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Conserved domains on  [gi|489915944|ref|WP_003819342|]
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low specificity L-threonine aldolase [Bifidobacterium bifidum]

Protein Classification

threonine aldolase family protein( domain architecture ID 10005169)

threonine aldolase family protein such as low-specificity L-threonine aldolase, which catalyzes cleavage of L-allo-threonine and L-threonine to glycine in a PLP-dependent manner

CATH:  3.40.640.10
Gene Ontology:  GO:0006567|GO:0004793
SCOP:  4000670

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];
1-341 4.90e-110

Threonine aldolase [Amino acid transport and metabolism];


:

Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 323.56  E-value: 4.90e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   1 MLSFGNDYSYGACPEILDRLARTNdTAFPGYGSDAACEDAKRRIREACEtpDADVWFLVGGTQTNQIVIDTMLAPYEGVV 80
Cdd:COG2008    2 MIDFRSDTVTGPHPEMLEAMAAAN-VGDDVYGEDPTVNRLEERVAELFG--KEAALFVPSGTMANQLALRAHTRPGDEVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  81 TVDSGHPNVHEAGAIES-TGHKVITLPHHAGKLDAAELDDYcatfyADDNHEHMVFPGLVYISHPTEYGTIYGKAELEVI 159
Cdd:COG2008   79 CHETAHIYVDEGGAPEAlSGVKLLPVPGEDGKLTPEDLEAA-----IRPGDVHFPQPGLVSLENTTEGGTVYPLEELRAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 160 AETAHRHGMPLFVDGARLGYGLTAAGTDVTlpDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGALLAK 239
Cdd:COG2008  154 AAVAREHGLPLHLDGARLFNAAAALGVSLA--EITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 240 GWLLGLQFGTLFTDDlyLRIAANANRQADRIREALRER-GYTLTFEAPTNQVFVTLDHPTIERLQAH-VRMGFMEKAdne 317
Cdd:COG2008  232 AGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALpGVRVPEPVETNIVFVILPDELAERLREKgVLFYPWGPG--- 306
                        330       340
                 ....*....|....*....|....
gi 489915944 318 htVMRLCTSWATTDEQVDQLIALL 341
Cdd:COG2008  307 --AVRLVTHWDTTEEDVDAFLAAL 328
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
1-341 4.90e-110

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 323.56  E-value: 4.90e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   1 MLSFGNDYSYGACPEILDRLARTNdTAFPGYGSDAACEDAKRRIREACEtpDADVWFLVGGTQTNQIVIDTMLAPYEGVV 80
Cdd:COG2008    2 MIDFRSDTVTGPHPEMLEAMAAAN-VGDDVYGEDPTVNRLEERVAELFG--KEAALFVPSGTMANQLALRAHTRPGDEVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  81 TVDSGHPNVHEAGAIES-TGHKVITLPHHAGKLDAAELDDYcatfyADDNHEHMVFPGLVYISHPTEYGTIYGKAELEVI 159
Cdd:COG2008   79 CHETAHIYVDEGGAPEAlSGVKLLPVPGEDGKLTPEDLEAA-----IRPGDVHFPQPGLVSLENTTEGGTVYPLEELRAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 160 AETAHRHGMPLFVDGARLGYGLTAAGTDVTlpDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGALLAK 239
Cdd:COG2008  154 AAVAREHGLPLHLDGARLFNAAAALGVSLA--EITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 240 GWLLGLQFGTLFTDDlyLRIAANANRQADRIREALRER-GYTLTFEAPTNQVFVTLDHPTIERLQAH-VRMGFMEKAdne 317
Cdd:COG2008  232 AGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALpGVRVPEPVETNIVFVILPDELAERLREKgVLFYPWGPG--- 306
                        330       340
                 ....*....|....*....|....
gi 489915944 318 htVMRLCTSWATTDEQVDQLIALL 341
Cdd:COG2008  307 --AVRLVTHWDTTEEDVDAFLAAL 328
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
4-341 2.13e-68

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: 217.59  E-value: 2.13e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   4 FGNDYSYGACPEILDRLARTNdTAFPGYGSDAACEDAKRRIREACEtpDADVWFLVGGTQTNQIVIDTMLAPYEGVVTVD 83
Cdd:cd06502    2 FRSDTVTGPTPEMLEAMAAAN-VGDDVYGEDPTTAKLEARAAELFG--KEAALFVPSGTAANQLALAAHTQPGGSVICHE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  84 SGHPNVHEAGAIES-TGHKVITLPHHAGKLDAAELDDYcatfYADDNHEHMVFPGLVYISHPTEYGTIYGKAELEVIAET 162
Cdd:cd06502   79 TAHIYTDEAGAPEFlSGVKLLPVPGENGKLTPEDLEAA----IRPRDDIHFPPPSLVSLENTTEGGTVYPLDELKAISAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 163 AHRHGMPLFVDGARLGYGLTAAGtdVTLPDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGALLAKGWL 242
Cdd:cd06502  155 AKENGLPLHLDGARLANAAAALG--VALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGF 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 243 LGLQFGTLFTDDLYLRIAANANRQADRIREALRERGYT---------LTFEAPTNQVFVTLDHPTIERLQAHVRMGFMek 313
Cdd:cd06502  233 LAAAGLAALENDLWLRRLRHDHEMARRLAEALEELGGLesevqtnivLLDPVEANAVFVELSKEAIERRGEGVLFYAW-- 310
                        330       340
                 ....*....|....*....|....*...
gi 489915944 314 adnEHTVMRLCTSWATTDEQVDQLIALL 341
Cdd:cd06502  311 ---GEGGVRFVTHWDTTEEDVDELLSAL 335
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
11-295 3.42e-22

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 94.59  E-value: 3.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   11 GACPEILDRLARTN--DTAfpgYGSDAACEDAKRRIREACETPDAdvWFLVGGTQTNQIVIDTMLAPYEGVVTVDSGHPN 88
Cdd:pfam01212   9 GPTPAMREAMAAAMvgDEV---YGGDPTVNRLEDRVAELFGKEAA--LFVPSGTAANQLALMAHCQRGDEVICGEPAHIH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   89 VHEAGAIES-TGHKVITLPH-HAGKLDAAELddycATFYADDNHEHMVFPGLVY--ISHPTEYGTIYGKAELEVIAETAH 164
Cdd:pfam01212  84 FDETGGHAElGGVQPRPLDGdEAGNMDLEDL----EAAIREVGADIFPPTGLISleNTHNSAGGQVVSLENLREIAALAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  165 RHGMPLFVDGARLGYGLTAAGtdVTLPDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGA------LLA 238
Cdd:pfam01212 160 EHGIPVHLDGARFANAAVALG--VIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGglrqagVLA 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489915944  239 KGWLLGLQFGtlftddlyLRIAANANRQADRIREALRERGYTLTFEAPTNQVFVTLD 295
Cdd:pfam01212 238 AAGLRALEEG--------VARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVA 286
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
2-205 8.28e-04

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 40.79  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944    2 LSFGNDYSYG---ACPEILDRLARTNDTA-FPGYGSDAACEDAKRRIRE--ACE-----TPDaDVWFLVGGTQTNQIVID 70
Cdd:TIGR01265  36 LSHGDPSVFGnlrTDPEAEEAVKDALRSGkFNGYAPSVGALAAREAVAEylSSDlpgklTAD-DVVLTSGCSQAIEICIE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   71 TMLAPYEGVVTVDSGHPN---VHEAGAIEStgHKVITLPHHAGKLDAAELDDYcatfyADDNHEHMVfpgLVYISHPTey 147
Cdd:TIGR01265 115 ALANPGANILVPRPGFPLydtRAAFSGLEV--RLYDLLPEKDWEIDLDGLESL-----ADEKTVAIV---VINPSNPC-- 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  148 GTIYGKAELEVIAETAHRHGMPLFVDGArlgYGLTAAG--TDVTLPDLARIADVFYIGGT 205
Cdd:TIGR01265 183 GSVFSRDHLQKIAEVAEKLGIPIIADEI---YGHMVFGdaPFIPMASFASIVPVLSLGGI 239
PLN02721 PLN02721
threonine aldolase
57-294 9.75e-03

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 37.36  E-value: 9.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  57 FLVGGTQTNQIVIDTML-APYEGVVTVDSGHPNVHEAGAIESTG--HKVITLPHHAGKLDAAELDDycATFYADDNHehm 133
Cdd:PLN02721  60 FVPSGTMGNLISVLVHCdVRGSEVILGDNSHIHLYENGGISTLGgvHPRTVKNNEDGTMDLDAIEA--AIRPKGDDH--- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 134 vFPGLVYI----SHPTEYGTIYGKAELEVIAETAHRHGMPLFVDGARLGYGLTAAGtdVTLPDLARIADVFYIGGTK-VG 208
Cdd:PLN02721 135 -FPTTRLIclenTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARIFNASVALG--VPVHRLVKAADSVSVCLSKgLG 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 209 ALFGEAVVFTKGntpkhFLTQIK-----------QHGALLAKGwLLGLQfgtlftdDLYLRIAANaNRQADRIREALRER 277
Cdd:PLN02721 212 APVGSVIVGSKS-----FIRKAKrlrktlgggmrQVGVLAAAA-LVALQ-------ENVPKLEDD-HKKAKLLAEGLNQI 277
                        250
                 ....*....|....*....
gi 489915944 278 GYTLTFEAP--TNQVFVTL 294
Cdd:PLN02721 278 KGLRVNVAAveTNIVYFDI 296
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
1-341 4.90e-110

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 323.56  E-value: 4.90e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   1 MLSFGNDYSYGACPEILDRLARTNdTAFPGYGSDAACEDAKRRIREACEtpDADVWFLVGGTQTNQIVIDTMLAPYEGVV 80
Cdd:COG2008    2 MIDFRSDTVTGPHPEMLEAMAAAN-VGDDVYGEDPTVNRLEERVAELFG--KEAALFVPSGTMANQLALRAHTRPGDEVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  81 TVDSGHPNVHEAGAIES-TGHKVITLPHHAGKLDAAELDDYcatfyADDNHEHMVFPGLVYISHPTEYGTIYGKAELEVI 159
Cdd:COG2008   79 CHETAHIYVDEGGAPEAlSGVKLLPVPGEDGKLTPEDLEAA-----IRPGDVHFPQPGLVSLENTTEGGTVYPLEELRAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 160 AETAHRHGMPLFVDGARLGYGLTAAGTDVTlpDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGALLAK 239
Cdd:COG2008  154 AAVAREHGLPLHLDGARLFNAAAALGVSLA--EITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 240 GWLLGLQFGTLFTDDlyLRIAANANRQADRIREALRER-GYTLTFEAPTNQVFVTLDHPTIERLQAH-VRMGFMEKAdne 317
Cdd:COG2008  232 AGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALpGVRVPEPVETNIVFVILPDELAERLREKgVLFYPWGPG--- 306
                        330       340
                 ....*....|....*....|....
gi 489915944 318 htVMRLCTSWATTDEQVDQLIALL 341
Cdd:COG2008  307 --AVRLVTHWDTTEEDVDAFLAAL 328
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
4-341 2.13e-68

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: 217.59  E-value: 2.13e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   4 FGNDYSYGACPEILDRLARTNdTAFPGYGSDAACEDAKRRIREACEtpDADVWFLVGGTQTNQIVIDTMLAPYEGVVTVD 83
Cdd:cd06502    2 FRSDTVTGPTPEMLEAMAAAN-VGDDVYGEDPTTAKLEARAAELFG--KEAALFVPSGTAANQLALAAHTQPGGSVICHE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  84 SGHPNVHEAGAIES-TGHKVITLPHHAGKLDAAELDDYcatfYADDNHEHMVFPGLVYISHPTEYGTIYGKAELEVIAET 162
Cdd:cd06502   79 TAHIYTDEAGAPEFlSGVKLLPVPGENGKLTPEDLEAA----IRPRDDIHFPPPSLVSLENTTEGGTVYPLDELKAISAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 163 AHRHGMPLFVDGARLGYGLTAAGtdVTLPDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGALLAKGWL 242
Cdd:cd06502  155 AKENGLPLHLDGARLANAAAALG--VALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGF 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 243 LGLQFGTLFTDDLYLRIAANANRQADRIREALRERGYT---------LTFEAPTNQVFVTLDHPTIERLQAHVRMGFMek 313
Cdd:cd06502  233 LAAAGLAALENDLWLRRLRHDHEMARRLAEALEELGGLesevqtnivLLDPVEANAVFVELSKEAIERRGEGVLFYAW-- 310
                        330       340
                 ....*....|....*....|....*...
gi 489915944 314 adnEHTVMRLCTSWATTDEQVDQLIALL 341
Cdd:cd06502  311 ---GEGGVRFVTHWDTTEEDVDELLSAL 335
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
11-295 3.42e-22

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 94.59  E-value: 3.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   11 GACPEILDRLARTN--DTAfpgYGSDAACEDAKRRIREACETPDAdvWFLVGGTQTNQIVIDTMLAPYEGVVTVDSGHPN 88
Cdd:pfam01212   9 GPTPAMREAMAAAMvgDEV---YGGDPTVNRLEDRVAELFGKEAA--LFVPSGTAANQLALMAHCQRGDEVICGEPAHIH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   89 VHEAGAIES-TGHKVITLPH-HAGKLDAAELddycATFYADDNHEHMVFPGLVY--ISHPTEYGTIYGKAELEVIAETAH 164
Cdd:pfam01212  84 FDETGGHAElGGVQPRPLDGdEAGNMDLEDL----EAAIREVGADIFPPTGLISleNTHNSAGGQVVSLENLREIAALAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  165 RHGMPLFVDGARLGYGLTAAGtdVTLPDLARIADVFYIGGTKVGALFGEAVVFTKGNTPKHFLTQIKQHGA------LLA 238
Cdd:pfam01212 160 EHGIPVHLDGARFANAAVALG--VIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGglrqagVLA 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489915944  239 KGWLLGLQFGtlftddlyLRIAANANRQADRIREALRERGYTLTFEAPTNQVFVTLD 295
Cdd:pfam01212 238 AAGLRALEEG--------VARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVA 286
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
6-339 3.65e-11

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 63.48  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944    6 NDYSYGACPEILDRLARTND----TAFPGYGSDAACEDA----KRRIREACETPDADVWFLVGGTQTNQIVIDTMLAPYE 77
Cdd:pfam00155   9 NEYLGDTLPAVAKAEKDALAggtrNLYGPTDGHPELREAlakfLGRSPVLKLDREAAVVFGSGAGANIEALIFLLANPGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   78 GVVTVDSGHPNVHEAgaIESTGHKVITLPHHAGKLDAAELDDYCATFyaDDNHEHMVFPGlvyISHPTeyGTIYGKAELE 157
Cdd:pfam00155  89 AILVPAPTYASYIRI--ARLAGGEVVRYPLYDSNDFHLDFDALEAAL--KEKPKVVLHTS---PHNPT--GTVATLEELE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  158 VIAETAHRHGMPLFVDGArlgYGLTAAGTD---VTLPDLARIADVFYIG---------GTKVGALFGEAVV---FTKGNT 222
Cdd:pfam00155 160 KLLDLAKEHNILLLVDEA---YAGFVFGSPdavATRALLAEGPNLLVVGsfskafglaGWRVGYILGNAAVisqLRKLAR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  223 PKHFLTqikqHGALLAKGWLLGLQFGTLFTDDLYLRIAANanrqADRIREALRERGytLTFEAPTNQVFVTLDHPtierl 302
Cdd:pfam00155 237 PFYSST----HLQAAAAAALSDPLLVASELEEMRQRIKER----RDYLRDGLQAAG--LSVLPSQAGFFLLTGLD----- 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 489915944  303 qAHVRMGFMEKADNEHTVMRL------CTSW------ATTDEQVDQLIA 339
Cdd:pfam00155 302 -PETAKELAQVLLEEVGVYVTpgsspgVPGWlritvaGGTEEELEELLE 349
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
2-341 5.64e-10

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 59.66  E-value: 5.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   2 LSFG-NDYSYGACPEILDRLARTNDTA-FPGYGSDAACEDAKRRIREAC------ETPDADVWFLVGGTQTNQIVIDTML 73
Cdd:cd00609    1 IDLSiGEPDFPPPPEVLEALAAAALRAgLLGYYPDPGLPELREAIAEWLgrrggvDVPPEEIVVTNGAQEALSLLLRALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  74 APYEGVVTVDSGHPNvHEAgAIESTGHKVITLPhhagkLDAAELDDYCATFYADDNHEHmvfPGLVYISH---PTeyGTI 150
Cdd:cd00609   81 NPGDEVLVPDPTYPG-YEA-AARLAGAEVVPVP-----LDEEGGFLLDLELLEAAKTPK---TKLLYLNNpnnPT--GAV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 151 YGKAELEVIAETAHRHGMPLFVDGArlgYG-LTAAGTDVTLPDLARIAD-VFYIG---------GTKVGALFGEAVVFTK 219
Cdd:cd00609  149 LSEEELEELAELAKKHGILIISDEA---YAeLVYDGEPPPALALLDAYErVIVLRsfsktfglpGLRIGYLIAPPEELLE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 220 GNTPKHFLTQIK--QHGALLAKGWLLGlqfgtlfTDDLYLRIAANANRQADRIREALRERGYTLTFEAP-TNQVFVTLDH 296
Cdd:cd00609  226 RLKKLLPYTTSGpsTLSQAAAAAALDD-------GEEHLEELRERYRRRRDALLEALKELGPLVVVKPSgGFFLWLDLPE 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489915944 297 PTIERLqahvrmgFMEKADNEHTVMRLCTSW------------ATTDEQVDQLIALL 341
Cdd:cd00609  299 GDDEEF-------LERLLLEAGVVVRPGSAFgeggegfvrlsfATPEEELEEALERL 348
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
38-219 2.25e-04

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: 41.21  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  38 EDAKRRIREACETPDADVWFLVGGTQTNQIVIDTMLAPYEGVVTVDSGHPNVHEAgAIESTGHKvitlPHHAGKLDAAEL 117
Cdd:cd01494    3 EELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWV-AAELAGAK----PVPVPVDDAGYG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 118 DDYCATFYADDNHEHmvfPGLVYISHPTEYGTIYgkAELEVIAETAHRHGMPLFVDGARLGYGLTAAGtdvtLPDLARIA 197
Cdd:cd01494   78 GLDVAILEELKAKPN---VALIVITPNTTSGGVL--VPLKEIRKIAKEYGILLLVDAASAGGASPAPG----VLIPEGGA 148
                        170       180
                 ....*....|....*....|..
gi 489915944 198 DVFYIGGTKVGALFGEAVVFTK 219
Cdd:cd01494  149 DVVTFSLHKNLGGEGGGVVIVK 170
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
52-179 3.69e-04

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: 41.85  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  52 DADVWFLVGGTQT-NQIVIDTMLAPYEgVVTVDSghpNVH---EAGAIESTGHKVITLP------HHAGKLDAAELDDyc 121
Cdd:cd00615   74 AKHTFFLVNGTSSsNKAVILAVCGPGD-KILIDR---NCHksvINGLVLSGAVPVYLKPernpyyGIAGGIPPETFKK-- 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489915944 122 ATFYADDnhehmvfPGLVYISHPTEYGTIYgkaELEVIAETAHRHGMPLFVDGARLGY 179
Cdd:cd00615  148 ALIEHPD-------AKAAVITNPTYYGICY---NLRKIVEEAHHRGLPVLVDEAHGAH 195
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
2-205 8.28e-04

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 40.79  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944    2 LSFGNDYSYG---ACPEILDRLARTNDTA-FPGYGSDAACEDAKRRIRE--ACE-----TPDaDVWFLVGGTQTNQIVID 70
Cdd:TIGR01265  36 LSHGDPSVFGnlrTDPEAEEAVKDALRSGkFNGYAPSVGALAAREAVAEylSSDlpgklTAD-DVVLTSGCSQAIEICIE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944   71 TMLAPYEGVVTVDSGHPN---VHEAGAIEStgHKVITLPHHAGKLDAAELDDYcatfyADDNHEHMVfpgLVYISHPTey 147
Cdd:TIGR01265 115 ALANPGANILVPRPGFPLydtRAAFSGLEV--RLYDLLPEKDWEIDLDGLESL-----ADEKTVAIV---VINPSNPC-- 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  148 GTIYGKAELEVIAETAHRHGMPLFVDGArlgYGLTAAG--TDVTLPDLARIADVFYIGGT 205
Cdd:TIGR01265 183 GSVFSRDHLQKIAEVAEKLGIPIIADEI---YGHMVFGdaPFIPMASFASIVPVLSLGGI 239
PLN02721 PLN02721
threonine aldolase
57-294 9.75e-03

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 37.36  E-value: 9.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944  57 FLVGGTQTNQIVIDTML-APYEGVVTVDSGHPNVHEAGAIESTG--HKVITLPHHAGKLDAAELDDycATFYADDNHehm 133
Cdd:PLN02721  60 FVPSGTMGNLISVLVHCdVRGSEVILGDNSHIHLYENGGISTLGgvHPRTVKNNEDGTMDLDAIEA--AIRPKGDDH--- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 134 vFPGLVYI----SHPTEYGTIYGKAELEVIAETAHRHGMPLFVDGARLGYGLTAAGtdVTLPDLARIADVFYIGGTK-VG 208
Cdd:PLN02721 135 -FPTTRLIclenTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARIFNASVALG--VPVHRLVKAADSVSVCLSKgLG 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915944 209 ALFGEAVVFTKGntpkhFLTQIK-----------QHGALLAKGwLLGLQfgtlftdDLYLRIAANaNRQADRIREALRER 277
Cdd:PLN02721 212 APVGSVIVGSKS-----FIRKAKrlrktlgggmrQVGVLAAAA-LVALQ-------ENVPKLEDD-HKKAKLLAEGLNQI 277
                        250
                 ....*....|....*....
gi 489915944 278 GYTLTFEAP--TNQVFVTL 294
Cdd:PLN02721 278 KGLRVNVAAveTNIVYFDI 296
 
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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