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Conserved domains on  [gi|1309179814|gb|PKQ36926|]
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threonine aldolase [Actinobacteria bacterium HGW-Actinobacteria-1]

Protein Classification

low specificity L-threonine aldolase( domain architecture ID 10005169)

low-specificity L-threonine aldolase catalyzes the cleavage of L-allo-threonine and L-threonine to glycine in a PLP-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
2-336 6.23e-140

Threonine aldolase [Amino acid transport and metabolism];


:

Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 399.44  E-value: 6.23e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDqAETFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:COG2008     5 FRSDTVTGPHPEMLEAMAAANVGDD-VYGEDPTVNRLEERVAELFGK-EAALFVPSGTMANQLALRAHTRPGDEVICHET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATPDGKLTPALIEGAITGvGVEHHSQPRVVSITQSTEYGTTYRSEEIAAIADVTHAHG 161
Cdd:COG2008    83 AHIYVDEGGAPEALSGVKLLPVPGEDGKLTPEDLEAAIRP-GDVHFPQPGLVSLENTTEGGTVYPLEELRAIAAVAREHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 162 LVLHVDGARISNAAAFLGCTLGEMTtdAGADIVSCGGAKNGMVFGEAVVFIRPELAEGFAFVRKNGAQLASKMRFISAQF 241
Cdd:COG2008   162 LPLHLDGARLFNAAAALGVSLAEIT--AGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 242 EALFGGDlwLQNAAHANEMARLLASEMQGISGVEITQSVEANEVFARVRRELIKPLQDvSDYYMWDVQSDEVRWVTSWDT 321
Cdd:COG2008   240 LAALEDD--LERLAEDHAMARRLAEGLAALPGVRVPEPVETNIVFVILPDELAERLRE-KGVLFYPWGPGAVRLVTHWDT 316

                         330
                  ....*....|....*
gi 1309179814 322 TSEDIDRFVGAARAL 336
Cdd:COG2008   317 TEEDVDAFLAALAEL 331
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
2-336 6.23e-140

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 399.44  E-value: 6.23e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDqAETFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:COG2008     5 FRSDTVTGPHPEMLEAMAAANVGDD-VYGEDPTVNRLEERVAELFGK-EAALFVPSGTMANQLALRAHTRPGDEVICHET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATPDGKLTPALIEGAITGvGVEHHSQPRVVSITQSTEYGTTYRSEEIAAIADVTHAHG 161
Cdd:COG2008    83 AHIYVDEGGAPEALSGVKLLPVPGEDGKLTPEDLEAAIRP-GDVHFPQPGLVSLENTTEGGTVYPLEELRAIAAVAREHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 162 LVLHVDGARISNAAAFLGCTLGEMTtdAGADIVSCGGAKNGMVFGEAVVFIRPELAEGFAFVRKNGAQLASKMRFISAQF 241
Cdd:COG2008   162 LPLHLDGARLFNAAAALGVSLAEIT--AGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 242 EALFGGDlwLQNAAHANEMARLLASEMQGISGVEITQSVEANEVFARVRRELIKPLQDvSDYYMWDVQSDEVRWVTSWDT 321
Cdd:COG2008   240 LAALEDD--LERLAEDHAMARRLAEGLAALPGVRVPEPVETNIVFVILPDELAERLRE-KGVLFYPWGPGAVRLVTHWDT 316

                         330
                  ....*....|....*
gi 1309179814 322 TSEDIDRFVGAARAL 336
Cdd:COG2008   317 TEEDVDAFLAALAEL 331
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 2-336 3.68e-117

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 342.01  E-value: 3.68e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDqAETFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:cd06502     2 FRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFGK-EAALFVPSGTAANQLALAAHTQPGGSVICHET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATPDGKLTPALIEGAITGVGVEHHSQPRVVSITQSTEYGTTYRSEEIAAIADVTHAHG 161
Cdd:cd06502    80 AHIYTDEAGAPEFLSGVKLLPVPGENGKLTPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPLDELKAISALAKENG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 162 LVLHVDGARISNAAAFLGCTLgeMTTDAGADIVSCGGAKNGMVFGEAVVFIRPELAEGFAFVRKNGAQLASKMRFISAQF 241
Cdd:cd06502   160 LPLHLDGARLANAAAALGVAL--KTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 242 EALFGGDLWLQNAAHANEMARLLA--------SEMQGISGVEITQSVEANEVFARVRRELIKPLQDVSDYYMWDVQSdeV 313
Cdd:cd06502   238 LAALENDLWLRRLRHDHEMARRLAealeelggLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGG--V 315

                         330       340
                  ....*....|....*....|...
gi 1309179814 314 RWVTSWDTTSEDIDRFVGAARAL 336
Cdd:cd06502   316 RFVTHWDTTEEDVDELLSALKAV 338
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
2-290 5.88e-58

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 188.96  E-value: 5.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDQAeTFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:pfam01212   2 LRSDTVTGPTPAMREAMAAAMVGDE-VYGGDPTVNRLEDRVAELFGKEA-ALFVPSGTAANQLALMAHCQRGDEVICGEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATP-DGKLTPALIEGAITGVGVEHHSQPRVVSITQSTEY--GTTYRSEEIAAIADVTH 158
Cdd:pfam01212  80 AHIHFDETGGHAELGGVQPRPLDGDeAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSagGQVVSLENLREIAALAR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 159 AHGLVLHVDGARISNAAAFLGCTLGEMTtdAGADIVSCGGAKNGMVFGEAVVFIRPE-LAEGFAFVRkngaQLASKMR-- 235
Cdd:pfam01212 160 EHGIPVHLDGARFANAAVALGVIVKEIT--SYADSVTMCLSKGLGAPVGSVLAGSDDfIAKAIRQRK----YLGGGLRqa 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179814 236 -FISAQfeALFGGDLWLQNAAHANEMARLLASEMQGISGVeITQSVEANEVFARVR 290
Cdd:pfam01212 234 gVLAAA--GLRALEEGVARLARDHATARRLAEGLELLRLA-IPRRVYTNTHMVYVA 286
GntG_guanitoxin NF041359
GntG family PLP-dependent aldolase;
50-332 3.38e-17

GntG family PLP-dependent aldolase;


Pssm-ID: 469251 [Multi-domain]  Cd Length: 342  Bit Score: 81.34  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  50 AETFFVFNGTGANVTALSAVMRSYHAVICAETAHINCDECGAPERFTGGKLLPVAT-PDGKLTPALIEGAITGVGvEHHS 128
Cdd:NF041359   53 EAALFVPSGTMGNLIALLSHCGRGEEYIVGDQAHIYLYEAGGAAVLGGIHPQPVPNqPDGSLDLDQVRAAIRPDD-EHFP 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 129 QPRVVSI--TQSTEYGTTYRSEEIAAIADVTHAHGLVLHVDGARISNAAAFLGCTLGEMTTDagADIVS-CGGAKNGMVF 205
Cdd:NF041359  132 RTRLICLenTHNRCGGKVLPLEYLAAVRDLAHEHGLALHLDGARLFNAAVALGVDPADLVRP--FDSVSvCLSKGLAAPV 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 206 GEAVVFIRPELAEGfafvRKNGAQLASKMR---FISAQfeALFGGDLWLQNAAHANEMARLLASEMQGISGV-EITQSVE 281
Cdd:NF041359  210 GSVLVGSREFIARA----RRLRKLLGGGMRqagVLAAA--GIVALEEMVERLADDHANAQRLAEGLAALPGVaIQTEPVQ 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179814 282 ANEVFARVRRELIKPLQDV-----SDYYMWDVQSDEVRWVTSWDTTSEDIDRFVGA 332
Cdd:NF041359  284 TNMVFFSLHEPELDAQALLaflkeRGILLSDVGERRLRAVTHYGITRADIDQAIDA 339
PLN02721 PLN02721
threonine aldolase
 2-339 1.20e-16

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 79.73  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHaHAYGNDEWTRSAKQTMKRHFGDQAeTFFVFNGTGANvtaLSAVM----RSYHAVI 77
Cdd:PLN02721   10 LRSDTVTKPTDAMRAAMANAEVDD-DVLGYDPTALRLEEEMAKIFGKEA-ALFVPSGTMGN---LISVLvhcdVRGSEVI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  78 CAETAHINCDECGAPErFTGG---KLLPvATPDGKLTPALIEGAITGVGVEHHSQPRVVSI--TQSTEYGTTYRSEEIAA 152
Cdd:PLN02721   85 LGDNSHIHLYENGGIS-TLGGvhpRTVK-NNEDGTMDLDAIEAAIRPKGDDHFPTTRLICLenTHANCGGRCLSVEYTDK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 153 IADVTHAHGLVLHVDGARISNAAAFLGCTLGEMTTdaGADIVS-C---G-GAKNGMVFGEAVVFIRpeLAEgfaFVRKng 227
Cdd:PLN02721  163 VGELAKRHGLKLHIDGARIFNASVALGVPVHRLVK--AADSVSvClskGlGAPVGSVIVGSKSFIR--KAK---RLRK-- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 228 aQLASKMR---FISAQfeALFGGDLWLQNAAHANEMARLLASEMQGISGVEI-TQSVEANEVFARVR-------RELIKP 296
Cdd:PLN02721  234 -TLGGGMRqvgVLAAA--ALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVnVAAVETNIVYFDITdgsritaEKLCKS 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1309179814 297 LQDVSDYYMwDVQSDEVRWVTSWDTTSEDIDRFVGAARALSEG 339
Cdd:PLN02721  311 LEEHGVLLM-PGNSSRIRVVTHHQISDSDVQYTLSCFQQAALT 352
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
2-336 6.23e-140

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 399.44  E-value: 6.23e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDqAETFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:COG2008     5 FRSDTVTGPHPEMLEAMAAANVGDD-VYGEDPTVNRLEERVAELFGK-EAALFVPSGTMANQLALRAHTRPGDEVICHET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATPDGKLTPALIEGAITGvGVEHHSQPRVVSITQSTEYGTTYRSEEIAAIADVTHAHG 161
Cdd:COG2008    83 AHIYVDEGGAPEALSGVKLLPVPGEDGKLTPEDLEAAIRP-GDVHFPQPGLVSLENTTEGGTVYPLEELRAIAAVAREHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 162 LVLHVDGARISNAAAFLGCTLGEMTtdAGADIVSCGGAKNGMVFGEAVVFIRPELAEGFAFVRKNGAQLASKMRFISAQF 241
Cdd:COG2008   162 LPLHLDGARLFNAAAALGVSLAEIT--AGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 242 EALFGGDlwLQNAAHANEMARLLASEMQGISGVEITQSVEANEVFARVRRELIKPLQDvSDYYMWDVQSDEVRWVTSWDT 321
Cdd:COG2008   240 LAALEDD--LERLAEDHAMARRLAEGLAALPGVRVPEPVETNIVFVILPDELAERLRE-KGVLFYPWGPGAVRLVTHWDT 316

                         330
                  ....*....|....*
gi 1309179814 322 TSEDIDRFVGAARAL 336
Cdd:COG2008   317 TEEDVDAFLAALAEL 331
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 2-336 3.68e-117

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 342.01  E-value: 3.68e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDqAETFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:cd06502     2 FRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFGK-EAALFVPSGTAANQLALAAHTQPGGSVICHET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATPDGKLTPALIEGAITGVGVEHHSQPRVVSITQSTEYGTTYRSEEIAAIADVTHAHG 161
Cdd:cd06502    80 AHIYTDEAGAPEFLSGVKLLPVPGENGKLTPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPLDELKAISALAKENG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 162 LVLHVDGARISNAAAFLGCTLgeMTTDAGADIVSCGGAKNGMVFGEAVVFIRPELAEGFAFVRKNGAQLASKMRFISAQF 241
Cdd:cd06502   160 LPLHLDGARLANAAAALGVAL--KTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 242 EALFGGDLWLQNAAHANEMARLLA--------SEMQGISGVEITQSVEANEVFARVRRELIKPLQDVSDYYMWDVQSdeV 313
Cdd:cd06502   238 LAALENDLWLRRLRHDHEMARRLAealeelggLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGG--V 315

                         330       340
                  ....*....|....*....|...
gi 1309179814 314 RWVTSWDTTSEDIDRFVGAARAL 336
Cdd:cd06502   316 RFVTHWDTTEEDVDELLSALKAV 338
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
2-290 5.88e-58

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 188.96  E-value: 5.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHAhAYGNDEWTRSAKQTMKRHFGDQAeTFFVFNGTGANVTALSAVMRSYHAVICAET 81
Cdd:pfam01212   2 LRSDTVTGPTPAMREAMAAAMVGDE-VYGGDPTVNRLEDRVAELFGKEA-ALFVPSGTAANQLALMAHCQRGDEVICGEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  82 AHINCDECGAPERFTGGKLLPVATP-DGKLTPALIEGAITGVGVEHHSQPRVVSITQSTEY--GTTYRSEEIAAIADVTH 158
Cdd:pfam01212  80 AHIHFDETGGHAELGGVQPRPLDGDeAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSagGQVVSLENLREIAALAR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 159 AHGLVLHVDGARISNAAAFLGCTLGEMTtdAGADIVSCGGAKNGMVFGEAVVFIRPE-LAEGFAFVRkngaQLASKMR-- 235
Cdd:pfam01212 160 EHGIPVHLDGARFANAAVALGVIVKEIT--SYADSVTMCLSKGLGAPVGSVLAGSDDfIAKAIRQRK----YLGGGLRqa 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179814 236 -FISAQfeALFGGDLWLQNAAHANEMARLLASEMQGISGVeITQSVEANEVFARVR 290
Cdd:pfam01212 234 gVLAAA--GLRALEEGVARLARDHATARRLAEGLELLRLA-IPRRVYTNTHMVYVA 286
GntG_guanitoxin NF041359
GntG family PLP-dependent aldolase;
50-332 3.38e-17

GntG family PLP-dependent aldolase;


Pssm-ID: 469251 [Multi-domain]  Cd Length: 342  Bit Score: 81.34  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  50 AETFFVFNGTGANVTALSAVMRSYHAVICAETAHINCDECGAPERFTGGKLLPVAT-PDGKLTPALIEGAITGVGvEHHS 128
Cdd:NF041359   53 EAALFVPSGTMGNLIALLSHCGRGEEYIVGDQAHIYLYEAGGAAVLGGIHPQPVPNqPDGSLDLDQVRAAIRPDD-EHFP 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 129 QPRVVSI--TQSTEYGTTYRSEEIAAIADVTHAHGLVLHVDGARISNAAAFLGCTLGEMTTDagADIVS-CGGAKNGMVF 205
Cdd:NF041359  132 RTRLICLenTHNRCGGKVLPLEYLAAVRDLAHEHGLALHLDGARLFNAAVALGVDPADLVRP--FDSVSvCLSKGLAAPV 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 206 GEAVVFIRPELAEGfafvRKNGAQLASKMR---FISAQfeALFGGDLWLQNAAHANEMARLLASEMQGISGV-EITQSVE 281
Cdd:NF041359  210 GSVLVGSREFIARA----RRLRKLLGGGMRqagVLAAA--GIVALEEMVERLADDHANAQRLAEGLAALPGVaIQTEPVQ 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179814 282 ANEVFARVRRELIKPLQDV-----SDYYMWDVQSDEVRWVTSWDTTSEDIDRFVGA 332
Cdd:NF041359  284 TNMVFFSLHEPELDAQALLaflkeRGILLSDVGERRLRAVTHYGITRADIDQAIDA 339
PLN02721 PLN02721
threonine aldolase
 2-339 1.20e-16

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 79.73  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   2 FASDNASGAHPDIMAALIAANTGHaHAYGNDEWTRSAKQTMKRHFGDQAeTFFVFNGTGANvtaLSAVM----RSYHAVI 77
Cdd:PLN02721   10 LRSDTVTKPTDAMRAAMANAEVDD-DVLGYDPTALRLEEEMAKIFGKEA-ALFVPSGTMGN---LISVLvhcdVRGSEVI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  78 CAETAHINCDECGAPErFTGG---KLLPvATPDGKLTPALIEGAITGVGVEHHSQPRVVSI--TQSTEYGTTYRSEEIAA 152
Cdd:PLN02721   85 LGDNSHIHLYENGGIS-TLGGvhpRTVK-NNEDGTMDLDAIEAAIRPKGDDHFPTTRLICLenTHANCGGRCLSVEYTDK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 153 IADVTHAHGLVLHVDGARISNAAAFLGCTLGEMTTdaGADIVS-C---G-GAKNGMVFGEAVVFIRpeLAEgfaFVRKng 227
Cdd:PLN02721  163 VGELAKRHGLKLHIDGARIFNASVALGVPVHRLVK--AADSVSvClskGlGAPVGSVIVGSKSFIR--KAK---RLRK-- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 228 aQLASKMR---FISAQfeALFGGDLWLQNAAHANEMARLLASEMQGISGVEI-TQSVEANEVFARVR-------RELIKP 296
Cdd:PLN02721  234 -TLGGGMRqvgVLAAA--ALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVnVAAVETNIVYFDITdgsritaEKLCKS 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1309179814 297 LQDVSDYYMwDVQSDEVRWVTSWDTTSEDIDRFVGAARALSEG 339
Cdd:PLN02721  311 LEEHGVLLM-PGNSSRIRVVTHHQISDSDVQYTLSCFQQAALT 352
PRK10534 PRK10534
L-threonine aldolase; Provisional
 4-186 5.51e-08

L-threonine aldolase; Provisional


Pssm-ID: 236710 [Multi-domain]  Cd Length: 333  Bit Score: 53.61  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   4 SDNASGAHPDIMAALIAANTGHaHAYGNDEwTRSAKQTMKRHFGDQAETFFVFNGTGANVTALSAVMRSYHAVICAETAH 83
Cdd:PRK10534    6 SDTVTRPSRAMLEAMMAAPVGD-DVYGDDP-TVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCERGEEYIVGQAAH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  84 INCDECGAPERFTGGKLLPV-ATPDGKLTPALIEGAITGVGVeHHSQPRVVSItQSTEYGTTYRSEEIAAIADVTHAHGL 162
Cdd:PRK10534   84 NYLYEAGGAAVLGSIQPQPIdAAADGTLPLDKVAAKIKPDDI-HFARTRLLSL-ENTHNGKVLPREYLKQAWEFTRERNL 161

                         170       180
                  ....*....|....*....|....
gi 1309179814 163 VLHVDGARISNAAAFLGCTLGEMT 186
Cdd:PRK10534  162 ALHVDGARIFNAVVAYGCELKEIT 185
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 48-218 8.53e-07

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 49.94  E-value: 8.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  48 DQAETFFVFNGTGANVTALSAVMRSY----HAVICAETAHINCDECGAPERFTGGKL--LPVaTPDGKLTPALIEGAITG 121
Cdd:pfam00266  60 SNDEIIFTSGTTEAINLVALSLGRSLkpgdEIVITEMEHHANLVPWQELAKRTGARVrvLPL-DEDGLLDLDELEKLITP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 122 vgvehhsQPRVVSITQ-STEYGTTYRSEEIAAIAdvtHAHGLVLHVDGARisnaaaflgcTLGEMTTDA---GADIVSCG 197
Cdd:pfam00266 139 -------KTKLVAITHvSNVTGTIQPVPEIGKLA---HQYGALVLVDAAQ----------AIGHRPIDVqklGVDFLAFS 198

                         170       180
                  ....*....|....*....|.
gi 1309179814 198 GAKNGMVFGEAVVFIRPELAE 218
Cdd:pfam00266 199 GHKLYGPTGIGVLYGRRDLLE 219
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 45-169 1.71e-05

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 46.36  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  45 HFGDQAETFFVFNGTGANVTALsAVMRSYHA----------------VICAETAHI----NCDECGAPERFtggkLLPVA 104
Cdd:COG0076   121 GLPEGAGGVFTSGGTEANLLAL-LAARDRALarrvraeglpgaprprIVVSEEAHSsvdkAARLLGLGRDA----LRKVP 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 105 T-PDGKLTPALIEGAITgvgvEHHSQPR----VVSITQSTEYGTTyrsEEIAAIADVTHAHGLVLHVDGA 169
Cdd:COG0076   196 VdEDGRMDPDALEAAID----EDRAAGLnpiaVVATAGTTNTGAI---DPLAEIADIAREHGLWLHVDAA 258
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 38-169 5.01e-05

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 44.55  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  38 AKQTMKRHFGDqAETFFVFNGT-GANVTALSAVMRSYHAVI----CAETAHINCDECGA------PERFTGGKLlPVATP 106
Cdd:cd00615    64 AQELAARAFGA-KHTFFLVNGTsSSNKAVILAVCGPGDKILidrnCHKSVINGLVLSGAvpvylkPERNPYYGI-AGGIP 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179814 107 DGKLTPALIEgaitgvgvehHSQPRVVSITQSTEYGTTYrseEIAAIADVTHAHGLVLHVDGA 169
Cdd:cd00615   142 PETFKKALIE----------HPDAKAAVITNPTYYGICY---NLRKIVEEAHHRGLPVLVDEA 191
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
38-169 1.79e-03

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 39.79  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  38 AKQTMKRHFGdQAETFFVFNGT-GANVTALSAVMRSYHAVI----CAETAHINCDECGA------PERFTGGKLLPVatP 106
Cdd:pfam01276  71 AQKYAARVFG-ADKSYFVVNGTsGSNKTVGMAVCTPGDTILidrnCHKSIHHALMLSGAtpvylePSRNAYGIIGGI--P 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179814 107 DGKLTPALIEGAITGVGVEhhSQPRVVSITQSTEYGTTYRSEEIAAIADVThahGLVLHVDGA 169
Cdd:pfam01276 148 LHEFQEETLKEAIAEVPDA--KGPRLAVITNPTYDGVLYNAKEIVDTLHHL---SDPILFDSA 205
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 8-168 3.54e-03

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 38.81  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814   8 SGAHPDIMAALIAANTGHAHAYGNdEWTRSAKQTMKRHFGDQAETFFVF--NGTGANVTALSAVMRSYHAVICAETAH-- 83
Cdd:cd06451     8 SNVPPRVLKAMNRPMLGHRSPEFL-ALMDEILEGLRYVFQTENGLTFLLsgSGTGAMEAALSNLLEPGDKVLVGVNGVfg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  84 ---INCdecgaPERFtGGKLLPVATPDGK-LTPALIEGAITgvgvEHhsQPRVVSITQS-TEYGTTYRSEEIAAIAdvtH 158
Cdd:cd06451    87 drwADM-----AERY-GADVDVVEKPWGEaVSPEEIAEALE----QH--DIKAVTLTHNeTSTGVLNPLEGIGALA---K 151

                         170
                  ....*....|
gi 1309179814 159 AHGLVLHVDG 168
Cdd:cd06451   152 KHDALLIVDA 161
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 96-276 3.81e-03

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 38.60  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  96 TGGKLLPV-ATPDGKLTPALIEGAITgvgvehhSQPRVVSITQ-STEYGTTYRSEEIAAIAdvtHAHGLVLHVDGARisn 173
Cdd:cd06453   112 TGAKLKVVpVDDDGQLDLEALEKLLT-------ERTKLVAVTHvSNVLGTINPVKEIGEIA---HEAGVPVLVDGAQ--- 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 174 aaaflgcTLGEMTTDA---GADIVSCGGAKNGMVFGEAVVFIRPELAEGFAFVRKNG------AQLASKMRFISAQFEA- 243
Cdd:cd06453   179 -------SAGHMPVDVqdlGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGemieevSFEETTYADLPHKFEAg 251

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1309179814 244 ---------LFGGDLWLQN------AAHANEMARLLASEMQGISGVEI 276
Cdd:cd06453   252 tpniagaigLGAAIDYLEKigmeaiAAHEHELTAYALERLSEIPGVRV 299
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 52-213 3.92e-03

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 37.75  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  52 TFFVFNGTGANVTAL-SAVMRSYHAVICAETAHincdecGAPERFT---GGKLLPVATPDGKLTPALIEGAITGVGVEHh 127
Cdd:cd01494    20 AVFVPSGTGANEAALlALLGPGDEVIVDANGHG------SRYWVAAelaGAKPVPVPVDDAGYGGLDVAILEELKAKPN- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814 128 sqPRVVSITQS-TEYGTTYRSEEIAAIAdvtHAHGLVLHVDGARISNAAAFLGCTLGEMttdaGADIVSCGGAKNGMVFG 206
Cdd:cd01494    93 --VALIVITPNtTSGGVLVPLKEIRKIA---KEYGILLLVDAASAGGASPAPGVLIPEG----GADVVTFSLHKNLGGEG 163


                  ....*..
gi 1309179814 207 EAVVFIR 213
Cdd:cd01494   164 GGVVIVK 170
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 10-164 5.84e-03

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 38.19  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  10 AHPDIMAALIAANTGHAHAYGNDEWTRSAKQT----MKRHFGDQ--AETFFVFNG-TGANVTALSAVMR----------- 71
Cdd:COG0436    44 TPDHIREAAIEALDDGVTGYTPSAGIPELREAiaayYKRRYGVDldPDEILVTNGaKEALALALLALLNpgdevlvpdpg 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179814  72 --SYHAVIcaetahincdecgapeRFTGGKLLPVAT---PDGKLTPALIEGAITgvgvehhSQPRVVSI------Tqste 140
Cdd:COG0436   124 ypSYRAAV----------------RLAGGKPVPVPLdeeNGFLPDPEALEAAIT-------PRTKAIVLnspnnpT---- 176

                         170       180
                  ....*....|....*....|....
gi 1309179814 141 yGTTYRSEEIAAIADVTHAHGLVL 164
Cdd:COG0436   177 -GAVYSREELEALAELAREHDLLV 199
 
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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