|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
56-501 |
1.04e-144 |
|
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: 423.09 E-value: 1.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 56 QPPEQLRQLLDLEMRDTGESQDKLLK-LCQDVIHFSVKTNHPRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFL 134
Cdd:COG0076 27 PSPEELRAALDEPLPEEGLPPEEALAeLEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAAT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 135 LVEEAVLKKMIECVGWKEG-DGIFNPGGSVSNMCAMNLARYRHCP-DIKEKGLSGLPRLILFTSAECHYSMKKAASFLGI 212
Cdd:COG0076 107 ELEREVVRWLADLLGLPEGaGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 213 GTQNVYFVETDGRGKMIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASWGGSALVS 292
Cdd:COG0076 187 GRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 293 RKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKsDLLKKCYSAKATYLFQQDkfyDVSYDTGDKSIQCSRRPDAF 372
Cdd:COG0076 267 PELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDP-ELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 373 KFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYIPPSLREMEEGPEFWRklslvapaikE 452
Cdd:COG0076 343 KLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGLDEEDALNYALR----------D 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 197382957 453 KMMKKGSLMLGYQPHRGKVNfFRQVVISPQVSREDMDFLLDEIDSLGRD 501
Cdd:COG0076 413 RLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
98-498 |
1.05e-123 |
|
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: 364.99 E-value: 1.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 98 FFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFLLVEEAVLKKMIECVGW--KEGDGIFNPGGSVSNMCAMNLARYR 175
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLpsEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 176 HCPDIKEKGLSGLPRLILFTSAECHYSMKKAASFLGIgtqNVYFVETDGRGKMIPEDLEKQIWQARQEGAVPFLVCATSG 255
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 256 TTVLGAFDPLDEIAEVCERHGLWLHVDASWGGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKdksdllk 335
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 336 kcysakatylfqqdkfydvsydtgdksiqcsrrpdAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLME 415
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 416 PEYTNVCFWYIPPSlremeegpefwrKLSLVAPAIKEKMMKKGSLMLGYQPHRGKvNFFRQVVISPQVSREDMDFLLDEI 495
Cdd:cd06450 276 PNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDI 342
|
...
gi 197382957 496 DSL 498
Cdd:cd06450 343 ERA 345
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
58-426 |
8.95e-120 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 356.34 E-value: 8.95e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 58 PEQLRQLLDLEMRDTGESQDKLLKLCQDVIHFSVKTNH-PRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFLLV 136
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 137 EEAVLKKMIECVGW------KEGDGIFNPGGSVSNMCAMNLARYRHCPDIKEKG-----LSGLPRLILFTSAECHYSMKK 205
Cdd:pfam00282 81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGkpadsSGILAKLVAYTSDQAHSSIEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 206 AASFLGIGtqnVYFVETDGRGKMIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASW 285
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 286 GGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSDlLKKCYSAKATYLFQQDKfydvSYDTGDKSIQC 365
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEA-LQQAFQFNPLYLGHTDS----AYDTGHKQIPL 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197382957 366 SRRPDAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYI 426
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
58-427 |
4.13e-42 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 157.56 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 58 PEQLRQLLDLEMRDTGESQDKLL-----KLCQDVIHFsvktNHPRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPV 132
Cdd:PLN02590 92 PGYLRDMLPDSAPERPESLKELLddvskKIMPGITHW----QSPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 133 FLLVEEAVLKKMIECVGWKE-------GDGIFNPGGSVSNMCAMNLARYRhcpDIKEKGLSGLPRLILFTSAECHYSMKK 205
Cdd:PLN02590 168 ATELEIIVLDWLAKLLQLPDhflstgnGGGVIQGTGCEAVLVVVLAARDR---ILKKVGKTLLPQLVVYGSDQTHSSFRK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 206 AASFLGIGTQNVYFVETDGRGK--MIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDA 283
Cdd:PLN02590 245 ACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 284 SWGGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSDLLKKCYSAKATYLFQQDKfYDVSYDTGDKSI 363
Cdd:PLN02590 325 AYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQI 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197382957 364 QCSRRPDAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYIP 427
Cdd:PLN02590 404 SLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
56-501 |
1.04e-144 |
|
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: 423.09 E-value: 1.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 56 QPPEQLRQLLDLEMRDTGESQDKLLK-LCQDVIHFSVKTNHPRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFL 134
Cdd:COG0076 27 PSPEELRAALDEPLPEEGLPPEEALAeLEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAAT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 135 LVEEAVLKKMIECVGWKEG-DGIFNPGGSVSNMCAMNLARYRHCP-DIKEKGLSGLPRLILFTSAECHYSMKKAASFLGI 212
Cdd:COG0076 107 ELEREVVRWLADLLGLPEGaGGVFTSGGTEANLLALLAARDRALArRVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 213 GTQNVYFVETDGRGKMIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASWGGSALVS 292
Cdd:COG0076 187 GRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 293 RKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKsDLLKKCYSAKATYLFQQDkfyDVSYDTGDKSIQCSRRPDAF 372
Cdd:COG0076 267 PELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDP-ELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 373 KFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYIPPSLREMEEGPEFWRklslvapaikE 452
Cdd:COG0076 343 KLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGLDEEDALNYALR----------D 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 197382957 453 KMMKKGSLMLGYQPHRGKVNfFRQVVISPQVSREDMDFLLDEIDSLGRD 501
Cdd:COG0076 413 RLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
98-498 |
1.05e-123 |
|
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: 364.99 E-value: 1.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 98 FFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFLLVEEAVLKKMIECVGW--KEGDGIFNPGGSVSNMCAMNLARYR 175
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLpsEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 176 HCPDIKEKGLSGLPRLILFTSAECHYSMKKAASFLGIgtqNVYFVETDGRGKMIPEDLEKQIWQARQEGAVPFLVCATSG 255
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 256 TTVLGAFDPLDEIAEVCERHGLWLHVDASWGGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKdksdllk 335
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 336 kcysakatylfqqdkfydvsydtgdksiqcsrrpdAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLME 415
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 416 PEYTNVCFWYIPPSlremeegpefwrKLSLVAPAIKEKMMKKGSLMLGYQPHRGKvNFFRQVVISPQVSREDMDFLLDEI 495
Cdd:cd06450 276 PNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDI 342
|
...
gi 197382957 496 DSL 498
Cdd:cd06450 343 ERA 345
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
58-426 |
8.95e-120 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 356.34 E-value: 8.95e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 58 PEQLRQLLDLEMRDTGESQDKLLKLCQDVIHFSVKTNH-PRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFLLV 136
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 137 EEAVLKKMIECVGW------KEGDGIFNPGGSVSNMCAMNLARYRHCPDIKEKG-----LSGLPRLILFTSAECHYSMKK 205
Cdd:pfam00282 81 ENVVMNWLGEMLGLpaeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGkpadsSGILAKLVAYTSDQAHSSIEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 206 AASFLGIGtqnVYFVETDGRGKMIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASW 285
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 286 GGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSDlLKKCYSAKATYLFQQDKfydvSYDTGDKSIQC 365
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEA-LQQAFQFNPLYLGHTDS----AYDTGHKQIPL 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197382957 366 SRRPDAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYI 426
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
58-427 |
4.13e-42 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 157.56 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 58 PEQLRQLLDLEMRDTGESQDKLL-----KLCQDVIHFsvktNHPRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPV 132
Cdd:PLN02590 92 PGYLRDMLPDSAPERPESLKELLddvskKIMPGITHW----QSPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 133 FLLVEEAVLKKMIECVGWKE-------GDGIFNPGGSVSNMCAMNLARYRhcpDIKEKGLSGLPRLILFTSAECHYSMKK 205
Cdd:PLN02590 168 ATELEIIVLDWLAKLLQLPDhflstgnGGGVIQGTGCEAVLVVVLAARDR---ILKKVGKTLLPQLVVYGSDQTHSSFRK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 206 AASFLGIGTQNVYFVETDGRGK--MIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDA 283
Cdd:PLN02590 245 ACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 284 SWGGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSDLLKKCYSAKATYLFQQDKfYDVSYDTGDKSI 363
Cdd:PLN02590 325 AYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQI 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197382957 364 QCSRRPDAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYIP 427
Cdd:PLN02590 404 SLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP 467
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
58-429 |
9.11e-38 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 144.67 E-value: 9.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 58 PEQLRQLLDlemrdtgesqDKLLKLCQDVIHFsvktNHPRFFNQLYAGLDYYSLAARIITEALNPSIYTYEVSPVFLLVE 137
Cdd:PLN02880 59 PETLDQVLD----------DVQAKILPGVTHW----QSPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 138 EAVLK---KMI----ECVGWKEGDGIFNPGGSVSNMCAMNLARYRhcpDIKEKGLSGLPRLILFTSAECHYSMKKAASFL 210
Cdd:PLN02880 125 MIVLDwlaKLLnlpeQFLSTGNGGGVIQGTASEAVLVVLLAARDR---VLRKVGKNALEKLVVYASDQTHSALQKACQIA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 211 GIGTQNVYFVETDGRGK--MIPEDLEKQIWQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASWGGS 288
Cdd:PLN02880 202 GIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 289 ALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSDLLKKcYSAKATYLFQQDKFYDVSYDTGDKSIQCSRR 368
Cdd:PLN02880 282 ACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQS-LSTNPEFLKNKASQANSVVDYKDWQIPLGRR 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197382957 369 PDAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPEYTNVCFWYIPPS 429
Cdd:PLN02880 361 FRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRIFSLVCFRLVPPK 421
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
137-495 |
2.56e-20 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 92.80 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 137 EEAVLKKMIE--CVGWKEGDGIFNPGGSVSNMCAMNLARYRHcpdikekglsglPRLILFTSAECHYSMKKAASFLGIGT 214
Cdd:PRK02769 67 ERDVMNFFAElfKIPFNESWGYITNGGTEGNLYGCYLARELF------------PDGTLYYSKDTHYSVSKIARLLRIKS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 215 QnvyFVETDGRGKMIPEDLEKQIWQARQEgavPFLVCATSGTTVLGAFDPLDEIAEVCERHGL---WLHVDASWGGSALV 291
Cdd:PRK02769 135 R---VITSLPNGEIDYDDLISKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 292 SRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSdllkkcysakatylfqQDKFY-DVSY-DTGDKSIQCSRRP 369
Cdd:PRK02769 209 FVNNPPPFSFADGIDSIAISGHKFIGSPMPCGIVLAKKKY----------------VERISvDVDYiGSRDQTISGSRNG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 370 -DAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKRegfkllmepeytNVCFWYIPPSlremeegpefwrkLSLVAP 448
Cdd:PRK02769 273 hTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRLQAN------------GIPAWRNPNS-------------ITVVFP 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 197382957 449 AIKEKMMKKGSL-MLGYQPHrgkvnffrqVVISPQVSREDMDFLLDEI 495
Cdd:PRK02769 328 CPSERIWKKWHLaTSGNQAH---------IITMPHHNKQQIDSLIDEL 366
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
141-328 |
1.60e-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: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 141 LKKMIECV----GWKEGDGIFNPGGSVSN-MCAMNLARYRhcpdikekglsglpRLILFtSAECHYSmkKAASFLGIGTQ 215
Cdd:cd01494 2 LEELEEKLarllQPGNDKAVFVPSGTGANeAALLALLGPG--------------DEVIV-DANGHGS--RYWVAAELAGA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 216 NVYFVETDGRGKMI--PEDLEKQIWQARqegavPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASWGGSALVSR 293
Cdd:cd01494 65 KPVPVPVDDAGYGGldVAILEELKAKPN-----VALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAP 139
|
170 180 190
....*....|....*....|....*....|....*
gi 197382957 294 KHRRllhGIHRADSVAWNPHKmLMAGIQCSALLVK 328
Cdd:cd01494 140 GVLI---PEGGADVVTFSLHK-NLGGEGGGVVIVK 170
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
188-405 |
1.25e-08 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 56.76 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 188 LPRLILFTSAECHYSMKKAASFLGIGTQNvyfVETDGRGKMIPEDLEKQIWQARQEgavPFLVCATSGTTVLGAFDPLDE 267
Cdd:PLN03032 109 FPDGILYASRESHYSVFKAARMYRMEAVK---VPTLPSGEIDYDDLERALAKNRDK---PAILNVNIGTTVKGAVDDLDR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 268 IAEVCERHG-----LWLHVDASWGGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSdllKKCYSAKA 342
Cdd:PLN03032 183 ILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTRKKH---VKALSQNV 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197382957 343 TYLfqqdkfydvsyDTGDKSIQCSRRPDAFKF-WMTWKALGTSGLEERVNRAFALSRYLVDEIK 405
Cdd:PLN03032 260 EYL-----------NSRDATIMGSRNGHAPLYlWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
156-336 |
3.94e-07 |
|
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: 52.25 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 156 IFNPGGSVS-NMCAMNLARYrhcpdIKEKglsglpRLILFTSAEcHYSMKKAASFLGI-GTQNVYFVETDGRGKMIPEDL 233
Cdd:pfam00266 65 IFTSGTTEAiNLVALSLGRS-----LKPG------DEIVITEME-HHANLVPWQELAKrTGARVRVLPLDEDGLLDLDEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 234 EKQIwqarQEGAVpfLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASwggSALVSRKH--RRLlhGIhraDSVAWN 311
Cdd:pfam00266 133 EKLI----TPKTK--LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA---QAIGHRPIdvQKL--GV---DFLAFS 198
|
170 180
....*....|....*....|....*.
gi 197382957 312 PHKML-MAGIqcSALLVKDksDLLKK 336
Cdd:pfam00266 199 GHKLYgPTGI--GVLYGRR--DLLEK 220
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
222-292 |
1.38e-06 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 50.07 E-value: 1.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197382957 222 TDGRGKMIPEDLEKQIWQARQEGAVPFLVC---ATSGTTVLgAFDPLDEIAEVCERHGLWLHVDASWGGSALVS 292
Cdd:COG2008 105 PGEDGKLTPEDLEAAIRPGDVHFPQPGLVSlenTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGARLFNAAAA 177
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
188-495 |
3.63e-06 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 49.43 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 188 LPRLILFTSAECHYSMKKAASFLGIGTQNvyfVETDGRGKMIPEDLEKQIWQARQEgavPFLVCATSGTTVLGAFDPLDE 267
Cdd:PLN02263 176 FPDGILYASRESHYSVFKAARMYRMECVK---VDTLVSGEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 268 IAEVCERHG-----LWLHVDASWGGSALVSRKHRRLLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSdllKKCYSAKA 342
Cdd:PLN02263 250 VIKTLEECGfsqdrFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEH---INVLSSNV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 343 TYLFQQdkfydvsydtgDKSIQCSRRPDAFKF-WMTWKALGTSGLEERVNRAFALSRYLVDEIKKrEGFKLLMEPEYTNV 421
Cdd:PLN02263 327 EYLASR-----------DATIMGSRNGHAPIFlWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE-AGISAMLNELSSTV 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197382957 422 CFwyippsLREMEEgpEFWRKLSLVApaikekmmkkgslmlgyqphRGKVnffRQVVISPQVSREDMDFLLDEI 495
Cdd:PLN02263 395 VF------ERPKDE--EFVRRWQLAC--------------------QGNI---AHVVVMPSVTIEKLDYFLKEL 437
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
186-316 |
2.66e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 43.20 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 186 SGLPRL-----ILFTSAEcHYSM----KKAASFLGIgtqNVYFVETDGRGKMIPEDLEKQIwQARqegavPFLVCATSGT 256
Cdd:COG0520 95 YGLGRLkpgdeILITEME-HHSNivpwQELAERTGA---EVRVIPLDEDGELDLEALEALL-TPR-----TKLVAVTHVS 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 197382957 257 TVLGAFDPLDEIAEVCERHGLWLHVDA--SWGgsalvsrkHRRL-LHGIHrADSVAWNPHKML 316
Cdd:COG0520 165 NVTGTVNPVKEIAALAHAHGALVLVDGaqSVP--------HLPVdVQALG-CDFYAFSGHKLY 218
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
230-284 |
4.68e-04 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 42.55 E-value: 4.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 197382957 230 PEDLEKQIWQARqEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDAS 284
Cdd:cd06454 117 MEDLEKLLREAR-RPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEA 170
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
265-329 |
1.32e-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: 40.69 E-value: 1.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197382957 265 LDEIAEVCERHGLWLHVDASWGGSALVSRKHRR--LLHGihrADSVAWNPHKMLMAGIQCSALLVKD 329
Cdd:cd00615 172 LRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSsaAMAG---ADIVVQSTHKTLPALTQGSMIHVKG 235
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
224-292 |
3.10e-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: 39.62 E-value: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197382957 224 GRGKMIPEDLEKQIwqaRQEGAV----PFLVCATSgTTVLGAFDPLDE---IAEVCERHGLWLHVDASWGGSALVS 292
Cdd:cd06502 104 ENGKLTPEDLEAAI---RPRDDIhfppPSLVSLEN-TTEGGTVYPLDElkaISALAKENGLPLHLDGARLANAAAA 175
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
156-283 |
3.46e-03 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 39.65 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382957 156 IFNPGGSVSNmcamNLAryrhcpdIK---EKGLSGLPRLIlfTSA-EcHYSMKKAASFL---GIgtqNVYFVETDGRGKM 228
Cdd:COG1104 66 IFTSGGTEAN----NLA-------IKgaaRAYRKKGKHII--TSAiE-HPAVLETARFLekeGF---EVTYLPVDEDGRV 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 197382957 229 IPEDLEKQIwqarQEGAVpfLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDA 283
Cdd:COG1104 129 DLEALEAAL----RPDTA--LVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDA 177
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
220-283 |
4.15e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 39.12 E-value: 4.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 197382957 220 VETDGRGKMIPEDLEKQIwqaRQEGAVPF----LVCAT-----SGTTVLgAFDPLDEIAEVCERHGLWLHVDA 283
Cdd:pfam01212 101 LDGDEAGNMDLEDLEAAI---REVGADIFpptgLISLEnthnsAGGQVV-SLENLREIAALAREHGIPVHLDG 169
|
|
| |
