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Conserved domains on  [gi|502749816|ref|WP_012984800|]
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low specificity L-threonine aldolase [Listeria seeligeri]

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];
37-337 2.86e-97

Threonine aldolase [Amino acid transport and metabolism];


:

Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 291.97  E-value: 2.86e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  37 NLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRkdNRRMAYHPLSHLEIHEQDGLKELQQINPI 116
Cdd:COG2008   25 NVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRP--GDEVICHETAHIYVDEGGAPEALSGVKLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 117 LLGTAERLLTIEDIKAL-------QEPVSSVLLELPQReiGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFYEK 189
Cdd:COG2008  103 PVPGEDGKLTPEDLEAAirpgdvhFPQPGLVSLENTTE--GGTVYPLEELRAIAAVAREHGLPLHLDGARLFNAAAALGV 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 190 SAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAKKL 269
Cdd:COG2008  181 SLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQGLAALEDDLERLAEDHAMARRL 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749816 270 AERFNACDGVKtVPEVPVSNMFHVHFEKSvdvigtkLAEIQDETGVGISGYLQEKAEDVCGFEVSVGD 337
Cdd:COG2008  261 AEGLAALPGVR-VPEPVETNIVFVILPDE-------LAERLREKGVLFYPWGPGAVRLVTHWDTTEED 320
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
37-337 2.86e-97

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 291.97  E-value: 2.86e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  37 NLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRkdNRRMAYHPLSHLEIHEQDGLKELQQINPI 116
Cdd:COG2008   25 NVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRP--GDEVICHETAHIYVDEGGAPEALSGVKLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 117 LLGTAERLLTIEDIKAL-------QEPVSSVLLELPQReiGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFYEK 189
Cdd:COG2008  103 PVPGEDGKLTPEDLEAAirpgdvhFPQPGLVSLENTTE--GGTVYPLEELRAIAAVAREHGLPLHLDGARLFNAAAALGV 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 190 SAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAKKL 269
Cdd:COG2008  181 SLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQGLAALEDDLERLAEDHAMARRL 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749816 270 AERFNACDGVKtVPEVPVSNMFHVHFEKSvdvigtkLAEIQDETGVGISGYLQEKAEDVCGFEVSVGD 337
Cdd:COG2008  261 AEGLAALPGVR-VPEPVETNIVFVILPDE-------LAERLREKGVLFYPWGPGAVRLVTHWDTTEED 320
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
37-294 1.02e-41

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 147.36  E-value: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816   37 NLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNRRMAYHplSHLEIHEQDGLKELQQINPI 116
Cdd:pfam01212  22 MVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEP--AHIHFDETGGHAELGGVQPR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  117 LLGTAER-LLTIEDIKAL--------QEPVSSVLLELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFY 187
Cdd:pfam01212 100 PLDGDEAgNMDLEDLEAAirevgadiFPPTGLISLENTHNSAGGQVVSLENLREIAALAREHGIPVHLDGARFANAAVAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  188 EKSAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAK 267
Cdd:pfam01212 180 GVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAAAGLRALEEGVARLARDHATAR 259

                         250       260
                  ....*....|....*....|....*..
gi 502749816  268 KLAERFNACDGVKTVPEVPVSNMFHVH 294
Cdd:pfam01212 260 RLAEGLELLRLAIPRRVYTNTHMVYVA 286
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 34-317 2.49e-39

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: 142.47  E-value: 2.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  34 IDENLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNrrMAYHPLSHLEIHEQDGLKELQQI 113
Cdd:cd06502   19 AAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGS--VICHETAHIYTDEAGAPEFLSGV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 114 NPILLGTAERLLTIEDIKALQEPVSSV------LLELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFY 187
Cdd:cd06502   97 KLLPVPGENGKLTPEDLEAAIRPRDDIhfpppsLVSLENTTEGGTVYPLDELKAISALAKENGLPLHLDGARLANAAAAL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 188 EKSAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGdLISLYPYILSA-DYYFDKRI--GKMASYYA 264
Cdd:cd06502  177 GVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGG-GMRQSGFLAAAgLAALENDLwlRRLRHDHE 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502749816 265 AAKKLAErfnACDGVKTVPEVPVSNMFHVHFEKSVDVIGTKLAEIQDETGVGI 317
Cdd:cd06502  256 MARRLAE---ALEELGGLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGV 305
PLN02721 PLN02721
threonine aldolase
 41-319 2.76e-37

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 137.13  E-value: 2.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  41 DIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRK-------DNrrmayhplSHLEIHEQDGLKELQQI 113
Cdd:PLN02721  34 DVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRgsevilgDN--------SHIHLYENGGISTLGGV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 114 NP-ILLGTAERLLTIEDIKALQEPVSS--------VLLELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEIT 184
Cdd:PLN02721 106 HPrTVKNNEDGTMDLDAIEAAIRPKGDdhfpttrlICLENTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARIFNAS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 185 PFYEKSAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYA 264
Cdd:PLN02721 186 VALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQVGVLAAAALVALQENVPKLEDDHK 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502749816 265 AAKKLAERFNACDGVKTVPEVPVSNMFHVHFEKSVDVIGTKLAEIQDETGVGISG 319
Cdd:PLN02721 266 KAKLLAEGLNQIKGLRVNVAAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMP 320
GntG_guanitoxin NF041359
GntG family PLP-dependent aldolase;
41-337 1.27e-31

GntG family PLP-dependent aldolase;


Pssm-ID: 469251 [Multi-domain]  Cd Length: 342  Bit Score: 121.78  E-value: 1.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  41 DIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNrrMAYHPLSHLEIHEQDGLKELQQINPILLGT 120
Cdd:NF041359  31 DVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCGRGEE--YIVGDQAHIYLYEAGGAAVLGGIHPQPVPN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 121 -AERLLTIEDIKA------LQEPVSSVL-LELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFYEKSAE 192
Cdd:NF041359 109 qPDGSLDLDQVRAairpddEHFPRTRLIcLENTHNRCGGKVLPLEYLAAVRDLAHEHGLALHLDGARLFNAAVALGVDPA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 193 EICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAKKLAER 272
Cdd:NF041359 189 DLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLAAAGIVALEEMVERLADDHANAQRLAEG 268

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502749816 273 FNACDGVKTVPEVPVSNMfhVHFEKSVDVIGT-KLAEIQDETGVGISGYLQEKAEDVCGFEVSVGD 337
Cdd:NF041359 269 LAALPGVAIQTEPVQTNM--VFFSLHEPELDAqALLAFLKERGILLSDVGERRLRAVTHYGITRAD 332
 
Name Accession Description Interval E-value
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
37-337 2.86e-97

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 291.97  E-value: 2.86e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  37 NLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRkdNRRMAYHPLSHLEIHEQDGLKELQQINPI 116
Cdd:COG2008   25 NVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRP--GDEVICHETAHIYVDEGGAPEALSGVKLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 117 LLGTAERLLTIEDIKAL-------QEPVSSVLLELPQReiGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFYEK 189
Cdd:COG2008  103 PVPGEDGKLTPEDLEAAirpgdvhFPQPGLVSLENTTE--GGTVYPLEELRAIAAVAREHGLPLHLDGARLFNAAAALGV 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 190 SAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAKKL 269
Cdd:COG2008  181 SLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQGLAALEDDLERLAEDHAMARRL 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502749816 270 AERFNACDGVKtVPEVPVSNMFHVHFEKSvdvigtkLAEIQDETGVGISGYLQEKAEDVCGFEVSVGD 337
Cdd:COG2008  261 AEGLAALPGVR-VPEPVETNIVFVILPDE-------LAERLREKGVLFYPWGPGAVRLVTHWDTTEED 320
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
37-294 1.02e-41

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 147.36  E-value: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816   37 NLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNRRMAYHplSHLEIHEQDGLKELQQINPI 116
Cdd:pfam01212  22 MVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEP--AHIHFDETGGHAELGGVQPR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  117 LLGTAER-LLTIEDIKAL--------QEPVSSVLLELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFY 187
Cdd:pfam01212 100 PLDGDEAgNMDLEDLEAAirevgadiFPPTGLISLENTHNSAGGQVVSLENLREIAALAREHGIPVHLDGARFANAAVAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  188 EKSAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAK 267
Cdd:pfam01212 180 GVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAAAGLRALEEGVARLARDHATAR 259

                         250       260
                  ....*....|....*....|....*..
gi 502749816  268 KLAERFNACDGVKTVPEVPVSNMFHVH 294
Cdd:pfam01212 260 RLAEGLELLRLAIPRRVYTNTHMVYVA 286
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 34-317 2.49e-39

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: 142.47  E-value: 2.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  34 IDENLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNrrMAYHPLSHLEIHEQDGLKELQQI 113
Cdd:cd06502   19 AAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGS--VICHETAHIYTDEAGAPEFLSGV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 114 NPILLGTAERLLTIEDIKALQEPVSSV------LLELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFY 187
Cdd:cd06502   97 KLLPVPGENGKLTPEDLEAAIRPRDDIhfpppsLVSLENTTEGGTVYPLDELKAISALAKENGLPLHLDGARLANAAAAL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 188 EKSAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGdLISLYPYILSA-DYYFDKRI--GKMASYYA 264
Cdd:cd06502  177 GVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGG-GMRQSGFLAAAgLAALENDLwlRRLRHDHE 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502749816 265 AAKKLAErfnACDGVKTVPEVPVSNMFHVHFEKSVDVIGTKLAEIQDETGVGI 317
Cdd:cd06502  256 MARRLAE---ALEELGGLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGV 305
PLN02721 PLN02721
threonine aldolase
 41-319 2.76e-37

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 137.13  E-value: 2.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  41 DIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRK-------DNrrmayhplSHLEIHEQDGLKELQQI 113
Cdd:PLN02721  34 DVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRgsevilgDN--------SHIHLYENGGISTLGGV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 114 NP-ILLGTAERLLTIEDIKALQEPVSS--------VLLELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEIT 184
Cdd:PLN02721 106 HPrTVKNNEDGTMDLDAIEAAIRPKGDdhfpttrlICLENTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARIFNAS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 185 PFYEKSAEEICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYA 264
Cdd:PLN02721 186 VALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQVGVLAAAALVALQENVPKLEDDHK 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502749816 265 AAKKLAERFNACDGVKTVPEVPVSNMFHVHFEKSVDVIGTKLAEIQDETGVGISG 319
Cdd:PLN02721 266 KAKLLAEGLNQIKGLRVNVAAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMP 320
GntG_guanitoxin NF041359
GntG family PLP-dependent aldolase;
41-337 1.27e-31

GntG family PLP-dependent aldolase;


Pssm-ID: 469251 [Multi-domain]  Cd Length: 342  Bit Score: 121.78  E-value: 1.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  41 DIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNrrMAYHPLSHLEIHEQDGLKELQQINPILLGT 120
Cdd:NF041359  31 DVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCGRGEE--YIVGDQAHIYLYEAGGAAVLGGIHPQPVPN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 121 -AERLLTIEDIKA------LQEPVSSVL-LELPQREIGGQLPSFEELEEISQYCKAQGIALHLDGARLWEITPFYEKSAE 192
Cdd:NF041359 109 qPDGSLDLDQVRAairpddEHFPRTRLIcLENTHNRCGGKVLPLEYLAAVRDLAHEHGLALHLDGARLFNAAVALGVDPA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 193 EICALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDLISLYPYILSADYYFDKRIGKMASYYAAAKKLAER 272
Cdd:NF041359 189 DLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLAAAGIVALEEMVERLADDHANAQRLAEG 268

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502749816 273 FNACDGVKTVPEVPVSNMfhVHFEKSVDVIGT-KLAEIQDETGVGISGYLQEKAEDVCGFEVSVGD 337
Cdd:NF041359 269 LAALPGVAIQTEPVQTNM--VFFSLHEPELDAqALLAFLKERGILLSDVGERRLRAVTHYGITRAD 332
PRK10534 PRK10534
L-threonine aldolase; Provisional
 41-238 1.29e-18

L-threonine aldolase; Provisional


Pssm-ID: 236710 [Multi-domain]  Cd Length: 333  Bit Score: 85.58  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  41 DIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALRIWADRKDNRRMAyhPLSHLEIHEQDGLKELQQINP-ILLG 119
Cdd:PRK10534  28 DVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCERGEEYIVG--QAAHNYLYEAGGAAVLGSIQPqPIDA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 120 TAERLLTIEDIKALQEP-----VSSVLLELPQREIGGQLPsFEELEEISQYCKAQGIALHLDGARLWEITPFYEKSAEEI 194
Cdd:PRK10534 106 AADGTLPLDKVAAKIKPddihfARTRLLSLENTHNGKVLP-REYLKQAWEFTRERNLALHVDGARIFNAVVAYGCELKEI 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 502749816 195 CALFDSVYVSFYKGIGAIAGAILAGDADFVQEAKIWKRRYGGDL 238
Cdd:PRK10534 185 TQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGM 228
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 49-220 3.67e-06

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: 46.61  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  49 IEDFQTKIAKIL--GKEEAVFFPSGTMAQQIA---LRIWADRKDNRRMAYHplSHLEIHEqdglkELQQINPIL---LGT 120
Cdd:cd01494    2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAAllaLLGPGDEVIVDANGHG--SRYWVAA-----ELAGAKPVPvpvDDA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816 121 AERLLTIEDIK--ALQEPVSSVLLELPQREIGGQLPsfeeLEEISQYCKAQGIALHLDGARLWEITPFYEKSAEEICAlf 198
Cdd:cd01494   75 GYGGLDVAILEelKAKPNVALIVITPNTTSGGVLVP----LKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA-- 148

                        170       180
                 ....*....|....*....|..
gi 502749816 199 DSVYVSFYKGIGAIAGAILAGD 220
Cdd:cd01494  149 DVVTFSLHKNLGGEGGGVVIVK 170
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
28-212 8.97e-05

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 43.95  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  28 KEAFQNIDEnLESDIYGNGAIIEDFQTKIAKIL------------GKEEAVFFPS-GTMAQQIALR--IWADRKDNRRMA 92
Cdd:PRK02948  14 KEALQTYQK-AASQYFGNESSLHDIGGTASSLLqvcrktfaemigGEEQGIYFTSgGTESNYLAIQslLNALPQNKKHII 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  93 YHPLSHLEIH------EQDGLkELQQINPILLGtaerLLTIEDI-KALQEPVSSVLLELPQREIGGQLPsfeeLEEISQY 165
Cdd:PRK02948  93 TTPMEHASIHsyfqslESQGY-TVTEIPVDKSG----LIRLVDLeRAITPDTVLASIQHANSEIGTIQP----IAEIGAL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502749816 166 CKAQGIALHLDGARLWEITPFYEKsAEEIcalfDSVYVSFY-----KGIGAI 212
Cdd:PRK02948 164 LKKYNVLFHSDCVQTFGKLPIDVF-EMGI----DSLSVSAHkiygpKGVGAV 210
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-295 1.07e-03

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 40.37  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816   26 VLKEAFQNIDENLESDIYGNGAIIEDFQTKIAKILG--------KEEAVFFPSGTMA-QQIALRIWADRKDnrRMAYHPL 96
Cdd:pfam00155  18 AVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGAnIEALIFLLANPGD--AILVPAP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816   97 SHLEIHeqDGLK----ELQQINpiLLGTAERLLTIEDIK-ALQEPVSSVLLELPQREIGgQLPSFEELEEISQYCKAQGI 171
Cdd:pfam00155  96 TYASYI--RIARlaggEVVRYP--LYDSNDFHLDFDALEaALKEKPKVVLHTSPHNPTG-TVATLEELEKLLDLAKEHNI 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502749816  172 ALHLDGArlWEITPFYEKSAEEICALFDS-----VYVSFYKGIGAiAG---AILAGDADFVQEAKIWKRRYGGDLISLYP 243
Cdd:pfam00155 171 LLLVDEA--YAGFVFGSPDAVATRALLAEgpnllVVGSFSKAFGL-AGwrvGYILGNAAVISQLRKLARPFYSSTHLQAA 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 502749816  244 Y--ILSADYYFDKRIGKMASYYAA-AKKLAERFNACdGVKTVPevPVSNMFHVHF 295
Cdd:pfam00155 248 AaaALSDPLLVASELEEMRQRIKErRDYLRDGLQAA-GLSVLP--SQAGFFLLTG 299
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
29-80 3.40e-03

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 38.90  E-value: 3.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502749816  29 EAFQNIDENLESDIYGNGAIIEDFQTKIAKILGKEEAVFFPSGTMAQQIALR 80
Cdd:COG0399   12 EEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALR 63
 
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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