYQELAFEVLSLFIGDDIPEEDLKA 73
 
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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