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Conserved domains on  [gi|145323806|ref|NP_001077492|]
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threonine aldolase 1 [Arabidopsis thaliana]

Protein Classification

low specificity L-threonine aldolase( domain architecture ID 10010873)

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
PLN02721 PLN02721
threonine aldolase
1-338 0e+00

threonine aldolase


:

Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 657.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   1 MVMRSVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSE 80
Cdd:PLN02721   3 MVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  81 VILGDNCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRCLSVEYTE 160
Cdd:PLN02721  83 VILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIR-PKGDDHFPTTRLICLENTHANCGGRCLSVEYTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 161 KVGEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQ 240
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 241 IGVLCAAALVALQENLPKLQHDHKKAKLLA--------------AVETNMIFMDMEDGSRLTAEKLRKNLEENGILLIRG 306
Cdd:PLN02721 242 VGVLAAAALVALQENVPKLEDDHKKAKLLAeglnqikglrvnvaAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMPG 321
                        330       340       350
                 ....*....|....*....|....*....|..
gi 145323806 307 NSSRIRIVIHHQITTSDVHYTLSCFQQAMLTM 338
Cdd:PLN02721 322 NSSRIRVVTHHQISDSDVQYTLSCFQQAALTL 353
 
Name Accession Description Interval E-value
PLN02721 PLN02721
threonine aldolase
1-338 0e+00

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 657.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   1 MVMRSVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSE 80
Cdd:PLN02721   3 MVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  81 VILGDNCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRCLSVEYTE 160
Cdd:PLN02721  83 VILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIR-PKGDDHFPTTRLICLENTHANCGGRCLSVEYTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 161 KVGEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQ 240
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 241 IGVLCAAALVALQENLPKLQHDHKKAKLLA--------------AVETNMIFMDMEDGSRLTAEKLRKNLEENGILLIRG 306
Cdd:PLN02721 242 VGVLAAAALVALQENVPKLEDDHKKAKLLAeglnqikglrvnvaAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMPG 321
                        330       340       350
                 ....*....|....*....|....*....|..
gi 145323806 307 NSSRIRIVIHHQITTSDVHYTLSCFQQAMLTM 338
Cdd:PLN02721 322 NSSRIRVVTHHQISDSDVQYTLSCFQQAALTL 353
GntG_guanitoxin NF041359
GntG family PLP-dependent aldolase;
6-333 2.91e-151

GntG family PLP-dependent aldolase;


Pssm-ID: 469251 [Multi-domain]  Cd Length: 342  Bit Score: 428.79  E-value: 2.91e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   6 VDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:NF041359   5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCG-RGEEYIVGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  86 NCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDpkGSTFYPSTRLICLENTHANSGGRCLSVEYTEKVGEI 165
Cdd:NF041359  84 QAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRP--DDEHFPRTRLICLENTHNRCGGKVLPLEYLAAVRDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 166 AKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLC 245
Cdd:NF041359 162 AHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 246 AAALVALQENLPKLQHDHKKAKLLAA--------------VETNMIFMDMEDGSrLTAEKLRKNLEENGILLIRGNSSRI 311
Cdd:NF041359 242 AAGIVALEEMVERLADDHANAQRLAEglaalpgvaiqtepVQTNMVFFSLHEPE-LDAQALLAFLKERGILLSDVGERRL 320
                        330       340
                 ....*....|....*....|..
gi 145323806 312 RIVIHHQITTSDVHYTLSCFQQ 333
Cdd:NF041359 321 RAVTHYGITRADIDQAIDAIQE 342
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
7-283 7.86e-133

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 380.02  E-value: 7.86e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806    7 DLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCdVRGSEVILGDN 86
Cdd:pfam01212   1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHC-QRGDEVICGEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   87 CHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFyPSTRLICLENTHANSGGRCLSVEYTEKVGEIA 166
Cdd:pfam01212  80 AHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGADIF-PPTGLISLENTHNSAGGQVVSLENLREIAALA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  167 KRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCA 246
Cdd:pfam01212 159 REHGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145323806  247 AALVALQENLPKLQHDHKKAKLLAA------------VETNMIFMDMED 283
Cdd:pfam01212 239 AGLRALEEGVARLARDHATARRLAEglellrlaiprrVYTNTHMVYVAA 287
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
3-335 1.94e-132

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 380.57  E-value: 1.94e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   3 MRsVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVI 82
Cdd:COG2008    1 MM-IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTR-PGDEVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  83 LGDNCHIHVYENGGISTIGGVHPKTVKNEeDGTMDLEAIEAAIRDpkGSTFYPSTRLICLENTHanSGGRCLSVEYTEKV 162
Cdd:COG2008   79 CHETAHIYVDEGGAPEALSGVKLLPVPGE-DGKLTPEDLEAAIRP--GDVHFPQPGLVSLENTT--EGGTVYPLEELRAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 163 GEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIG 242
Cdd:COG2008  154 AAVAREHGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 243 VLCAAALVALQENLPKLQHDHKKAKLLAA-------------VETNMIFMDMEDGsrltaekLRKNLEENGILLIRGNSS 309
Cdd:COG2008  234 FLAAQGLAALEDDLERLAEDHAMARRLAEglaalpgvrvpepVETNIVFVILPDE-------LAERLREKGVLFYPWGPG 306
                        330       340
                 ....*....|....*....|....*.
gi 145323806 310 RIRIVIHHQITTSDVHYTLSCFQQAM 335
Cdd:COG2008  307 AVRLVTHWDTTEEDVDAFLAALAELL 332
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
7-324 5.69e-109

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: 321.20  E-value: 5.69e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   7 DLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGDN 86
Cdd:cd06502    1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQ-PGGSVICHET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  87 CHIHVYENGGISTIGGVHPKTVKNEeDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRclSVEYTEKVGEIA 166
Cdd:cd06502   80 AHIYTDEAGAPEFLSGVKLLPVPGE-NGKLTPEDLEAAIR-PRDDIHFPPPSLVSLENTTEGGTVY--PLDELKAISALA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 167 KRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCA 246
Cdd:cd06502  156 KENGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 247 AALVALQENL--PKLQHDHKKAKLLAA-----------VETNMIFMDMEDGSRLTAEKLRKNLEEN--GILLIRGNSSRI 311
Cdd:cd06502  236 AGLAALENDLwlRRLRHDHEMARRLAEaleelggleseVQTNIVLLDPVEANAVFVELSKEAIERRgeGVLFYAWGEGGV 315
                        330
                 ....*....|...
gi 145323806 312 RIVIHHQITTSDV 324
Cdd:cd06502  316 RFVTHWDTTEEDV 328
 
Name Accession Description Interval E-value
PLN02721 PLN02721
threonine aldolase
1-338 0e+00

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 657.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   1 MVMRSVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSE 80
Cdd:PLN02721   3 MVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDVRGSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  81 VILGDNCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRCLSVEYTE 160
Cdd:PLN02721  83 VILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIR-PKGDDHFPTTRLICLENTHANCGGRCLSVEYTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 161 KVGEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQ 240
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 241 IGVLCAAALVALQENLPKLQHDHKKAKLLA--------------AVETNMIFMDMEDGSRLTAEKLRKNLEENGILLIRG 306
Cdd:PLN02721 242 VGVLAAAALVALQENVPKLEDDHKKAKLLAeglnqikglrvnvaAVETNIVYFDITDGSRITAEKLCKSLEEHGVLLMPG 321
                        330       340       350
                 ....*....|....*....|....*....|..
gi 145323806 307 NSSRIRIVIHHQITTSDVHYTLSCFQQAMLTM 338
Cdd:PLN02721 322 NSSRIRVVTHHQISDSDVQYTLSCFQQAALTL 353
GntG_guanitoxin NF041359
GntG family PLP-dependent aldolase;
6-333 2.91e-151

GntG family PLP-dependent aldolase;


Pssm-ID: 469251 [Multi-domain]  Cd Length: 342  Bit Score: 428.79  E-value: 2.91e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   6 VDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:NF041359   5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCG-RGEEYIVGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  86 NCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDpkGSTFYPSTRLICLENTHANSGGRCLSVEYTEKVGEI 165
Cdd:NF041359  84 QAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRP--DDEHFPRTRLICLENTHNRCGGKVLPLEYLAAVRDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 166 AKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLC 245
Cdd:NF041359 162 AHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 246 AAALVALQENLPKLQHDHKKAKLLAA--------------VETNMIFMDMEDGSrLTAEKLRKNLEENGILLIRGNSSRI 311
Cdd:NF041359 242 AAGIVALEEMVERLADDHANAQRLAEglaalpgvaiqtepVQTNMVFFSLHEPE-LDAQALLAFLKERGILLSDVGERRL 320
                        330       340
                 ....*....|....*....|..
gi 145323806 312 RIVIHHQITTSDVHYTLSCFQQ 333
Cdd:NF041359 321 RAVTHYGITRADIDQAIDAIQE 342
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
7-283 7.86e-133

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 380.02  E-value: 7.86e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806    7 DLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCdVRGSEVILGDN 86
Cdd:pfam01212   1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHC-QRGDEVICGEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   87 CHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFyPSTRLICLENTHANSGGRCLSVEYTEKVGEIA 166
Cdd:pfam01212  80 AHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGADIF-PPTGLISLENTHNSAGGQVVSLENLREIAALA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  167 KRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCA 246
Cdd:pfam01212 159 REHGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145323806  247 AALVALQENLPKLQHDHKKAKLLAA------------VETNMIFMDMED 283
Cdd:pfam01212 239 AGLRALEEGVARLARDHATARRLAEglellrlaiprrVYTNTHMVYVAA 287
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
3-335 1.94e-132

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 380.57  E-value: 1.94e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   3 MRsVDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVI 82
Cdd:COG2008    1 MM-IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTR-PGDEVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  83 LGDNCHIHVYENGGISTIGGVHPKTVKNEeDGTMDLEAIEAAIRDpkGSTFYPSTRLICLENTHanSGGRCLSVEYTEKV 162
Cdd:COG2008   79 CHETAHIYVDEGGAPEALSGVKLLPVPGE-DGKLTPEDLEAAIRP--GDVHFPQPGLVSLENTT--EGGTVYPLEELRAI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 163 GEIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIG 242
Cdd:COG2008  154 AAVAREHGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 243 VLCAAALVALQENLPKLQHDHKKAKLLAA-------------VETNMIFMDMEDGsrltaekLRKNLEENGILLIRGNSS 309
Cdd:COG2008  234 FLAAQGLAALEDDLERLAEDHAMARRLAEglaalpgvrvpepVETNIVFVILPDE-------LAERLREKGVLFYPWGPG 306
                        330       340
                 ....*....|....*....|....*.
gi 145323806 310 RIRIVIHHQITTSDVHYTLSCFQQAM 335
Cdd:COG2008  307 AVRLVTHWDTTEEDVDAFLAALAELL 332
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
7-324 5.69e-109

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: 321.20  E-value: 5.69e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   7 DLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGDN 86
Cdd:cd06502    1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQ-PGGSVICHET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  87 CHIHVYENGGISTIGGVHPKTVKNEeDGTMDLEAIEAAIRdPKGSTFYPSTRLICLENTHANSGGRclSVEYTEKVGEIA 166
Cdd:cd06502   80 AHIYTDEAGAPEFLSGVKLLPVPGE-NGKLTPEDLEAAIR-PRDDIHFPPPSLVSLENTTEGGTVY--PLDELKAISALA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 167 KRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLCA 246
Cdd:cd06502  156 KENGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 247 AALVALQENL--PKLQHDHKKAKLLAA-----------VETNMIFMDMEDGSRLTAEKLRKNLEEN--GILLIRGNSSRI 311
Cdd:cd06502  236 AGLAALENDLwlRRLRHDHEMARRLAEaleelggleseVQTNIVLLDPVEANAVFVELSKEAIERRgeGVLFYAWGEGGV 315
                        330
                 ....*....|...
gi 145323806 312 RIVIHHQITTSDV 324
Cdd:cd06502  316 RFVTHWDTTEEDV 328
PRK10534 PRK10534
L-threonine aldolase; Provisional
6-324 1.95e-99

L-threonine aldolase; Provisional


Pssm-ID: 236710 [Multi-domain]  Cd Length: 333  Bit Score: 297.06  E-value: 1.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   6 VDLRSDTVTRPTDAMREAMCNAEVDDDVLGYDPTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:PRK10534   2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCE-RGEEYIVGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  86 NCHIHVYENGGISTIGGVHPKTVKNEEDGTMDLEAIEAAIRdPKGSTFYPsTRLICLENTHansGGRCLSVEYTEKVGEI 165
Cdd:PRK10534  81 AAHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIK-PDDIHFAR-TRLLSLENTH---NGKVLPREYLKQAWEF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 166 AKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVCLSKGLGAPVGSVIVGSQSFIEKAKTVRKTLGGGMRQIGVLC 245
Cdd:PRK10534 156 TRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 246 AAALVALQENLPKLQHDHKKAKLLAAV-----------ETNMIFMDMEDGSrltAEKLRKNLEENGILLirgNSSRI-RI 313
Cdd:PRK10534 236 AAGLYALKHNVARLQEDHDNAAWLAEQlreagadvmrqDTNMLFVRVGEEQ---AAALGEYMRERNVLI---NASPIvRL 309
                        330
                 ....*....|.
gi 145323806 314 VIHHQITTSDV 324
Cdd:PRK10534 310 VTHLDVSREQL 320
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
52-219 4.29e-18

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: 80.50  E-value: 4.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  52 GKEAALFVPSGTMGNLISVMVHCDvRGSEVILGDNCHIHVYENGGisTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKgs 131
Cdd:cd01494   16 GNDKAVFVPSGTGANEAALLALLG-PGDEVIVDANGHGSRYWVAA--ELAGAKPVPVPVDDAGYGGLDVAILEELKAK-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 132 tfyPSTRLICLENTHANSGGRCLSVEytekVGEIAKRHGVKLHIDGARLFNASIALGVPVHklVKAADSVQVCLSKGLGA 211
Cdd:cd01494   91 ---PNVALIVITPNTTSGGVLVPLKE----IRKIAKEYGILLLVDAASAGGASPAPGVLIP--EGGADVVTFSLHKNLGG 161

                 ....*...
gi 145323806 212 PVGSVIVG 219
Cdd:cd01494  162 EGGGVVIV 169
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
38-238 2.90e-11

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 63.76  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  38 PTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDVRGSEVILGDNC-------HIHVYENGGISTiggvhpKTVkn 110
Cdd:cd00614   40 PTVDALEKKLAALEGGEAALAFSSG-MAAISTVLLALLKAGDHVVASDDLyggtyrlFERLLPKLGIEV------TFV-- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 111 eeDGTmDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSGGRCLSVeytEKVGEIAKRHGVKLHIDgarlfnASIALGVP 190
Cdd:cd00614  111 --DPD-DPEALEAAIK--------PETKLVYVE-SPTNPTLKVVDI---EAIAELAHEHGALLVVD------NTFATPYL 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145323806 191 VHKLVKAADSVQVCLSK---GLGAPVGSVIVGSQS-FIEKAKTVRKTLGGGM 238
Cdd:cd00614  170 QRPLELGADIVVHSATKyigGHSDVIAGVVVGSGEaLIQRLRFLRLALGTIL 221
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
16-315 3.62e-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: 60.43  E-value: 3.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  16 PTDAMREAMCNAEVDDDVLGYDPTA--RRLEEEMAKMMGK--------EAALFVPSGTMGNLISVMVHCDvRGSEVILGD 85
Cdd:cd00609   12 PPPEVLEALAAAALRAGLLGYYPDPglPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLN-PGDEVLVPD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  86 NCHiHVYENggISTIGGVHPKTVKNEEDGTM--DLEAIEAAIRdpkgstfyPSTRLICLeNTHANSGGRCLSVEYTEKVG 163
Cdd:cd00609   91 PTY-PGYEA--AARLAGAEVVPVPLDEEGGFllDLELLEAAKT--------PKTKLLYL-NNPNNPTGAVLSEEELEELA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 164 EIAKRHGVKLHIDGARLFNASIALGVPVHKLVKAADSVQVC--LSKGLGAP---VGSVIVGSQSFIEKAKTVRKTLGGGM 238
Cdd:cd00609  159 ELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLrsFSKTFGLPglrIGYLIAPPEELLERLKKLLPYTTSGP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 239 RQIG-VLCAAALVALQENLPKLQHDHKK--AKLLAAVE------------TNMIFMDMEDGSrlTAEKLRKNLEENGILL 303
Cdd:cd00609  239 STLSqAAAAAALDDGEEHLEELRERYRRrrDALLEALKelgplvvvkpsgGFFLWLDLPEGD--DEEFLERLLLEAGVVV 316
                        330
                 ....*....|....*...
gi 145323806 304 IRGNS------SRIRIVI 315
Cdd:cd00609  317 RPGSAfgeggeGFVRLSF 334
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
38-215 4.90e-10

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 59.91  E-value: 4.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  38 PTARRLEEEMAKMMGKEAAL--------FVPSGTMGNLISVMVH-------------CDVRGSEVILGDNCHIHVYENGg 96
Cdd:cd06450   34 PAATEMEAEVVNWLAKLFGLpsedadgvFTSGGSESNLLALLAArdrarkrlkagggRGIDKLVIVCSDQAHVSVEKAA- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  97 isTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFYPstrlICLENTHANSGgrCLSVEYTEKVGEIAKRHGVKLHID 176
Cdd:cd06450  113 --AYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNP----IMVVATAGTTD--TGAIDPLEEIADLAEKYDLWLHVD 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 145323806 177 GArlFNASIALGV-PVHKL--VKAADSVQVCLSKGLGAPVGS 215
Cdd:cd06450  185 AA--YGGFLLPFPePRHLDfgIERVDSISVDPHKYGLVPLGC 224
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-326 1.54e-09

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 58.47  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   43 LEEEMAKMMG--------KEAALFVPSGTMGNLISVMVHCDVRGSEVILGDNCHIHVYENGGISTiGGVHPKTVKNEEDG 114
Cdd:pfam00155  44 LREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAG-GEVVRYPLYDSNDF 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  115 TMDLEAIEAAIRDPkgstfypsTRLICLENTHANSgGRCLSVEYTEKVGEIAKRHGVKL-----HIDGArlFNASIAlgV 189
Cdd:pfam00155 123 HLDFDALEAALKEK--------PKVVLHTSPHNPT-GTVATLEELEKLLDLAKEHNILLlvdeaYAGFV--FGSPDA--V 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  190 PVHKLVKAADSVQVC--LSKGLGAP---VGSVIVGSqsfiekakTVRKTLGGGMRQI---GVLCAAALVALQENLPKLQH 261
Cdd:pfam00155 190 ATRALLAEGPNLLVVgsFSKAFGLAgwrVGYILGNA--------AVISQLRKLARPFyssTHLQAAAAAALSDPLLVASE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  262 DHKKAKLLAAV------------------ETNMIFMDmeDGSRLTAEKLRKNL-EENGILLIRGNS----SRIRIVIHHq 318
Cdd:pfam00155 262 LEEMRQRIKERrdylrdglqaaglsvlpsQAGFFLLT--GLDPETAKELAQVLlEEVGVYVTPGSSpgvpGWLRITVAG- 338

                  ....*...
gi 145323806  319 ITTSDVHY 326
Cdd:pfam00155 339 GTEEELEE 346
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
38-215 4.77e-09

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: 57.53  E-value: 4.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  38 PTARRLEEEMAKMMGKEAAL-------FVPSGTMGNLISVMV--------------HCDVRGSEVILGDNCHIHVYENGG 96
Cdd:COG0076  103 PAATELEREVVRWLADLLGLpegaggvFTSGGTEANLLALLAardralarrvraegLPGAPRPRIVVSEEAHSSVDKAAR 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  97 ISTIGGVHPKTVKNEEDGTMDLEAIEAAIRDPKGSTFYPStrLIClenthANSGgrclSVEYT-----EKVGEIAKRHGV 171
Cdd:COG0076  183 LLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPI--AVV-----ATAG----TTNTGaidplAEIADIAREHGL 251
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 145323806 172 KLHIDGArlFNASIAL---GVPVHKLVKAADSVQVCLSKGLGAPVGS 215
Cdd:COG0076  252 WLHVDAA--YGGFALPspeLRHLLDGIERADSITVDPHKWLYVPYGC 296
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
102-238 1.35e-07

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.83  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 102 GVHPKTVKNEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLenTHA-NSGGRCLSVEyteKVGEIAKRHGVKLHIDGARl 180
Cdd:COG0520  128 GAEVRVIPLDEDGELDLEALEALLT--------PRTKLVAV--THVsNVTGTVNPVK---EIAALAHAHGALVLVDGAQ- 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145323806 181 fnasialGVPVHKL-VKAADSVQVCLS--KgLGAPVGS-VIVGSQSFIEKAKTVRktLGGGM 238
Cdd:COG0520  194 -------SVPHLPVdVQALGCDFYAFSghK-LYGPTGIgVLYGKRELLEALPPFL--GGGGM 245
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
9-238 6.88e-07

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 50.43  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   9 RSDTVTRPTDAMREAMCNAEVDddvlGYD------PTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDVRGSEVI 82
Cdd:COG0626   27 LTSTFVFPSAEALAARFAGEEG----GYIysrygnPTRRALEEALAALEGGEAALAFASG-MAAISAVLLALLKAGDHVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  83 LGDNC-----HI--HVYENGGISTIggvhpkTVkneeDGTmDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSGGRCLS 155
Cdd:COG0626  102 ASDDLyggtrRLldKVLARFGIEVT------FV----DPT-DLAAVEAAIR--------PNTKLVFLE-TPSNPTLEVVD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 156 VeytEKVGEIAKRHGVKLHID----GARLFNAsIALGvpvhklvkaAD-SVQvCLSKGLG----APVGSVIVGSQSFIEK 226
Cdd:COG0626  162 I---AAIAAIAHAAGALLVVDntfaTPLLQRP-LELG---------ADiVVH-SATKYLGghsdVLGGAVVGRDEELAER 227
                        250
                 ....*....|..
gi 145323806 227 AKTVRKTLGGGM 238
Cdd:COG0626  228 LRFLQNALGAVL 239
Cys_Met_Meta_PP pfam01053
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ...
35-238 1.80e-06

Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.


Pssm-ID: 395837 [Multi-domain]  Cd Length: 376  Bit Score: 49.15  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   35 GYD------PTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVrGSEVILGDNCHihvyenGG-------ISTIG 101
Cdd:pfam01053  38 GYDysrsgnPTRDVLEERIAALEGGAAALAFSSGMAAITAAILALLKA-GDHIVATDDLY------GGtyrlfnkVLPRF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  102 GVHPKTVkneeDGTmDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSggrCLSVEYTEKVGEIAKRHGVKLHID---GA 178
Cdd:pfam01053 111 GIEVTFV----DTS-DPEDLEAAIK--------PNTKAVYLE-TPTNP---LLKVVDIEAIAKLAKKHGILVVVDntfAS 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145323806  179 RLFNASIALGvpvhklvkaADSVQVCLSKGLG----APVGSVIVGSQSFIEKAKTVRKTLGGGM 238
Cdd:pfam01053 174 PYLQRPLDLG---------ADIVVHSATKYIGghsdVVGGVIVVNGEELGKELYFLQNATGAVL 228
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
102-178 5.55e-06

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: 47.46  E-value: 5.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145323806 102 GVHPKTVKNEEDGTMDLEAIEAAIRDpkgstfypSTRLICLenTHA-NSGGrclSVEYTEKVGEIAKRHGVKLHIDGA 178
Cdd:cd06453  113 GAKLKVVPVDDDGQLDLEALEKLLTE--------RTKLVAV--THVsNVLG---TINPVKEIGEIAHEAGVPVLVDGA 177
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
38-173 8.43e-06

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 46.99  E-value: 8.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  38 PTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVhCDV-RGSEVILGD-------NChihvyenggISTIGGVhPKTVK 109
Cdd:COG0399   30 PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRA-LGIgPGDEVITPAftfvataNA---------ILYVGAT-PVFVD 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145323806 110 -NEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLenTHAnsGGRClsVEYtEKVGEIAKRHGVKL 173
Cdd:COG0399   99 iDPDTYNIDPEALEAAIT--------PRTKAIIP--VHL--YGQP--ADM-DAIMAIAKKHGLKV 148
MalY COG1168
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor ...
108-173 1.61e-05

Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 440782  Cd Length: 387  Bit Score: 46.24  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145323806 108 VKNEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLENTHaNSGGRCLSVEYTEKVGEIAKRHGVKL 173
Cdd:COG1168  141 ILEDGRYRIDFDDLEAKLD--------PGVKLLLLCNPH-NPTGRVWTREELERLAELCERHDVLV 197
PRK07324 PRK07324
transaminase; Validated
111-307 4.02e-05

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 44.93  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 111 EEDGTM-DLEAIEAAIRdpkgstfyPSTRLICLENTHaNSGGRCLSVEYTEKVGEIAKRHG-------VKLHIDGARLFn 182
Cdd:PRK07324 135 EENGWLpDLDELRRLVR--------PNTKLICINNAN-NPTGALMDRAYLEEIVEIARSVDayvlsdeVYRPLDEDGST- 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 183 ASIA----LGVPVHKLVKAAdSVQvclskglGAPVGSvIVGSQSFIEKAKTVR--KTLGGGM--RQIGVL---CAAALVA 251
Cdd:PRK07324 205 PSIAdlyeKGISTNSMSKTY-SLP-------GIRVGW-IAANEEVIDILRKYRdyTMICAGVfdDMLASLaleHRDAILE 275
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145323806 252 -----LQENLPKLQ---HDHKKAKLL--AAVETNMIFMDMEDGSRLTAEKLrknLEENGILLIRGN 307
Cdd:PRK07324 276 rnrkiVRTNLAILDewvAKEPRVSYVkpKAVSTSFVKLDVDMPSEDFCLKL---LKETGVLLVPGN 338
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
37-223 5.64e-05

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 44.70  E-value: 5.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  37 DPTARRLEEEMAKMMGKEAALFVPSGTMGNLIsvMVHCDVR-GSEVILGD-------NCHIHVYENGGISTIGGvhpktv 108
Cdd:PRK05994  62 NPTNAVLEERVAALEGGTAALAVASGHAAQFL--VFHTLLQpGDEFIAARklyggsiNQFGHAFKSFGWQVRWA------ 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 109 kneeDGTmDLEAIEAAIrDPKgstfypsTRLICLENThANSGGrclSVEYTEKVGEIAKRHGVKLHIDGARlfnASIALG 188
Cdd:PRK05994 134 ----DAD-DPASFERAI-TPR-------TKAIFIESI-ANPGG---TVTDIAAIAEVAHRAGLPLIVDNTL---ASPYLI 193
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 145323806 189 VPVHklvKAADSVQVCLSK---GLGAPVGSVIVGSQSF 223
Cdd:PRK05994 194 RPIE---HGADIVVHSLTKflgGHGNSMGGIIVDGGTF 228
PRK06767 PRK06767
methionine gamma-lyase; Provisional
37-238 1.17e-04

methionine gamma-lyase; Provisional


Pssm-ID: 180685 [Multi-domain]  Cd Length: 386  Bit Score: 43.68  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  37 DPTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDVRGSEVILGDNCHIHVYengGISTIggVHPKTVKNEEDGTM 116
Cdd:PRK06767  60 NPTVKLFEERMAVLEGGEEALAFGSG-MAAISATLIGFLKAGDHIICSNGLYGCTY---GFLEV--LEEKFMITHSFCDM 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 117 DLEA-IEAAIRdpkgstfyPSTRLICLEnTHANSGGRCLSVeytEKVGEIAKRHGVKLHIDGArlFnASIALGVPvhkLV 195
Cdd:PRK06767 134 ETEAdIENKIR--------PNTKLIFVE-TPINPTMKLIDL---KQVIRVAKRNGLLVIVDNT--F-CSPYLQRP---LE 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 145323806 196 KAADSVQVCLSK---GLGAPVGSVIVGSQSFI-EKAKTVRKTLGGGM 238
Cdd:PRK06767 196 LGCDAVVHSATKyigGHGDVVAGVTICKTRALaEKIRPMRKDIGGIM 242
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
38-178 1.20e-04

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 43.43  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   38 PTARRLEEEMAKMMGKEAALFVPSGTMGNLISVMVHCDVRGSEVILGD-------NCHIHVyenGGISTIGGVHPKTvkn 110
Cdd:pfam01041  24 PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSftfvataNAALRL---GAKPVFVDIDPDT--- 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145323806  111 eedGTMDLEAIEAAIRdpkgstfyPSTRLICLenthANSGGRCLSVeytEKVGEIAKRHGVKLHIDGA 178
Cdd:pfam01041  98 ---YNIDPEAIEAAIT--------PRTKAIIP----VHLYGQPADM---DAIRAIAARHGLPVIEDAA 147
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
8-179 3.12e-04

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 42.34  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   8 LRSDTVTRP--TDAMREAMCNAEVDDDVLGYDPTAR-----RLEEEMAKMMGKEAALFVPSGtmgnlisvmvhcdvRGSE 80
Cdd:cd00617   16 LRSEDVYIDllTDSGTGAMSDYQWAAMMLGDEAYAGsksfyDLEDAVQDLFGFKHIIPTHQG--------------RGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  81 VIL-------GD----NCHI-----HVYENGGIS---TIGGVHPKTVKNEEDGTMDLEAIEAAIrDPKGSTFYPstrLIC 141
Cdd:cd00617   82 NILfsillkpGRtvpsNMHFdttrgHIEANGAVPvdlVIDEAHDAQELIPFKGNIDVAKLEKLI-DEVGAENIP---YIV 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 145323806 142 LENTHANSGGRCLSVEYTEKVGEIAKRHGVKLHIDGAR 179
Cdd:cd00617  158 LTITNNTAGGQPVSMANLREVRELAHKYGIPVVLDAAR 195
PRK07671 PRK07671
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase;
37-236 4.21e-04

bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase;


Pssm-ID: 181076 [Multi-domain]  Cd Length: 377  Bit Score: 41.63  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  37 DPTARRLEEEMAKMMGKEAALFVPSGtMGNLISVMVHCDvRGSEVILGDNchihVYeNGGISTIGGVHPK-TVKNEEDGT 115
Cdd:PRK07671  49 NPTRAALEELIAVLEGGHAGFAFGSG-MAAITAVMMLFS-SGDHVILTDD----VY-GGTYRVMTKVLNRfGIEHTFVDT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 116 MDLEAIEAAIRdpkgstfyPSTRLICLEnTHANSggrCLSVEYTEKVGEIAKRHGVKLHIDG---ARLFNASIALGvpvh 192
Cdd:PRK07671 122 SNLEEVEEAIR--------PNTKAIYVE-TPTNP---LLKITDIKKISTIAKEKGLLTIVDNtfmTPYWQSPISLG---- 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 145323806 193 klvkaADSVQVCLSKGLGAP----VGSVIVGSQSFIEKAKTVRKTLGG 236
Cdd:PRK07671 186 -----ADIVLHSATKYLGGHsdvvAGLVVVNSPELAEDLHFVQNSTGG 228
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
31-178 4.90e-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: 41.47  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  31 DDVLgyDPT--ARRLEEEMAKMMGKEAALFVPSGT-MGNLISVMVHCDvRGSEVILGDNCHIHVYeNGGIstIGGVHPKT 107
Cdd:cd00615   52 DDLL--DPTgpIKEAQELAARAFGAKHTFFLVNGTsSSNKAVILAVCG-PGDKILIDRNCHKSVI-NGLV--LSGAVPVY 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 108 VKNEED------GTMDLEAIEAAI---RDPKG-----STFYpstrliclenthansgGRCLSveyTEKVGEIAKRHGVKL 173
Cdd:cd00615  126 LKPERNpyygiaGGIPPETFKKALiehPDAKAavitnPTYY----------------GICYN---LRKIVEEAHHRGLPV 186

                 ....*
gi 145323806 174 HIDGA 178
Cdd:cd00615  187 LVDEA 191
tnaA PRK13238
tryptophanase;
114-180 6.59e-04

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 41.34  E-value: 6.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145323806 114 GTMDLEAIEAAIRDpKGSTFYPstrLICLENTHANSGGRCLSVEYTEKVGEIAKRHGVKLHIDGARL 180
Cdd:PRK13238 159 GNFDLEKLEALIEE-VGAENVP---FIVMTITNNSAGGQPVSMANLRAVYEIAKKYGIPVVIDAARF 221
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
84-214 1.33e-03

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 40.09  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806   84 GDNCHIHVYENGgisTIGGVHPKTVKNEEDGTMDLEAIEAAI--RDPKGSTfypstrlICLENTHANSGGRClSVEYTEK 161
Cdd:pfam00282 151 SDQAHSSIEKAA---LYGGVKLREIPSDDNGKMRGMDLEKAIeeDKENGLI-------PFFVVATLGTTGSG-AFDDLQE 219
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145323806  162 VGEIAKRHGVKLHIDGArlfNASIALGVPVH----KLVKAADSVQVCLSKGLGAPVG 214
Cdd:pfam00282 220 LGDICAKHNLWLHVDAA---YGGSAFICPEFrhwlFGIERADSITFNPHKWMLVLLD 273
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
101-178 2.34e-03

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: 39.54  E-value: 2.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145323806  101 GGVHPKTVKNEEDGTMDLEAIEAAIRdpkgstfyPSTRLICLenTHA-NSGGRCLSVEyteKVGEIAKRHGVKLHIDGA 178
Cdd:pfam00266 112 TGARVRVLPLDEDGLLDLDELEKLIT--------PKTKLVAI--THVsNVTGTIQPVP---EIGKLAHQYGALVLVDAA 177
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
43-277 8.10e-03

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 37.91  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806  43 LEEEMAKMMGKEAALFVPSGTMGNLISVmvhcdvrGSEVILGDNCHIHVYENGGISTIGGV-HPKTVKN--EEDGTMDLE 119
Cdd:PRK13392  96 LERELADLHGKESALLFTSGYVSNDAAL-------STLGKLLPGCVILSDALNHASMIEGIrRSGAEKQvfRHNDLADLE 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 120 AIEAAIrDPKgstfypSTRLICLENTHANSGgrclSVEYTEKVGEIAKRHGVKLHID--------GARlfNASIAlgvPV 191
Cdd:PRK13392 169 EQLASV-DPD------RPKLIAFESVYSMDG----DIAPIEAICDLADRYNALTYVDevhavglyGAR--GGGIA---ER 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323806 192 HKLVKAADSVQVCLSKGLGApVGSVIVGSQSFIEkakTVRKTLGGGMRQIGV---LCAAALVALQ----ENLPKLQHDHK 264
Cdd:PRK13392 233 DGLMDRIDMIQGTLAKAFGC-LGGYIAASADLID---FVRSFAPGFIFTTALppaVAAGATAAIRhlktSQTERDAHQDR 308
                        250
                 ....*....|...
gi 145323806 265 KAKLLAAVETNMI 277
Cdd:PRK13392 309 VAALKAKLNANGI 321
 
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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