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Conserved domains on  [gi|1111000928|ref|XP_019326539|]
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PREDICTED: glutamate decarboxylase 2 [Aptenodytes forsteri]

Protein Classification

PLP-dependent decarboxylase( domain architecture ID 10447228)

PLP-dependent decarboxylase such as DOPA decarboxylase, glutamate decarboxylase, and histidine decarboxylase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
31-402 2.86e-156

Pyridoxal-dependent decarboxylase conserved domain;


:

Pssm-ID: 395219  Cd Length: 373  Bit Score: 448.41  E-value: 2.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  31 PNELLQEYNWELADQPQTLEEILLNCRTTLKYAIKTGH-PRYFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLL 109
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 110 EYVTLRKMREMVGWP----GGCGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMATIP-----RLVAFTSEHSHFSVKK 180
Cdd:pfam00282  81 ENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 181 GAAALGIGtdsVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAW 260
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 261 GGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFqqdkHYDLSYDTGDKALQCG 340
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLG----HTDSAYDTGHKQIPLS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1111000928 341 RHVDVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVFdgKPQHTNVCFWYI 402
Cdd:pfam00282 314 RRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
31-402 2.86e-156

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 448.41  E-value: 2.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  31 PNELLQEYNWELADQPQTLEEILLNCRTTLKYAIKTGH-PRYFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLL 109
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 110 EYVTLRKMREMVGWP----GGCGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMATIP-----RLVAFTSEHSHFSVKK 180
Cdd:pfam00282  81 ENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 181 GAAALGIGtdsVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAW 260
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 261 GGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFqqdkHYDLSYDTGDKALQCG 340
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLG----HTDSAYDTGHKQIPLS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1111000928 341 RHVDVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVFdgKPQHTNVCFWYI 402
Cdd:pfam00282 314 RRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
71-474 5.56e-146

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: 420.84  E-value: 5.56e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  71 YFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVGWPGGCGDGIFSPGGAISNMYAMLIARFK 150
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 151 MFPEVKEKGMATIPRLVAFTSEHSHFSVKKGAAALGIgtdSVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAG 230
Cdd:cd06450    81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 231 TTVYGAFDPLIAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVReeglmqs 310
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 311 cnqmhasylfqqdkhydlsydtgdkalqcgrhvdVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdG 390
Cdd:cd06450   231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--G 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 391 KPQHTNVCFWYIPPslrsmedneermSRLMKVAPVIKARMMEYGTTMVSYQPLGDKvNFFRMVISNPAATHQDIDFLIGE 470
Cdd:cd06450   275 EPNLSLVCFRLKPS------------VKLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341

                  ....
gi 1111000928 471 IERL 474
Cdd:cd06450   342 IERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
4-477 9.68e-145

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: 422.32  E-value: 9.68e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928   4 LQDVVDILLQYVvKSFDRSTKVIDfhyPNELLQEYNWELADQPQTLEEIL--LNcRTTLKYAIKTGHPRYFNQLSTGLDM 81
Cdd:COG0076     6 LHQALDLAADYL-AGLDRPVFGPS---PEELRAALDEPLPEEGLPPEEALaeLE-DLVLPGSVDWNHPRFLAFVTGGTTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  82 VGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVGWPGGCgDGIFSPGGAISNMYAMLIARFKMFPE-VKEKGM 160
Cdd:COG0076    81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGA-GGVFTSGGTEANLLALLAARDRALARrVRAEGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 161 ATIPRLVAFTSEHSHFSVKKGAAALGIGTDSVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPL 240
Cdd:COG0076   160 PGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 241 IAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLF 320
Cdd:COG0076   240 AEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 321 QQDkhyDLSYDTGDKALQCGRHVDVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFW 400
Cdd:COG0076   320 PAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFR 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111000928 401 YIPPSLRSM-EDNEErmsrlmkvapvIKARMMEYGTTMVSYQPLGDKVNfFRMVISNPAATHQDIDFLIGEIERLGQD 477
Cdd:COG0076   395 YKPAGLDEEdALNYA-----------LRDRLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
PLN02590 PLN02590
probable tyrosine decarboxylase
44-464 7.36e-42

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 156.41  E-value: 7.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  44 DQPQTLEEILLNCRTTLKYAIKTGH-PRYFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVG 122
Cdd:PLN02590  105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 123 WPG-----GCGDGIFSPGGAISNMYAMLIARFKMFPEVkekGMATIPRLVAFTSEHSHFSVKKGAAALGIGTDSVILIRC 197
Cdd:PLN02590  185 LPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 198 DERGK--MIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLN 275
Cdd:PLN02590  262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 276 GIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAK 355
Cdd:PLN02590  342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 356 GSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFWYIPPSLRSMEDNEERMSRLMKVAPVikarmmeyGT 435
Cdd:PLN02590  422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRYFSLVCFRLAPVDGDEDQCNERNRELLAAVNST--------GK 491
                         410       420
                  ....*....|....*....|....*....
gi 1111000928 436 TMVSYQPLGDKVnFFRMVISNPAATHQDI 464
Cdd:PLN02590  492 IFISHTALSGKF-VLRFAVGAPLTEEKHV 519
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
31-402 2.86e-156

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 448.41  E-value: 2.86e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  31 PNELLQEYNWELADQPQTLEEILLNCRTTLKYAIKTGH-PRYFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLL 109
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 110 EYVTLRKMREMVGWP----GGCGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMATIP-----RLVAFTSEHSHFSVKK 180
Cdd:pfam00282  81 ENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 181 GAAALGIGtdsVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAW 260
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 261 GGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFqqdkHYDLSYDTGDKALQCG 340
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLG----HTDSAYDTGHKQIPLS 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1111000928 341 RHVDVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVFdgKPQHTNVCFWYI 402
Cdd:pfam00282 314 RRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
71-474 5.56e-146

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: 420.84  E-value: 5.56e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  71 YFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVGWPGGCGDGIFSPGGAISNMYAMLIARFK 150
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 151 MFPEVKEKGMATIPRLVAFTSEHSHFSVKKGAAALGIgtdSVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAG 230
Cdd:cd06450    81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 231 TTVYGAFDPLIAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVReeglmqs 310
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 311 cnqmhasylfqqdkhydlsydtgdkalqcgrhvdVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdG 390
Cdd:cd06450   231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--G 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 391 KPQHTNVCFWYIPPslrsmedneermSRLMKVAPVIKARMMEYGTTMVSYQPLGDKvNFFRMVISNPAATHQDIDFLIGE 470
Cdd:cd06450   275 EPNLSLVCFRLKPS------------VKLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341

                  ....
gi 1111000928 471 IERL 474
Cdd:cd06450   342 IERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
4-477 9.68e-145

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: 422.32  E-value: 9.68e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928   4 LQDVVDILLQYVvKSFDRSTKVIDfhyPNELLQEYNWELADQPQTLEEIL--LNcRTTLKYAIKTGHPRYFNQLSTGLDM 81
Cdd:COG0076     6 LHQALDLAADYL-AGLDRPVFGPS---PEELRAALDEPLPEEGLPPEEALaeLE-DLVLPGSVDWNHPRFLAFVTGGTTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  82 VGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVGWPGGCgDGIFSPGGAISNMYAMLIARFKMFPE-VKEKGM 160
Cdd:COG0076    81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGA-GGVFTSGGTEANLLALLAARDRALARrVRAEGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 161 ATIPRLVAFTSEHSHFSVKKGAAALGIGTDSVILIRCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPL 240
Cdd:COG0076   160 PGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 241 IAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLNGIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLF 320
Cdd:COG0076   240 AEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 321 QQDkhyDLSYDTGDKALQCGRHVDVFKLWLMWRAKGSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFW 400
Cdd:COG0076   320 PAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFR 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111000928 401 YIPPSLRSM-EDNEErmsrlmkvapvIKARMMEYGTTMVSYQPLGDKVNfFRMVISNPAATHQDIDFLIGEIERLGQD 477
Cdd:COG0076   395 YKPAGLDEEdALNYA-----------LRDRLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
PLN02590 PLN02590
probable tyrosine decarboxylase
44-464 7.36e-42

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 156.41  E-value: 7.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  44 DQPQTLEEILLNCRTTLKYAIKTGH-PRYFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVG 122
Cdd:PLN02590  105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 123 WPG-----GCGDGIFSPGGAISNMYAMLIARFKMFPEVkekGMATIPRLVAFTSEHSHFSVKKGAAALGIGTDSVILIRC 197
Cdd:PLN02590  185 LPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 198 DERGK--MIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLN 275
Cdd:PLN02590  262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 276 GIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAK 355
Cdd:PLN02590  342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 356 GSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFWYIPPSLRSMEDNEERMSRLMKVAPVikarmmeyGT 435
Cdd:PLN02590  422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRYFSLVCFRLAPVDGDEDQCNERNRELLAAVNST--------GK 491
                         410       420
                  ....*....|....*....|....*....
gi 1111000928 436 TMVSYQPLGDKVnFFRMVISNPAATHQDI 464
Cdd:PLN02590  492 IFISHTALSGKF-VLRFAVGAPLTEEKHV 519
PLN02880 PLN02880
tyrosine decarboxylase
44-418 2.30e-34

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 134.65  E-value: 2.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928  44 DQPQTLEEILLNCRTTLKYAIKTGH-PRYFNQLSTGLDMVGLAADWLTSAANTNMFTYEIAPVFVLLEYVTLRKMREMVG 122
Cdd:PLN02880   57 NQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLN 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 123 WP-----GGCGDGIFSPGGAISNMYAMLIARFKMfpeVKEKGMATIPRLVAFTSEHSHFSVKKGAAALGIGTDSVILIR- 196
Cdd:PLN02880  137 LPeqflsTGNGGGVIQGTASEAVLVVLLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKt 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 197 -CDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAWGGGLLMSRKHKWKLN 275
Cdd:PLN02880  214 dSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYID 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 276 GIERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAK 355
Cdd:PLN02880  294 GVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLY 373
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1111000928 356 GSTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFWYIPPSlrSMEDNEERMSR 418
Cdd:PLN02880  374 GVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFSLVCFRLVPPK--NNEDNGNKLNH 432
PRK02769 PRK02769
histidine decarboxylase; Provisional
130-382 9.63e-23

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 99.73  E-value: 9.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 130 GIFSPGGAISNMYAMLIARfKMFPEVkekgmatiprlVAFTSEHSHFSVKKGAAALGIGTDsviLIRCDERGKMIPSDLE 209
Cdd:PRK02769   87 GYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKSR---VITSLPNGEIDYDDLI 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 210 RRILEAKQKgfvPFLVSATAGTTVYGAFDPLIAIADICKKYKI---WMHVDGAWGGGLLMSRKHKWKLNGIERANSVTWN 286
Cdd:PRK02769  152 SKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAIS 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 287 PHKMMGVPLQCSALLVREEGLMQscNQMHASYLfqqdkhydlsyDTGDKALQCGR--HVDVFkLWLMWRAKGSTGFEAQI 364
Cdd:PRK02769  229 GHKFIGSPMPCGIVLAKKKYVER--ISVDVDYI-----------GSRDQTISGSRngHTALL-LWAAIRSLGSKGLRQRV 294
                         250
                  ....*....|....*...
gi 1111000928 365 DKCLELAEYLYNKIKNRE 382
Cdd:PRK02769  295 QHCLDMAQYAVDRLQANG 312
PLN03032 PLN03032
serine decarboxylase; Provisional
130-379 4.84e-14

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 73.32  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 130 GIFSPGGAISNMYAMLIARFKMfpevkekgmatiPRLVAFTSEHSHFSVKKGAAALGIGTDSVILIrcdERGKMIPSDLE 209
Cdd:PLN03032   88 GYITTCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 210 RRILEAKQKgfvPFLVSATAGTTVYGAFDPLIAIADICKKYKI-----WMHVDGAWGGGLLMSRKHKWKLNGIERANSVT 284
Cdd:PLN03032  153 RALAKNRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVS 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 285 WNPHKMMGVPLQCSALLVREEGLMQscnqmhasylFQQDKHYDLSYDTGDKALQCGrHVDVFkLWLMWRAKGSTGFEAQI 364
Cdd:PLN03032  230 VSGHKFLGCPMPCGVALTRKKHVKA----------LSQNVEYLNSRDATIMGSRNG-HAPLY-LWYTLRRKGYRGIKRDV 297
                         250
                  ....*....|....*
gi 1111000928 365 DKCLELAEYLYNKIK 379
Cdd:PLN03032  298 QHCMRNAHYLKDRLT 312
PLN02263 PLN02263
serine decarboxylase
136-380 5.29e-13

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 70.62  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 136 GAISNMYAMLIARfKMFPEVkekgmatiprlVAFTSEHSHFSVKKGAAALGIGtdsVILIRCDERGKMIPSDLERRILEA 215
Cdd:PLN02263  161 GTEGNLHGILVGR-EVFPDG-----------ILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLAN 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 216 KQKgfvPFLVSATAGTTVYGAFDPLIAIADICKKY-----KIWMHVDGAWGGGLLMSRKHKWKLNGIERANSVTWNPHKM 290
Cdd:PLN02263  226 KDK---PAIINVNIGTTVKGAVDDLDLVIKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKF 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 291 MGVPLQCSALLVREEglmqscnqmHASYLfQQDKHYDLSYDTGDKALQCGrHVDVFkLWLMWRAKGSTGFEAQIDKCLEL 370
Cdd:PLN02263  303 VGCPMPCGVQITRME---------HINVL-SSNVEYLASRDATIMGSRNG-HAPIF-LWYTLNRKGYRGFQKEVQKCLRN 370
                         250
                  ....*....|
gi 1111000928 371 AEYLYNKIKN 380
Cdd:PLN02263  371 AHYLKDRLRE 380
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
124-303 1.26e-12

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: 65.87  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 124 PGGCGDGIFSPGGAISNMYAMLIARfkmfpevkekgmatIPRLVAFTSEHSHFSVKKGAAALgIGTDSVIlIRCDERGKM 203
Cdd:cd01494    14 QPGNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAEL-AGAKPVP-VPVDDAGYG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 204 IpsdLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAWGGGllmSRKHKWKLNGIERANSV 283
Cdd:cd01494    78 G---LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG---ASPAPGVLIPEGGADVV 151
                         170       180
                  ....*....|....*....|
gi 1111000928 284 TWNPHKMMGVPlQCSALLVR 303
Cdd:cd01494   152 TFSLHKNLGGE-GGGVVIVK 170
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
173-259 5.78e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 44.90  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 173 HSHFSVKKGAAALGIGTdsVILIRCDERGKMIPSDLERRILEAKQKGFVPF-LVSAT-----AGTTVYgAFDPLIAIADI 246
Cdd:pfam01212  81 HIHFDETGGHAELGGVQ--PRPLDGDEAGNMDLEDLEAAIREVGADIFPPTgLISLEnthnsAGGQVV-SLENLREIAAL 157
                          90
                  ....*....|...
gi 1111000928 247 CKKYKIWMHVDGA 259
Cdd:pfam01212 158 AREHGIPVHLDGA 170
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
224-399 2.36e-04

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: 43.39  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 224 LVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGAWGgglLMSRKHKWKLNGIERANSVTwnpHKMMGvPLQCSALLVR 303
Cdd:pfam00266 142 LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA---IGHRPIDVQKLGVDFLAFSG---HKLYG-PTGIGVLYGR 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 304 EEGLmqscNQMH-----ASYLFQQDKHYDLSYDTGDK----------ALQCGRHVDvfklWLMwrakgSTGFEAQIDKCL 368
Cdd:pfam00266 215 RDLL----EKMPpllggGGMIETVSLQESTFADAPWKfeagtpniagIIGLGAALE----YLS-----EIGLEAIEKHEH 281
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1111000928 369 ELAEYLYNKIKNREGYEmVFDGKPQHTNVCF 399
Cdd:pfam00266 282 ELAQYLYERLLSLPGIR-LYGPERRASIISF 311
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
232-317 1.85e-03

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: 40.31  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111000928 232 TVYGAFDPLIAIADICKKYKIWMHVDGAWGGGLLMS---RKHKWKLNGIERANSVtwnpHKMMGVPLQCSALLVREEGL- 307
Cdd:cd00615   164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKGDLVn 239
                          90
                  ....*....|...
gi 1111000928 308 ---MQSCNQMHAS 317
Cdd:cd00615   240 pdrVNEALNLHQS 252
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
199-259 2.58e-03

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: 40.01  E-value: 2.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1111000928 199 ERGKMIPSDLERRILEAKQKGFV-PFLVS---ATAGTTVYgAFDPLIAIADICKKYKIWMHVDGA 259
Cdd:cd06502   104 ENGKLTPEDLEAAIRPRDDIHFPpPSLVSlenTTEGGTVY-PLDELKAISALAKENGLPLHLDGA 167
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
192-259 7.18e-03

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 38.58  E-value: 7.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111000928 192 VILIRCDERGKMIPSDLERrILEAKQKgfvpfLVSATAGTTVYGAFDPLIAIADICKKYKIWMHVDGA 259
Cdd:COG0520   131 VRVIPLDEDGELDLEALEA-LLTPRTK-----LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA 192
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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