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Conserved domains on  [gi|1931223899|ref|XP_037296176|]
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LOW QUALITY PROTEIN: glutamate decarboxylase [Manduca sexta]

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;
91-460 1.67e-158

Pyridoxal-dependent decarboxylase conserved domain;


:

Pssm-ID: 395219  Cd Length: 373  Bit Score: 456.49  E-value: 1.67e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  91 PEEMVKILDLELHDEPLPLKQLLEDCKTALKYQVKTGH-PHFFNQLSCGLDIISLAGEWLTAAANTNMFTYEIAPVFILM 169
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 170 ENIVLEKMRSMIGW------KTGDSILAPGGSVSNLYAFLAARHRKFPQYKEKGL----SSIPGQLVMFTSDQCHYSVKS 239
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKpadsSGILAKLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 240 CASVCGLGtdyCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNATSGTTVLGAFDPLMEIADICQKYDMWMHVDAAW 319
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 320 GGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGILLSCNAMSAEYLFMTDKIydpqYDTGDKVIQC 399
Cdd:pfam00282 238 GGSAFICPEFRH-WLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSA----YDTGHKQIPL 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931223899 400 GRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPDkFHLILEPEMVNVSFWY 460
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGR-FEICAEVGLGLVCFRL 372
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
91-460 1.67e-158

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 456.49  E-value: 1.67e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  91 PEEMVKILDLELHDEPLPLKQLLEDCKTALKYQVKTGH-PHFFNQLSCGLDIISLAGEWLTAAANTNMFTYEIAPVFILM 169
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 170 ENIVLEKMRSMIGW------KTGDSILAPGGSVSNLYAFLAARHRKFPQYKEKGL----SSIPGQLVMFTSDQCHYSVKS 239
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKpadsSGILAKLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 240 CASVCGLGtdyCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNATSGTTVLGAFDPLMEIADICQKYDMWMHVDAAW 319
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 320 GGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGILLSCNAMSAEYLFMTDKIydpqYDTGDKVIQC 399
Cdd:pfam00282 238 GGSAFICPEFRH-WLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSA----YDTGHKQIPL 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931223899 400 GRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPDkFHLILEPEMVNVSFWY 460
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGR-FEICAEVGLGLVCFRL 372
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
59-536 1.58e-121

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: 365.31  E-value: 1.58e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  59 QTREFLARVIDVLLDYVQkvndRNEKILEFKMPEEMVKILDLELHDEPLPLKQLLED-CKTALKYQVKTGHPHFFNQLSC 137
Cdd:COG0076     1 EFRALLHQALDLAADYLA----GLDRPVFGPSPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 138 GLDIISLAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMIGW-KTGDSILAPGGSVSNLYAFLAARHRKFPQY-KE 215
Cdd:COG0076    77 GTTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALARRvRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 216 KGLSSIPgQLVMFTSDQCHYSVKSCASVCGLGTDYCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNATSGTTVLGA 295
Cdd:COG0076   157 EGLPGAP-RPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 296 FDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGILLSCNAMS 375
Cdd:COG0076   236 IDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRH-LLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 376 AEYLFMTDkiyDPQYDTGDKVIQCGRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPDkFHLILEPEMVN 455
Cdd:COG0076   315 ASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPG-FELLAPPELNI 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 456 VSFWYLPKQLRGIPHDaNKELRLgkvcaklkgKMMQAGTIMVGYQPDDRRPNfFRNIISSAAVTEKDVDFLLSEMDRLGQ 535
Cdd:COG0076   391 VCFRYKPAGLDEEDAL-NYALRD---------RLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAA 459

                  .
gi 1931223899 536 D 536
Cdd:COG0076   460 E 460
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
131-533 8.20e-115

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: 343.80  E-value: 8.20e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 131 FFNQLSCGLDIISLAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMIGW--KTGDSILAPGGSVSNLYAFLAARHR 208
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLpsEDADGVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 209 KFPQYKEKGLSSIPgQLVMFTSDQCHYSV-KSCAsvcgLGTDYCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNAT 287
Cdd:cd06450    81 ARKRLKAGGGRGID-KLVIVCSDQAHVSVeKAAA----YLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 288 SGTTVLGAFDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKyegi 367
Cdd:cd06450   156 AGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRH-LDFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 368 llscnamsaeylfmtdkiydpqydtgdkviqcgrhndIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPdKFHL 447
Cdd:cd06450   231 -------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADP-GFEL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 448 ILEPEMVNVSFWYLPKQlrgiphdankelRLGKVCAKLKGKMMQAGTIMVGYQPDDrRPNFFRNIISSAAVTEKDVDFLL 527
Cdd:cd06450   273 LGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLG-GPNVLRFVVTNPLTTRDDADALL 339

                  ....*.
gi 1931223899 528 SEMDRL 533
Cdd:cd06450   340 EDIERA 345
PLN02880 PLN02880
tyrosine decarboxylase
59-462 7.38e-35

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 136.96  E-value: 7.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  59 QTREFLARVIDVLLDYVQKVndRNEKILEFKMPEEMVKILDLELHDEPLPLKQLLEDCKTALKYQVKTGH-PHFFNQLSC 137
Cdd:PLN02880   14 QLRECGHRMVDFIADYYKSI--ENFPVLSQVQPGYLRELLPDSAPNQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 138 GLDIISLAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMIgwKTGDSILAPG-------GSVSN--LYAFLAARHR 208
Cdd:PLN02880   92 NSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLL--NLPEQFLSTGngggviqGTASEavLVVLLAARDR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 209 KFPQYKEKGLSsipgQLVMFTSDQCHYSVKSCASVCGLGTDYCVCVPSDERGR--MIPAQLERLVRYHKDKGNVPFFVNA 286
Cdd:PLN02880  170 VLRKVGKNALE----KLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 287 TSGTTVLGAFDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEG 366
Cdd:PLN02880  246 TVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRH-YIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 367 ILLscNAMSAEYLFMTDKIYDPQ--YDTGDKVIQCGRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPdK 444
Cdd:PLN02880  325 ALI--QSLSTNPEFLKNKASQANsvVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDS-R 401
                         410
                  ....*....|....*...
gi 1931223899 445 FHLILEPEMVNVSFWYLP 462
Cdd:PLN02880  402 FEVVTPRIFSLVCFRLVP 419
 
Name Accession Description Interval E-value
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
91-460 1.67e-158

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 456.49  E-value: 1.67e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  91 PEEMVKILDLELHDEPLPLKQLLEDCKTALKYQVKTGH-PHFFNQLSCGLDIISLAGEWLTAAANTNMFTYEIAPVFILM 169
Cdd:pfam00282   1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 170 ENIVLEKMRSMIGW------KTGDSILAPGGSVSNLYAFLAARHRKFPQYKEKGL----SSIPGQLVMFTSDQCHYSVKS 239
Cdd:pfam00282  81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKpadsSGILAKLVAYTSDQAHSSIEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 240 CASVCGLGtdyCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNATSGTTVLGAFDPLMEIADICQKYDMWMHVDAAW 319
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 320 GGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGILLSCNAMSAEYLFMTDKIydpqYDTGDKVIQC 399
Cdd:pfam00282 238 GGSAFICPEFRH-WLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSA----YDTGHKQIPL 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931223899 400 GRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPDkFHLILEPEMVNVSFWY 460
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGR-FEICAEVGLGLVCFRL 372
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
59-536 1.58e-121

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: 365.31  E-value: 1.58e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  59 QTREFLARVIDVLLDYVQkvndRNEKILEFKMPEEMVKILDLELHDEPLPLKQLLED-CKTALKYQVKTGHPHFFNQLSC 137
Cdd:COG0076     1 EFRALLHQALDLAADYLA----GLDRPVFGPSPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 138 GLDIISLAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMIGW-KTGDSILAPGGSVSNLYAFLAARHRKFPQY-KE 215
Cdd:COG0076    77 GTTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDRALARRvRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 216 KGLSSIPgQLVMFTSDQCHYSVKSCASVCGLGTDYCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNATSGTTVLGA 295
Cdd:COG0076   157 EGLPGAP-RPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 296 FDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGILLSCNAMS 375
Cdd:COG0076   236 IDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRH-LLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 376 AEYLFMTDkiyDPQYDTGDKVIQCGRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPDkFHLILEPEMVN 455
Cdd:COG0076   315 ASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPG-FELLAPPELNI 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 456 VSFWYLPKQLRGIPHDaNKELRLgkvcaklkgKMMQAGTIMVGYQPDDRRPNfFRNIISSAAVTEKDVDFLLSEMDRLGQ 535
Cdd:COG0076   391 VCFRYKPAGLDEEDAL-NYALRD---------RLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAA 459

                  .
gi 1931223899 536 D 536
Cdd:COG0076   460 E 460
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
131-533 8.20e-115

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: 343.80  E-value: 8.20e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 131 FFNQLSCGLDIISLAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMIGW--KTGDSILAPGGSVSNLYAFLAARHR 208
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLpsEDADGVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 209 KFPQYKEKGLSSIPgQLVMFTSDQCHYSV-KSCAsvcgLGTDYCVCVPSDERGRMIPAQLERLVRYHKDKGNVPFFVNAT 287
Cdd:cd06450    81 ARKRLKAGGGRGID-KLVIVCSDQAHVSVeKAAA----YLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 288 SGTTVLGAFDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKyegi 367
Cdd:cd06450   156 AGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRH-LDFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 368 llscnamsaeylfmtdkiydpqydtgdkviqcgrhndIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPdKFHL 447
Cdd:cd06450   231 -------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADP-GFEL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 448 ILEPEMVNVSFWYLPKQlrgiphdankelRLGKVCAKLKGKMMQAGTIMVGYQPDDrRPNFFRNIISSAAVTEKDVDFLL 527
Cdd:cd06450   273 LGEPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLG-GPNVLRFVVTNPLTTRDDADALL 339

                  ....*.
gi 1931223899 528 SEMDRL 533
Cdd:cd06450   340 EDIERA 345
PLN02880 PLN02880
tyrosine decarboxylase
59-462 7.38e-35

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 136.96  E-value: 7.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  59 QTREFLARVIDVLLDYVQKVndRNEKILEFKMPEEMVKILDLELHDEPLPLKQLLEDCKTALKYQVKTGH-PHFFNQLSC 137
Cdd:PLN02880   14 QLRECGHRMVDFIADYYKSI--ENFPVLSQVQPGYLRELLPDSAPNQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 138 GLDIISLAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMIgwKTGDSILAPG-------GSVSN--LYAFLAARHR 208
Cdd:PLN02880   92 NSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLL--NLPEQFLSTGngggviqGTASEavLVVLLAARDR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 209 KFPQYKEKGLSsipgQLVMFTSDQCHYSVKSCASVCGLGTDYCVCVPSDERGR--MIPAQLERLVRYHKDKGNVPFFVNA 286
Cdd:PLN02880  170 VLRKVGKNALE----KLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 287 TSGTTVLGAFDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEG 366
Cdd:PLN02880  246 TVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRH-YIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 367 ILLscNAMSAEYLFMTDKIYDPQ--YDTGDKVIQCGRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPdK 444
Cdd:PLN02880  325 ALI--QSLSTNPEFLKNKASQANsvVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDS-R 401
                         410
                  ....*....|....*...
gi 1931223899 445 FHLILEPEMVNVSFWYLP 462
Cdd:PLN02880  402 FEVVTPRIFSLVCFRLVP 419
PLN02590 PLN02590
probable tyrosine decarboxylase
67-475 3.42e-34

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 135.99  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899  67 VIDVLLDYVQKVNDRNEK--ILEFKMPEEMVKILDLELHDEPLPLKQLLEDCKTALKYQVKTGH-PHFFNQLSCGLDIIS 143
Cdd:PLN02590   66 MVDFIADYYKNLQDSPQDfpVLSQVQPGYLRDMLPDSAPERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 144 LAGEWLTAAANTNMFTYEIAPVFILMENIVLEKMRSMI-------GWKTGDSILAPGGSVSNLYAFLAARHRKFpqyKEK 216
Cdd:PLN02590  146 FLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLqlpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRIL---KKV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 217 GLSSIPgQLVMFTSDQCHYSVKSCASVCGLGTDYCVCVPSDERGR--MIPAQLERLVRYHKDKGNVPFFVNATSGTTVLG 294
Cdd:PLN02590  223 GKTLLP-QLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSA 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 295 AFDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHpRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGILLSCNAM 374
Cdd:PLN02590  302 AVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRK-FIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKT 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 375 SAEYLFMTDKIYDPQYDTGDKVIQCGRHNDIFKLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKEQPdkfHLilepEMV 454
Cdd:PLN02590  381 NPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDP---SF----EVV 453
                         410       420
                  ....*....|....*....|.
gi 1931223899 455 NVSFWYLpKQLRGIPHDANKE 475
Cdd:PLN02590  454 TTRYFSL-VCFRLAPVDGDED 473
PRK02769 PRK02769
histidine decarboxylase; Provisional
193-441 1.59e-15

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 78.16  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 193 GGSVSNLYAFLAARHRkFPQykekglssipgqLVMFTSDQCHYSVKSCASVcgLGTDYCVcVPSDERGRMIPAQLERLVR 272
Cdd:PRK02769   92 GGTEGNLYGCYLAREL-FPD------------GTLYYSKDTHYSVSKIARL--LRIKSRV-ITSLPNGEIDYDDLISKIK 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 273 YHKDKgnvPFFVNATSGTTVLGAFDPLMEIADICQKY---DMWMHVDAAWGGGLLFSKKYRHPrLTGIERADSVTWNPHK 349
Cdd:PRK02769  156 ENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIgidDYYIHADAALSGMILPFVNNPPP-FSFADGIDSIAISGHK 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 350 LMGTLLQCstvhfkyeGILLScnamsaeYLFMTDKIY-DPQY-DTGDKVIQCGR--HNDIFkLWLQWRGKGTSGFERLMD 425
Cdd:PRK02769  232 FIGSPMPC--------GIVLA-------KKKYVERISvDVDYiGSRDQTISGSRngHTALL-LWAAIRSLGSKGLRQRVQ 295
                         250
                  ....*....|....*.
gi 1931223899 426 RLMELSEYMVRRIKEQ 441
Cdd:PRK02769  296 HCLDMAQYAVDRLQAN 311
PLN03032 PLN03032
serine decarboxylase; Provisional
194-440 1.65e-10

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 62.92  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 194 GSVSNLYAFLAARHrKFPQYkekglssipgqlVMFTSDQCHYSVKSCASVCGLGtdyCVCVPSDERGRMIPAQLERLVRY 273
Cdd:PLN03032   94 GTEGNLHGILVGRE-VFPDG------------ILYASRESHYSVFKAARMYRME---AVKVPTLPSGEIDYDDLERALAK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 274 HKDKgnvPFFVNATSGTTVLGAFDPLMEIADICQKYDM-----WMHVDAAWGGgLLFSKKYRHPRLTGIERADSVTWNPH 348
Cdd:PLN03032  158 NRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGALFG-LMMPFVSRAPEVTFRKPIGSVSVSGH 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 349 KLMGTLLQCSTVHFKYEGIllscNAMSA--EYLfmtdkiydpqyDTGDKVIQCGR--HNDIFkLWLQWRGKGTSGFERLM 424
Cdd:PLN03032  234 KFLGCPMPCGVALTRKKHV----KALSQnvEYL-----------NSRDATIMGSRngHAPLY-LWYTLRRKGYRGIKRDV 297
                         250
                  ....*....|....*.
gi 1931223899 425 DRLMELSEYMVRRIKE 440
Cdd:PLN03032  298 QHCMRNAHYLKDRLTE 313
PLN02263 PLN02263
serine decarboxylase
226-440 6.42e-10

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 61.37  E-value: 6.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 226 VMFTSDQCHYSVKSCASVCGLGtdyCVCVPSDERGRMIPAQLERLVRYHKDKgnvPFFVNATSGTTVLGAFDPLMEIADI 305
Cdd:PLN02263  180 ILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDLVIKT 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 306 CQK----YD-MWMHVDAAWGGGLL-FSKkyRHPRLTGIERADSVTWNPHKLMGTLLQCSTVHFKYEGI-LLSCNAmsaEY 378
Cdd:PLN02263  254 LEEcgfsQDrFYIHCDGALFGLMMpFVK--RAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEHInVLSSNV---EY 328
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931223899 379 LfmtdkiydpqyDTGDKVIQCGR--HNDIFkLWLQWRGKGTSGFERLMDRLMELSEYMVRRIKE 440
Cdd:PLN02263  329 L-----------ASRDATIMGSRngHAPIF-LWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
192-352 1.51e-09

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: 57.01  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 192 PGGSVSNLYAFLAARhrkfpqykekglssIPGQLVMFtSDQCHYSV-KSCASVCGLGTdycVCVPSDERGRMI--PAQLE 268
Cdd:cd01494    24 PSGTGANEAALLALL--------------GPGDEVIV-DANGHGSRyWVAAELAGAKP---VPVPVDDAGYGGldVAILE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 269 RLVRYHKdkgnvPFFVNATSGTTVLGAFDPLMEIADICQKYDMWMHVDAAWGGGLLFSKKYRHPRltgiERADSVTWNPH 348
Cdd:cd01494    86 ELKAKPN-----VALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE----GGADVVTFSLH 156

                  ....
gi 1931223899 349 KLMG 352
Cdd:cd01494   157 KNLG 160
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
301-363 1.40e-06

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: 49.94  E-value: 1.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1931223899 301 EIADICQKYDMWMHVDAAWGGGLLFSKKYrhPRLTGIERADSVTWNPHKLMGTLLQCSTVHFK 363
Cdd:cd00615   174 KIVEEAHHRGLPVLVDEAHGAHFRFHPIL--PSSAAMAGADIVVQSTHKTLPALTQGSMIHVK 234
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
301-460 2.53e-05

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 47.03  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 301 EIADICQKYDMWMHVDAAWGGGLLFSKKYRHPRLT-GierADSVTWNPHKLMGTLLQCSTVHFKYEGI----LLSCNAM- 374
Cdd:COG1982   181 AIAELAHEHGIPVLVDEAHGAHFGFHPDLPRSAMEaG---ADLVVQSTHKTLGALTQSSMLHVKGGRVdherVNEALMLl 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931223899 375 ---SAEYLFMT--DkiydpqydtgdkviqCGRHndifklwlQWRGKGtsgfERLMDRLMELSEYMVRRIKEQPDkFHlIL 449
Cdd:COG1982   258 qstSPSYLLMAslD---------------VARR--------QMAGEG----EELLDEALELAIEARKEINKIPG-LY-VF 308
                         170
                  ....*....|.
gi 1931223899 450 EPEMVNVSFWY 460
Cdd:COG1982   309 GPEDLGAPGVY 319
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
254-318 1.70e-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: 40.69  E-value: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931223899 254 VPSDERGRMIPAQLERLVRyHKDKgnvpfFVNATSGTTVLGAFDPLMEIADICQKYDMWMHVDAA 318
Cdd:pfam00266 119 LPLDEDGLLDLDELEKLIT-PKTK-----LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA 177
 
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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