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Conserved domains on  [gi|18410191|ref|NP_565047|]
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Pyridoxal-5'-phosphate-dependent enzyme family protein [Arabidopsis thaliana]

Protein Classification

threonine synthase( domain architecture ID 11476960)

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:0009088|GO:0030170|GO:0004795
SCOP:  4000798

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02569 PLN02569
threonine synthase
30-513 0e+00

threonine synthase


:

Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 983.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   30 TVRCTSASPAVPPQTPQKPRRSPDENIRDEARRR-PHQLQNLSARYVPFNAPPSSTESYSLDEIVYRSQSGALLDVQHDF 108
Cdd:PLN02569   1 VASVTRAVISDPPPIKSATKFTADENIRDEARRGpPAPPDEFSAKYVPFLECPLTGEKYSLDEVVYRSKSGGLLDVRHDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  109 AALKRYDGEFWRNLFDSRVGKTNWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQYLQMNDLWVKHCGIS 188
Cdd:PLN02569  81 EALKRYDGKYWRALFDSRVGKTTWPYGSGVWSKKEWVLPEIDDDDIVSLFEGNSNLFWAERLGKEFLGMNDLWVKHCGIS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  189 HTGSFKDLGMSVLVSQVNRLRKMNKPVIGVGCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSI 268
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQVNRLRKMAKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  269 DTDFDGCMHLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVD 348
Cdd:PLN02569 241 DTDFDGCMRLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFDWEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  349 RIPRLVCAQAANANPLYLHYKSGFkEDFNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATALADS 428
Cdd:PLN02569 321 RLPRLVCAQAANANPLYRAYKSGW-EEFKPVKANPTFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDAQAEADK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  429 TGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLKFTQSKIDYHSKNIKEMACRLANPPVKVKAKFGSVMDVLK 508
Cdd:PLN02569 400 TGMFLCPHTGVALAALKKLRASGVIGPTDRTVVVSTAHGLKFTQSKIDYHSKEIPDMACRFANPPVSVKADFGSVMDVLK 479

                 ....*
gi 18410191  509 EYLKS 513
Cdd:PLN02569 480 KYLSL 484
 
Name Accession Description Interval E-value
PLN02569 PLN02569
threonine synthase
30-513 0e+00

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 983.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   30 TVRCTSASPAVPPQTPQKPRRSPDENIRDEARRR-PHQLQNLSARYVPFNAPPSSTESYSLDEIVYRSQSGALLDVQHDF 108
Cdd:PLN02569   1 VASVTRAVISDPPPIKSATKFTADENIRDEARRGpPAPPDEFSAKYVPFLECPLTGEKYSLDEVVYRSKSGGLLDVRHDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  109 AALKRYDGEFWRNLFDSRVGKTNWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQYLQMNDLWVKHCGIS 188
Cdd:PLN02569  81 EALKRYDGKYWRALFDSRVGKTTWPYGSGVWSKKEWVLPEIDDDDIVSLFEGNSNLFWAERLGKEFLGMNDLWVKHCGIS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  189 HTGSFKDLGMSVLVSQVNRLRKMNKPVIGVGCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSI 268
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQVNRLRKMAKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  269 DTDFDGCMHLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVD 348
Cdd:PLN02569 241 DTDFDGCMRLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFDWEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  349 RIPRLVCAQAANANPLYLHYKSGFkEDFNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATALADS 428
Cdd:PLN02569 321 RLPRLVCAQAANANPLYRAYKSGW-EEFKPVKANPTFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDAQAEADK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  429 TGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLKFTQSKIDYHSKNIKEMACRLANPPVKVKAKFGSVMDVLK 508
Cdd:PLN02569 400 TGMFLCPHTGVALAALKKLRASGVIGPTDRTVVVSTAHGLKFTQSKIDYHSKEIPDMACRFANPPVSVKADFGSVMDVLK 479

                 ....*
gi 18410191  509 EYLKS 513
Cdd:PLN02569 480 KYLSL 484
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
139-470 6.27e-155

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: 444.34  E-value: 6.27e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 139 WSKKEWVLPeIDDDDIVSAFEGNSNLFWAERFGKQyLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRkmnkpVIGV 218
Cdd:cd01563   1 LWRYRELLP-VTEDDIVSLGEGNTPLVRAPRLGER-LGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELG-----VKAV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 219 GCASTGDTSAALSAYCASAGIPSIVFLPADKiSMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSLR 298
Cdd:cd01563  74 ACASTGNTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLNPYR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 299 LEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPLYLHYKSGfKEDFNP 378
Cdd:cd01563 153 LEGQKTIAFEIAEQLGWEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAFKEG-KDDIEP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 379 LKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATALADST-GMFICPHTGVALTALMKLRKSGVIGAND 457
Cdd:cd01563 232 VENPETIATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTeGIFVEPASAASLAGLKKLREEGIIDKGE 311
                       330
                ....*....|...
gi 18410191 458 RTVVVSTAHGLKF 470
Cdd:cd01563 312 RVVVVLTGHGLKD 324
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
125-509 1.14e-139

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: 408.05  E-value: 1.14e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 125 SRVGKTNWPYGSGVWSKKEWvLPEIDDDDIVSAFEGNSNLFWAERFGKQYlqMNDLWVKHCGISHTGSFKDLGMSVLVSq 204
Cdd:COG0498  31 PALSREDLASRRGLWRYREL-LPFDDEEKAVSLGEGGTPLVKAPRLADEL--GKNLYVKEEGHNPTGSFKDRAMQVAVS- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 205 vnRLRKMNKPVIGvgCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTA 284
Cdd:COG0498 107 --LALERGAKTIV--CASSGNGSAALAAYAARAGIEVFVFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAA 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 285 ELPIYLANSLNSLRLEGQKTAAIEILQQFNwQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPL 364
Cdd:COG0498 183 DEGLYAVNSINPARLEGQKTYAFEIAEQLG-RVPDWVVVPTGNGGNILAGYKAFKELKELGLIDRLPRLIAVQATGCNPI 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 365 YLHYKSGfKEDFNPLKANTTfASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTA 443
Cdd:COG0498 262 LTAFETG-RDEYEPERPETI-APSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRlLARREGIFVEPATAVAVAG 339
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18410191 444 LMKLRKSGVIGANDRTVVVSTAHGLKFTQSKIDYHSKNikemacrlanpPVKVKAKFGSVMDVLKE 509
Cdd:COG0498 340 LRKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE-----------PLAVPPDLEAVKAAVEE 394
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
138-469 3.86e-82

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: 258.47  E-value: 3.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   138 VWSKKEwVLPEIDDDdIVSAFEGNSNLFWAERFGKQyLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRkmnkpVIG 217
Cdd:TIGR00260   1 VWRYRE-FLPVTEKD-LVDLGEGVTPLFRAPALAAN-VGIKNLYVKELGHNPTLSFKDRGMAVALTKALELG-----NDT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   218 VGCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSL 297
Cdd:TIGR00260  73 VLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   298 --RLEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLvDRIPRLVCAQAANANPLYLHYKSGfkED 375
Cdd:TIGR00260 153 pyRLEGQKTYAFEAVEQLGWEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGL-DSLPVKRGIQAEGAADIVRAFLEG--GQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   376 FNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTALMKLRKSGVIG 454
Cdd:TIGR00260 230 WEPIETPETLSTAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKlLAREEGYFVEPHSAVAVAALLKLVEKGTAD 309
                         330
                  ....*....|....*
gi 18410191   455 ANDRTVVVSTAHGLK 469
Cdd:TIGR00260 310 PAERVVCALTGNGLK 324
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
155-464 3.20e-54

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: 184.44  E-value: 3.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   155 VSAFEGNSNLFWAERFGKQYLQmnDLWVKHCGISHTGSFKDLGMSVLVSQVNRlrkmNKPVIGVGCASTGDTSAALSAYC 234
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGV--DVYLKLESLNPTGSFKDRGALNLLLRLKE----GEGGKTVVEASSGNHGRALAAAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   235 ASAGIPSIVFLPAD----KISMAQLVqpianGAFVLSIDTDFDGCMHLIREVTAELP--IYLANSLNSLRLEGQKTAAIE 308
Cdd:pfam00291  75 ARLGLKVTIVVPEDappgKLLLMRAL-----GAEVVLVGGDYDEAVAAARELAAEGPgaYYINQYDNPLNIEGYGTIGLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   309 ILQQFNwQVPDWVIVPGGNLGNIYAFYKGFhmcKELGlvdRIPRLVCAQAANANPLylhYKSGFKEDFNPLKANTTFASA 388
Cdd:pfam00291 150 ILEQLG-GDPDAVVVPVGGGGLIAGIARGL---KELG---PDVRVIGVEPEGAPAL---ARSLAAGRPVPVPVADTIADG 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18410191   389 IQIGDPVSiDRAVYALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTALmKLRKSGVIGANDRTVVVST 464
Cdd:pfam00291 220 LGVGDEPG-ALALDLLDEYVGEVVTVSDEEALEAMRlLARREGIVVEPSSAAALAAL-KLALAGELKGGDRVVVVLT 294
 
Name Accession Description Interval E-value
PLN02569 PLN02569
threonine synthase
30-513 0e+00

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 983.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   30 TVRCTSASPAVPPQTPQKPRRSPDENIRDEARRR-PHQLQNLSARYVPFNAPPSSTESYSLDEIVYRSQSGALLDVQHDF 108
Cdd:PLN02569   1 VASVTRAVISDPPPIKSATKFTADENIRDEARRGpPAPPDEFSAKYVPFLECPLTGEKYSLDEVVYRSKSGGLLDVRHDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  109 AALKRYDGEFWRNLFDSRVGKTNWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQYLQMNDLWVKHCGIS 188
Cdd:PLN02569  81 EALKRYDGKYWRALFDSRVGKTTWPYGSGVWSKKEWVLPEIDDDDIVSLFEGNSNLFWAERLGKEFLGMNDLWVKHCGIS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  189 HTGSFKDLGMSVLVSQVNRLRKMNKPVIGVGCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSI 268
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQVNRLRKMAKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  269 DTDFDGCMHLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVD 348
Cdd:PLN02569 241 DTDFDGCMRLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFDWEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  349 RIPRLVCAQAANANPLYLHYKSGFkEDFNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATALADS 428
Cdd:PLN02569 321 RLPRLVCAQAANANPLYRAYKSGW-EEFKPVKANPTFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDAQAEADK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  429 TGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLKFTQSKIDYHSKNIKEMACRLANPPVKVKAKFGSVMDVLK 508
Cdd:PLN02569 400 TGMFLCPHTGVALAALKKLRASGVIGPTDRTVVVSTAHGLKFTQSKIDYHSKEIPDMACRFANPPVSVKADFGSVMDVLK 479

                 ....*
gi 18410191  509 EYLKS 513
Cdd:PLN02569 480 KYLSL 484
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
139-470 6.27e-155

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: 444.34  E-value: 6.27e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 139 WSKKEWVLPeIDDDDIVSAFEGNSNLFWAERFGKQyLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRkmnkpVIGV 218
Cdd:cd01563   1 LWRYRELLP-VTEDDIVSLGEGNTPLVRAPRLGER-LGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELG-----VKAV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 219 GCASTGDTSAALSAYCASAGIPSIVFLPADKiSMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSLR 298
Cdd:cd01563  74 ACASTGNTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLNPYR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 299 LEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPLYLHYKSGfKEDFNP 378
Cdd:cd01563 153 LEGQKTIAFEIAEQLGWEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAFKEG-KDDIEP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 379 LKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATALADST-GMFICPHTGVALTALMKLRKSGVIGAND 457
Cdd:cd01563 232 VENPETIATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTeGIFVEPASAASLAGLKKLREEGIIDKGE 311
                       330
                ....*....|...
gi 18410191 458 RTVVVSTAHGLKF 470
Cdd:cd01563 312 RVVVVLTGHGLKD 324
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
125-509 1.14e-139

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: 408.05  E-value: 1.14e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 125 SRVGKTNWPYGSGVWSKKEWvLPEIDDDDIVSAFEGNSNLFWAERFGKQYlqMNDLWVKHCGISHTGSFKDLGMSVLVSq 204
Cdd:COG0498  31 PALSREDLASRRGLWRYREL-LPFDDEEKAVSLGEGGTPLVKAPRLADEL--GKNLYVKEEGHNPTGSFKDRAMQVAVS- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 205 vnRLRKMNKPVIGvgCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTA 284
Cdd:COG0498 107 --LALERGAKTIV--CASSGNGSAALAAYAARAGIEVFVFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAA 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 285 ELPIYLANSLNSLRLEGQKTAAIEILQQFNwQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPL 364
Cdd:COG0498 183 DEGLYAVNSINPARLEGQKTYAFEIAEQLG-RVPDWVVVPTGNGGNILAGYKAFKELKELGLIDRLPRLIAVQATGCNPI 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 365 YLHYKSGfKEDFNPLKANTTfASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTA 443
Cdd:COG0498 262 LTAFETG-RDEYEPERPETI-APSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRlLARREGIFVEPATAVAVAG 339
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18410191 444 LMKLRKSGVIGANDRTVVVSTAHGLKFTQSKIDYHSKNikemacrlanpPVKVKAKFGSVMDVLKE 509
Cdd:COG0498 340 LRKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE-----------PLAVPPDLEAVKAAVEE 394
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
138-469 3.86e-82

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: 258.47  E-value: 3.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   138 VWSKKEwVLPEIDDDdIVSAFEGNSNLFWAERFGKQyLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRkmnkpVIG 217
Cdd:TIGR00260   1 VWRYRE-FLPVTEKD-LVDLGEGVTPLFRAPALAAN-VGIKNLYVKELGHNPTLSFKDRGMAVALTKALELG-----NDT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   218 VGCASTGDTSAALSAYCASAGIPSIVFLPADKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSL 297
Cdd:TIGR00260  73 VLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   298 --RLEGQKTAAIEILQQFNWQVPDWVIVPGGNLGNIYAFYKGFHMCKELGLvDRIPRLVCAQAANANPLYLHYKSGfkED 375
Cdd:TIGR00260 153 pyRLEGQKTYAFEAVEQLGWEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGL-DSLPVKRGIQAEGAADIVRAFLEG--GQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   376 FNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTALMKLRKSGVIG 454
Cdd:TIGR00260 230 WEPIETPETLSTAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKlLAREEGYFVEPHSAVAVAALLKLVEKGTAD 309
                         330
                  ....*....|....*
gi 18410191   455 ANDRTVVVSTAHGLK 469
Cdd:TIGR00260 310 PAERVVCALTGNGLK 324
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
164-466 2.91e-56

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: 188.11  E-value: 2.91e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 164 LFWAERFGKQYLqmNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRKMNKPVIGvgCASTGDTSAALSAYCASAGIPSIV 243
Cdd:cd00640   3 LVRLKRLSKLGG--ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGVII--ESTGGNTGIALAAAAARLGLKCTI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 244 FLPADKiSMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELP-IYLANS-LNSLRLEGQKTAAIEILQQFNWQVPDWV 321
Cdd:cd00640  79 VMPEGA-SPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPgAYYVNQfDNPANIAGQGTIGLEILEQLGGQKPDAV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 322 IVPGGNLGNIYAFYKGFhmcKELGlvdRIPRLVCAQAananplylhyksgfkedfnplkanttfasaiqigdpvsidrav 401
Cdd:cd00640 158 VVPVGGGGNIAGIARAL---KELL---PNVKVIGVEP------------------------------------------- 188
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18410191 402 yalkksngIVEEATEEELMDAT-ALADSTGMFICPHTGVALTALMKLRKSGviGANDRTVVVSTAH 466
Cdd:cd00640 189 --------EVVTVSDEEALEAIrLLAREEGILVEPSSAAALAAALKLAKKL--GKGKTVVVILTGG 244
PRK08197 PRK08197
threonine synthase; Validated
85-470 1.00e-55

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 191.37  E-value: 1.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   85 ESYSLDEIVYRSQSGALLDVQHDFAALKRydgEFWRNLFDSRvGKTNWPYGSgvwskkewVLPEIDDDDIVSAFEGNSNL 164
Cdd:PRK08197  15 ETYDADQVHNLCKCGKPLLVRYDLEAVKQ---AVTREALAGR-PANLWRYHE--------LLPVRDPEHIVSLGEGMTPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  165 FWAERFGKQyLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLRkmnkpVIGVGCASTGDTSAALSAYCASAGIPSIVF 244
Cdd:PRK08197  83 LPLPRLGKA-LGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELG-----VKHLAMPTNGNAGAAWAAYAARAGIRATIF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  245 LPADkISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNS-LRLEGQKTAAIEILQQFNWQVPDWVIV 323
Cdd:PRK08197 157 MPAD-APEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEpYRIEGKKTMGLELAEQLGWRLPDVILY 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  324 P-GGNLGNIyAFYKGFHMCKELGLVD-RIPRLVCAQAANANPLYLHYKSGfKEDFNPLKANTTFASAIQIgdPVSI-DRA 400
Cdd:PRK08197 236 PtGGGVGLI-GIWKAFDELEALGWIGgKRPRLVAVQAEGCAPIVKAWEEG-KEESEFWEDAHTVAFGIRV--PKALgDFL 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18410191  401 VY-ALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLKF 470
Cdd:PRK08197 312 VLdAVRETGGCAIAVSDDAILAAQReLAREEGLFACPEGAATFAAARQLRESGWLKGDERVVLFNTGSGLKY 383
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
155-464 3.20e-54

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: 184.44  E-value: 3.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   155 VSAFEGNSNLFWAERFGKQYLQmnDLWVKHCGISHTGSFKDLGMSVLVSQVNRlrkmNKPVIGVGCASTGDTSAALSAYC 234
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGV--DVYLKLESLNPTGSFKDRGALNLLLRLKE----GEGGKTVVEASSGNHGRALAAAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   235 ASAGIPSIVFLPAD----KISMAQLVqpianGAFVLSIDTDFDGCMHLIREVTAELP--IYLANSLNSLRLEGQKTAAIE 308
Cdd:pfam00291  75 ARLGLKVTIVVPEDappgKLLLMRAL-----GAEVVLVGGDYDEAVAAARELAAEGPgaYYINQYDNPLNIEGYGTIGLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   309 ILQQFNwQVPDWVIVPGGNLGNIYAFYKGFhmcKELGlvdRIPRLVCAQAANANPLylhYKSGFKEDFNPLKANTTFASA 388
Cdd:pfam00291 150 ILEQLG-GDPDAVVVPVGGGGLIAGIARGL---KELG---PDVRVIGVEPEGAPAL---ARSLAAGRPVPVPVADTIADG 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18410191   389 IQIGDPVSiDRAVYALKKSNGIVEEATEEELMDATA-LADSTGMFICPHTGVALTALmKLRKSGVIGANDRTVVVST 464
Cdd:pfam00291 220 LGVGDEPG-ALALDLLDEYVGEVVTVSDEEALEAMRlLARREGIVVEPSSAAALAAL-KLALAGELKGGDRVVVVLT 294
PRK05638 PRK05638
threonine synthase; Validated
91-469 2.72e-48

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 172.69  E-value: 2.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   91 EIVYRSQSGALLDVQHDFAALkryDGEFWRNlfdsrvgktnwpYGSGVWSKKEwVLPEIDDddIVSAFEGNSNLFWA--- 167
Cdd:PRK05638  14 YIPPFCICGELLEIIYDYSSV---DVRKWKN------------RDPGVWRYKE-LLPQVKK--IISLGEGGTPLIRAris 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  168 ERFGKqylqmnDLWVKHCGISHTGSFKDLGMSVLVSqvNRLRKMNKPVIgvgCASTGDTSAALSAYCASAGIPSIVFLPA 247
Cdd:PRK05638  76 EKLGE------NVYIKDETRNPTGSFRDRLATVAVS--YGLPYAANGFI---VASDGNAAASVAAYSARAGKEAFVVVPR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  248 dKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSL-NSLRLEGQKTAAIEILQQFNwqvPDWVIVPGG 326
Cdd:PRK05638 145 -KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEyNIIGLEGQKTIAFELWEEIN---PTHVIVPTG 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  327 NLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPLYLHYKSgfkedfNPLKANTTFASAIQIGDPVSIDRAVYALKK 406
Cdd:PRK05638 221 SGSYLYSIYKGFKELLEIGVIEEIPKLIAVQTERCNPIASEILG------NKTKCNETKALGLYVKNPVMKEYVSEAIKE 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18410191  407 SNGIVEEATEEELMDATALADSTGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLK 469
Cdd:PRK05638 295 SGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTGSGLK 357
PRK08329 PRK08329
threonine synthase; Validated
190-469 1.10e-26

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 110.69  E-value: 1.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  190 TGSFKDLGMSVLVSQVNRLrKMNKPVIGvgcaSTGDTSAALSAYCASAGIPSIVFLPAD----KISMAQLVqpianGAFV 265
Cdd:PRK08329  84 TGSFKDRGTYVTVAKLKEE-GINEVVID----SSGNAALSLALYSLSEGIKVHVFVSYNaskeKISLLSRL-----GAEL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  266 LSIDTDFdgcMHLIREVTA----ELPIYLANSLNSLRLEGQKTAAIEILQQFNwqVPDWVIVPGGNLGNIYAFYKGFHMC 341
Cdd:PRK08329 154 HFVEGDR---MEVHEEAVKfskrNNIPYVSHWLNPYFLEGTKTIAYEIYEQIG--VPDYAFVPVGSGTLFLGIWKGFKEL 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  342 KELGLVDRIPRLVCAQAananplylhykSGFKEDFNPLKANTTFASAIQIGDPVSIDRAVYALKKSNGIVEEATEEELMD 421
Cdd:PRK08329 229 HEMGEISKMPKLVAVQA-----------EGYESLCKRSKSENKLADGIAIPEPPRKEEMLRALEESNGFCISVGEEETRA 297
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18410191  422 ATALADSTGMFICPHTGVALTALMKLRKSGVIGANDRTVVVSTAHGLK 469
Cdd:PRK08329 298 ALHWLRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLK 345
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
190-505 1.45e-23

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: 103.47  E-value: 1.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 190 TGSFKDLGMSVLVSQVNR-LRKMNKPVIGVGcASTGDT-SAALSAYcasAGIPSI---VFLPADKIS---MAQLV-QPIA 260
Cdd:cd01560 107 TLAFKDMALQFLGRLLEYfLKRRNERITILV-ATSGDTgSAAIEGF---RGKPNVdvvVLYPKGGVSpiqELQMTtLPAD 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 261 NGaFVLSIDTDFDGCMHLIREVTAE------LPIYLANSLNSLRLEGQKT----AAIEILQQFNWQVPDwVIVPGGNLGN 330
Cdd:cd01560 183 NV-HVVAVEGDFDDCQSLVKALFADedfnkkLKLSSANSINWARILAQIVyyfyAYLQLLKRGEGEKVE-FSVPTGNFGN 260
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 331 IYAFYkgfhMCKELGLvdRIPRLVCAQAANaNPLYLHYKSGfkeDFNP---LKAntTFASAIQIGDPVSIDRAVYAL--- 404
Cdd:cd01560 261 ILAGY----YAKKMGL--PIKKLIVATNEN-DVLRRFFKTG---RYDRresLKQ--TLSPAMDILKSSNFERLLFLLagr 328
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 405 --------------------------KKSNGIV-EEATEEELMDATA-LADSTGMFICPHTGVALTALMKLRKSgvigAN 456
Cdd:cd01560 329 drtkvkmlmeefeatgflslpkeelkKLREDFSsGSVSDEETLETIReVYEETGYLIDPHTAVGVRAAERVRKS----PG 404
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 18410191 457 DRTVVVSTAHGLKFTQSkidyhsknIKEMacrLANPPVKVKAKFGSVMD 505
Cdd:cd01560 405 TPGVVLSTAHPAKFPEA--------VKEA---LGEEPVELPEELEGLED 442
PRK06450 PRK06450
threonine synthase; Validated
99-469 1.81e-23

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 101.35  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191   99 GALLDVQHDFaalkrydgEFWRNLfdsrvGKTNWPYgsgvwsKKEWVlpeiddddivSAFEGNSNLFwaerfgkqylQMN 178
Cdd:PRK06450  25 GGPFEILIDF--------EFDKNL-----ERKNFPY------IKHFI----------SLGEGRTPLI----------KKG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  179 DLWVKHCGISHTGSFKDLGMSVLVSQVNRLRkmnkpVIGVGCASTGDTSAALSAYCASAGIPSIVFLPaDKISMAQLVQP 258
Cdd:PRK06450  66 NIWFKLDFLNPTGSYKDRGSVTLISYLAEKG-----IKQISEDSSGNAGASIAAYGAAAGIEVKIFVP-ETASGGKLKQI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  259 IANGAFVLSIDTDFDgcmhlirEVTAELP----IYLANSLNSLRLEGQKTAAIEILQQFNWQVPDWVIVP--GGNLgnIY 332
Cdd:PRK06450 140 ESYGAEVVRVRGSRE-------DVAKAAEnsgyYYASHVLQPQFRDGIRTLAYEIAKDLDWKIPNYVFIPvsAGTL--LL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  333 AFYKGFHMCKELGLVDRIPRLVCAQAANANPLYLHYKsgfKEDFNPLKANTTFASAIQIGDPVSIDRAVYALKKsNGIVE 412
Cdd:PRK06450 211 GVYSGFKHLLDSGVISEMPKIVAVQTEQVSPLCAKFK---GISYTPPDKVTSIADALVSTRPFLLDYMVKALSE-YGECI 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18410191  413 EATEEELMDATALADSTGMFICPHTGVALTALMKLRKsgviganDRTVVVSTAHGLK 469
Cdd:PRK06450 287 VVSDNEIVEAWKELAKKGLLVEYSSATVYAAYKKYSV-------NDSVLVLTGSGLK 336
PRK06381 PRK06381
threonine synthase; Validated
160-464 1.19e-22

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 98.62  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  160 GNSNLFWAERFGKqYLQMNDLWVKHCGISHTGSFKDLGMSVLVSQVNRLrKMNkpviGVGCASTGDTSAALSAYCASAGI 239
Cdd:PRK06381  14 GGTPLLRARKLEE-ELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRL-GYS----GITVGTCGNYGASIAYFARLYGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  240 PSIVFLPAdKISMAQLVQPIANGAFVLSIDTDFDGCMHLIREVTAELPIYLAN--SLNS-LRLEGQKTAAIEILQQFNwQ 316
Cdd:PRK06381  88 KAVIFIPR-SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANpgSVNSvVDIEAYSAIAYEIYEALG-D 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  317 VPDWVIVPGGNLGNIYAFYKGFHMCKELGLVDRIPRLVCAQAANANPLYLHYKSGFKE--DFNPLKANTTfasaiQIGDP 394
Cdd:PRK06381 166 VPDAVAVPVGNGTTLAGIYHGFRRLYDRGKTSRMPRMIGVSTSGGNQIVESFKRGSSEvvDLEVDEIRET-----AVNEP 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18410191  395 -VSI-----DRAVYALKKSNGIVEEATEEELMD-ATALADSTGMFICPHTGVALTALMKLRKSGviGANDRTVVVST 464
Cdd:PRK06381 241 lVSYrsfdgDNALEAIYDSHGYAFGFSDDEMVKyAELLRRMEGLNALPASASALAALVKYLKKN--GVNDNVVAVIT 315
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
168-462 1.72e-11

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: 65.20  E-value: 1.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 168 ERFGKQ-YLQMNDLwvkhcgiSHTGSFKDLGMSVLVSQvnrLRKMNKPViGVGCASTGDTSAALSAYCASAGIPSIVFLP 246
Cdd:cd01562  28 ELLGAEvYLKCENL-------QKTGSFKIRGAYNKLLS---LSEEERAK-GVVAASAGNHAQGVAYAAKLLGIPATIVMP 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 247 AD----KISMAQlvqpiANGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSLR-LEGQKTAAIEILQqfnwQVP--D 319
Cdd:cd01562  97 ETapaaKVDATR-----AYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDvIAGQGTIGLEILE----QVPdlD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 320 WVIVP---GGNLGNIYAFYKGFHmckelglvdriP--RLVCAQAANANPLYLHYKSGFKEdfnPLKANTTFASAIQIGDP 394
Cdd:cd01562 168 AVFVPvggGGLIAGIATAVKALS-----------PntKVIGVEPEGAPAMAQSLAAGKPV---TLPEVDTIADGLAVKRP 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18410191 395 vsiDRAVYALKKSN--GIVeEATEEELMDATALADSTGMFICPHTG-VALTALMklrkSGVIGANDRTVVV 462
Cdd:cd01562 234 ---GELTFEIIRKLvdDVV-TVSEDEIAAAMLLLFEREKLVAEPAGaLALAALL----SGKLDLKGKKVVV 296
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
167-462 8.78e-08

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: 53.89  E-value: 8.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 167 AERFGkqylqmNDLWVKHCGISHTGSFKDLGMSVLVSQVNRlrkmNKPVIGVGCASTGDTSAALsAYCASA-GIPSIVFL 245
Cdd:COG1171  34 SERLG------AEVYLKLENLQPTGSFKLRGAYNALASLSE----EERARGVVAASAGNHAQGV-AYAARLlGIPATIVM 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 246 PAD----KISMAQlvqpiANGAFVLSIDTDFDGCMHLIREVTAElpiylanslNSLRL----------EGQKTAAIEILQ 311
Cdd:COG1171 103 PETapavKVAATR-----AYGAEVVLHGDTYDDAEAAAAELAEE---------EGATFvhpfddpdviAGQGTIALEILE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191 312 QfnWQVPDWVIVP--GGNL--GNIYAFykgfhmcKELGlvDRIpRLVCAQAANANPLYLHYKSGFKEDfnpLKANTTFAS 387
Cdd:COG1171 169 Q--LPDLDAVFVPvgGGGLiaGVAAAL-------KALS--PDI-RVIGVEPEGAAAMYRSLAAGEPVT---LPGVDTIAD 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18410191 388 AIQIGDPVSIDRAVyALKKSNGIVeEATEEELMDATA-LADSTGMfICPHTG-VALTALMKLRksgvIGANDRTVVV 462
Cdd:COG1171 234 GLAVGRPGELTFEI-LRDLVDDIV-TVSEDEIAAAMRlLLERTKI-VVEPAGaAALAALLAGK----ERLKGKRVVV 303
PRK06815 PRK06815
threonine/serine dehydratase;
179-328 1.60e-06

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 50.08  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  179 DLWVKHCGISHTGSFKDLGMSvlvsqvNRLRKMNKPV--IGVGCASTGDTSAALSAYCASAGIPSIVFLPADkISMAQLV 256
Cdd:PRK06815  36 EVYLKCEHLQHTGSFKFRGAS------NKLRLLNEAQrqQGVITASSGNHGQGVALAAKLAGIPVTVYAPEQ-ASAIKLD 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18410191  257 QPIANGAFVLSIDTDFDGC-MHLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQqfnwQVPD----WVIVPGGNL 328
Cdd:PRK06815 109 AIRALGAEVRLYGGDALNAeLAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVE----QQPDldavFVAVGGGGL 181
PRK08246 PRK08246
serine/threonine dehydratase;
180-337 2.37e-06

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 49.57  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  180 LWVKHCGISHTGSFKDLGMsvlvsqVNRLRKMNKPVIGVGCASTGDTSAALSAYCASAGIPSIVFLPAdkISMAQLVQPI 259
Cdd:PRK08246  39 VWLKLEHLQHTGSFKARGA------FNRLLAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPE--TAPPAKVARL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  260 -ANGAFVLSIDTDFDGCMHLIREVTAE---LPIYLANslNSLRLEGQKTAAIEILQqfnwQVPD----WVIVPGGNL-GN 330
Cdd:PRK08246 111 rALGAEVVVVGAEYADALEAAQAFAAEtgaLLCHAYD--QPEVLAGAGTLGLEIEE----QAPGvdtvLVAVGGGGLiAG 184

                 ....*..
gi 18410191  331 IYAFYKG 337
Cdd:PRK08246 185 IAAWFEG 191
PRK08813 PRK08813
threonine dehydratase; Provisional
164-427 3.77e-05

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 45.77  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  164 LFWAERFGkqylqmndLWVKHCGISHTGSFKDLG-MSVLVsqVNRLRKMNKPVIgvgCASTGDTS--AALSAYcaSAGIP 240
Cdd:PRK08813  42 LHYAERFG--------VWLKLENLQRTGSYKVRGaLNALL--AGLERGDERPVI---CASAGNHAqgVAWSAY--RLGVQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  241 SIVFLP--ADKISMAQLVQPianGAFVLSIDTDFDGCMHLIREVTAELPIYLANSLNSLR-LEGQKTAAIEILQqfnwQV 317
Cdd:PRK08813 107 AITVMPhgAPQTKIAGVAHW---GATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDvIAGQGTVGIELAA----HA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  318 PDWVIVP--GGNLGNIYAfykgfhmckeLGLVDRIPRLVCAQAANANPLylhyKSGFKEDFNPLKANTTFASAIQIGDPV 395
Cdd:PRK08813 180 PDVVIVPigGGGLASGVA----------LALKSQGVRVVGAQVEGVDSM----ARAIRGDLREIAPVATLADGVKVKIPG 245
                        250       260       270
                 ....*....|....*....|....*....|...
gi 18410191  396 SIDRAVYA-LKKSNGIVEEATEEELMDATALAD 427
Cdd:PRK08813 246 FLTRRLCSsLLDDVVIVREAELRETLVRLALEE 278
PRK08639 PRK08639
threonine dehydratase; Validated
163-328 5.10e-04

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 42.49  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  163 NLFWAERFGKQ-YLQMNDL-WVKhcgishtgSFKDLGMSVLVSQVNRLRKMNkpviGVGCASTGDtSAALSAY-CASAGI 239
Cdd:PRK08639  31 NDYLSEKYGANvYLKREDLqPVR--------SYKLRGAYNAISQLSDEELAA----GVVCASAGN-HAQGVAYaCRHLGI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410191  240 PSIVFLPA-------DKISM--AQLVQPIANGafvlsiDTdFDGCMHLIREVTAELPIYLANSLNSLR-LEGQKTAAIEI 309
Cdd:PRK08639  98 PGVIFMPVttpqqkiDQVRFfgGEFVEIVLVG------DT-FDDSAAAAQEYAEETGATFIPPFDDPDvIAGQGTVAVEI 170
                        170       180
                 ....*....|....*....|..
gi 18410191  310 LQQFNWQ-VPDWVIVP--GGNL 328
Cdd:PRK08639 171 LEQLEKEgSPDYVFVPvgGGGL 192
 
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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