|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
140-586 |
1.57e-134 |
|
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: 399.98 E-value: 1.57e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 140 EPAELRKLFDFELREKGESQEK-LRQLMRETIRYSVKTGHPYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTL 218
Cdd:COG0076 28 SPEELRAALDEPLPEEGLPPEEaLAELEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 219 MEEQVLAEMRRIVGFPDngHGDGIFCPGGSIANGYAISCARYNYAPE-SKKNGLFNAKPLIIFTSEDAHYSVEKLAMFMG 297
Cdd:COG0076 108 LEREVVRWLADLLGLPE--GAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 298 FGSENVRKIATNEVGKMRLSDLEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAAWGGGALM 377
Cdd:COG0076 186 LGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 378 SKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDkfyDTSFDTGDKHIQCGRRADVF 457
Cdd:COG0076 266 SPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 458 KFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVLDhPECTNITFWYVPPSLRHM-EHNQEFYDKLHkvapki 536
Cdd:COG0076 343 KLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAP-PELNIVCFRYKPAGLDEEdALNYALRDRLR------ 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 195031471 537 keamiKKGSMMITYQPLRKLPNfFRLVLQNSCLEESDMLYFINEIESLGQ 586
Cdd:COG0076 416 -----ARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAA 459
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
141-512 |
8.70e-114 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 344.02 E-value: 8.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 141 PAELRKLFDFELREKGESQEKLRQLMRETIRYSVKTGH-PYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTLM 219
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 220 EEQVLAEMRRIVGFP--DNGH-GDGIFCPGGSIANGYAISCARYNYAPESKKNG------LFNAKpLIIFTSEDAHYSVE 290
Cdd:pfam00282 81 ENVVMNWLGEMLGLPaeFLGQeGGGVLQPGSSESNLLALLAARTKWIKRMKAAGkpadssGILAK-LVAYTSDQAHSSIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 291 KLAMFMGFGsenVRKIATNEVGKMRLSDLEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAA 370
Cdd:pfam00282 160 KAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 371 WGGGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDKFYdtsfDTGDKHIQC 450
Cdd:pfam00282 237 YGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195031471 451 GRRADVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVLDhPECTNITFWYV 512
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAE-VGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
181-584 |
1.29e-113 |
|
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: 342.26 E-value: 1.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 181 FINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTLMEEQVLAEMRRIVGFPdNGHGDGIFCPGGSIANGYAISCARY 260
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLP-SEDADGVFTSGGSESNLLALLAARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 261 NYAPESKKNGLFNAKPLIIFTSEDAHYSVEKLAMFMGfgsENVRKIATNEVGKMRLSDLEEQIQLCLDNNWQPLMVSATA 340
Cdd:cd06450 80 RARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 341 GTTVLGAFDDLVGISELCRKHNMWMHVDAAWGGGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRhaqilg 420
Cdd:cd06450 157 GTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 421 qchstnaaylfqkdkfydtsfdtgdkhiqcgrradVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVlD 500
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL-G 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 501 HPECTNITFWYVPPslrhmehnqefyDKLHKVAPKIKEAMIKKGSMMITYQPLRKlPNFFRLVLQNSCLEESDMLYFINE 580
Cdd:cd06450 275 EPNLSLVCFRLKPS------------VKLDELNYDLSDRLNERGGWHVPATTLGG-PNVLRFVVTNPLTTRDDADALLED 341
|
....
gi 195031471 581 IESL 584
Cdd:cd06450 342 IERA 345
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
140-498 |
5.16e-34 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 135.99 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 140 EPAELRKLFDFELREKGES-QEKLRQLMRETIRYSVKTGHPYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTL 218
Cdd:PLN02590 91 QPGYLRDMLPDSAPERPESlKELLDDVSKKIMPGITHWQSPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 219 MEEQVLAEMRRIVGFPDN----GHGDGIFCPGGSIANGYAISCARYNYApesKKNGLFNAKPLIIFTSEDAHYSVEKLAM 294
Cdd:PLN02590 171 LEIIVLDWLAKLLQLPDHflstGNGGGVIQGTGCEAVLVVVLAARDRIL---KKVGKTLLPQLVVYGSDQTHSSFRKACL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 295 FMGFGSENVRKIATNEVGK--MRLSDLEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAAWG 372
Cdd:PLN02590 248 IGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 373 GGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDKFYDTSFDTGDKHIQCGR 452
Cdd:PLN02590 328 GNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSR 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 195031471 453 RADVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELV 498
Cdd:PLN02590 408 RFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV 453
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
140-586 |
1.57e-134 |
|
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: 399.98 E-value: 1.57e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 140 EPAELRKLFDFELREKGESQEK-LRQLMRETIRYSVKTGHPYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTL 218
Cdd:COG0076 28 SPEELRAALDEPLPEEGLPPEEaLAELEDLVLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 219 MEEQVLAEMRRIVGFPDngHGDGIFCPGGSIANGYAISCARYNYAPE-SKKNGLFNAKPLIIFTSEDAHYSVEKLAMFMG 297
Cdd:COG0076 108 LEREVVRWLADLLGLPE--GAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 298 FGSENVRKIATNEVGKMRLSDLEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAAWGGGALM 377
Cdd:COG0076 186 LGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 378 SKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDkfyDTSFDTGDKHIQCGRRADVF 457
Cdd:COG0076 266 SPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 458 KFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVLDhPECTNITFWYVPPSLRHM-EHNQEFYDKLHkvapki 536
Cdd:COG0076 343 KLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAP-PELNIVCFRYKPAGLDEEdALNYALRDRLR------ 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 195031471 537 keamiKKGSMMITYQPLRKLPNfFRLVLQNSCLEESDMLYFINEIESLGQ 586
Cdd:COG0076 416 -----ARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAA 459
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
141-512 |
8.70e-114 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 344.02 E-value: 8.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 141 PAELRKLFDFELREKGESQEKLRQLMRETIRYSVKTGH-PYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTLM 219
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 220 EEQVLAEMRRIVGFP--DNGH-GDGIFCPGGSIANGYAISCARYNYAPESKKNG------LFNAKpLIIFTSEDAHYSVE 290
Cdd:pfam00282 81 ENVVMNWLGEMLGLPaeFLGQeGGGVLQPGSSESNLLALLAARTKWIKRMKAAGkpadssGILAK-LVAYTSDQAHSSIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 291 KLAMFMGFGsenVRKIATNEVGKMRLSDLEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAA 370
Cdd:pfam00282 160 KAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 371 WGGGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDKFYdtsfDTGDKHIQC 450
Cdd:pfam00282 237 YGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195031471 451 GRRADVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVLDhPECTNITFWYV 512
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAE-VGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
181-584 |
1.29e-113 |
|
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: 342.26 E-value: 1.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 181 FINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTLMEEQVLAEMRRIVGFPdNGHGDGIFCPGGSIANGYAISCARY 260
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLP-SEDADGVFTSGGSESNLLALLAARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 261 NYAPESKKNGLFNAKPLIIFTSEDAHYSVEKLAMFMGfgsENVRKIATNEVGKMRLSDLEEQIQLCLDNNWQPLMVSATA 340
Cdd:cd06450 80 RARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 341 GTTVLGAFDDLVGISELCRKHNMWMHVDAAWGGGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRhaqilg 420
Cdd:cd06450 157 GTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 421 qchstnaaylfqkdkfydtsfdtgdkhiqcgrradVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVlD 500
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL-G 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 501 HPECTNITFWYVPPslrhmehnqefyDKLHKVAPKIKEAMIKKGSMMITYQPLRKlPNFFRLVLQNSCLEESDMLYFINE 580
Cdd:cd06450 275 EPNLSLVCFRLKPS------------VKLDELNYDLSDRLNERGGWHVPATTLGG-PNVLRFVVTNPLTTRDDADALLED 341
|
....
gi 195031471 581 IESL 584
Cdd:cd06450 342 IERA 345
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
140-498 |
5.16e-34 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 135.99 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 140 EPAELRKLFDFELREKGES-QEKLRQLMRETIRYSVKTGHPYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTL 218
Cdd:PLN02590 91 QPGYLRDMLPDSAPERPESlKELLDDVSKKIMPGITHWQSPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 219 MEEQVLAEMRRIVGFPDN----GHGDGIFCPGGSIANGYAISCARYNYApesKKNGLFNAKPLIIFTSEDAHYSVEKLAM 294
Cdd:PLN02590 171 LEIIVLDWLAKLLQLPDHflstGNGGGVIQGTGCEAVLVVVLAARDRIL---KKVGKTLLPQLVVYGSDQTHSSFRKACL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 295 FMGFGSENVRKIATNEVGK--MRLSDLEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAAWG 372
Cdd:PLN02590 248 IGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 373 GGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDKFYDTSFDTGDKHIQCGR 452
Cdd:PLN02590 328 GNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSR 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 195031471 453 RADVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELV 498
Cdd:PLN02590 408 RFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV 453
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
140-532 |
5.72e-34 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 135.04 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 140 EPAELRKLFDFELREKGESQEKLRQLMRETIRYSVKTGH-PYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPVFTL 218
Cdd:PLN02880 43 QPGYLRELLPDSAPNQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 219 MEEQVLAEMRRIVGFPDN----GHGDGIFCPGGSIANGYAISCARYNYAPESKKNGLfnaKPLIIFTSEDAHYSVEKLAM 294
Cdd:PLN02880 123 LEMIVLDWLAKLLNLPEQflstGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKNAL---EKLVVYASDQTHSALQKACQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 295 FMGFGSENVRKIATNEVGKMRLSD--LEEQIQLCLDNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAAWG 372
Cdd:PLN02880 200 IAGIHPENCRLLKTDSSTNYALAPelLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 373 GGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTRHAQILGQCHSTNAAYLFQKDKFYDTSFDTGDKHIQCGR 452
Cdd:PLN02880 280 GSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 453 RADVFKFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRERPGFELVLDhPECTNITFWYVPPSLRHMEHNQEFYDKLHKV 532
Cdd:PLN02880 360 RFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTP-RIFSLVCFRLVPPKNNEDNGNKLNHDLLDAV 438
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
246-492 |
7.23e-19 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 88.56 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 246 GGSIANGYAISCARyNYAPESkknglfnakplIIFTSEDAHYSVEKLAMFMGFGSENVRKIATnevGKMRLSDLEEQIQL 325
Cdd:PRK02769 92 GGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKSRVITSLPN---GEIDYDDLISKIKE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 326 cldNNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNM---WMHVDAAWGGGALMSKKYRHLLNGIERADSVTWNPHKLL 402
Cdd:PRK02769 157 ---NKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 403 SASQQCSTFLTRHAQIlgQCHSTNAAYLfqkdkfydtsfDTGDKHIQCGRRAdvFKFWFMWKA---KGSKGFEAHVEQVF 479
Cdd:PRK02769 234 GSPMPCGIVLAKKKYV--ERISVDVDYI-----------GSRDQTISGSRNG--HTALLLWAAirsLGSKGLRQRVQHCL 298
|
250
....*....|...
gi 195031471 480 EMSEFFTAKLRER 492
Cdd:PRK02769 299 DMAQYAVDRLQAN 311
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
278-491 |
5.41e-12 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 68.30 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 278 IIFTSEDAHYSVEKLAMFMGFGSEnvrKIATNEVGKMRLSDLEEQIqlcLDNNWQPLMVSATAGTTVLGAFDDLVGISEL 357
Cdd:PLN02263 180 ILYASRESHYSVFKAARMYRMECV---KVDTLVSGEIDCADFKAKL---LANKDKPAIINVNIGTTVKGAVDDLDLVIKT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 358 CRK----HN-MWMHVDAAWGGgaLMskkyrhlLNGIERADSVTWNP---------HKLLSASQQCSTFLTR--HAQILgq 421
Cdd:PLN02263 254 LEEcgfsQDrFYIHCDGALFG--LM-------MPFVKRAPKVTFKKpigsvsvsgHKFVGCPMPCGVQITRmeHINVL-- 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 422 chSTNAAYLFQKDKfydTSFDTGDKHiqcgrrADVFkFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRE 491
Cdd:PLN02263 323 --SSNVEYLASRDA---TIMGSRNGH------APIF-LWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
278-491 |
7.82e-10 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 61.00 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 278 IIFTSEDAHYSVEKLAMFMGFGSEnvrKIATNEVGKMRLSDLEEQIqlcLDNNWQPLMVSATAGTTVLGAFDDLVGISEL 357
Cdd:PLN03032 113 ILYASRESHYSVFKAARMYRMEAV---KVPTLPSGEIDYDDLERAL---AKNRDKPAILNVNIGTTVKGAVDDLDRILRI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 358 CRK-----HNMWMHVDAAWGGGALMSKKYRHLLNGIERADSVTWNPHKLLSASQQCSTFLTR--HAQILgqchSTNAAYL 430
Cdd:PLN03032 187 LKElgyteDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTRkkHVKAL----SQNVEYL 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195031471 431 FQKDKfydTSFDTGDKHiqcgrrADVFkFWFMWKAKGSKGFEAHVEQVFEMSEFFTAKLRE 491
Cdd:PLN03032 263 NSRDA---TIMGSRNGH------APLY-LWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTE 313
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
236-406 |
1.15e-07 |
|
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: 52.00 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 236 NGHGDGIFCPGGSIANGYAIScarynyapeskknGLFNAKPLIIFtSEDAHYSVEKLAMFMGFGseNVRKIATNEVGKMR 315
Cdd:cd01494 15 PGNDKAVFVPSGTGANEAALL-------------ALLGPGDEVIV-DANGHGSRYWVAAELAGA--KPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 316 LsdleeQIQLCLDNNWQP---LMVsATAGTTVLGAFDDLVGISELCRKHNMWMHVDAAWGGGALMSKKYrhlLNGIERAD 392
Cdd:cd01494 79 L-----DVAILEELKAKPnvaLIV-ITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGAD 149
|
170
....*....|....
gi 195031471 393 SVTWNPHKLLSASQ 406
Cdd:cd01494 150 VVTFSLHKNLGGEG 163
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
242-370 |
2.58e-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: 53.02 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 242 IFCPGGsianGYAISCARYNYAPEskknglFNAKPLIIfTSEDAHYSV----EKLAMFMGFgseNVRKIATNEVGKMRLS 317
Cdd:pfam00266 65 IFTSGT----TEAINLVALSLGRS------LKPGDEIV-ITEMEHHANlvpwQELAKRTGA---RVRVLPLDEDGLLDLD 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 195031471 318 DLEEQIqlcldnNWQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAA 370
Cdd:pfam00266 131 ELEKLI------TPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA 177
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
221-369 |
3.69e-04 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 43.18 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 221 EQVLAEMRRIVGFPDNGHGDGI-FCPGGSIANGYAIscarynyapESKKNGLFNAKPLIIfTSEDAHYSVEKLAMFM--- 296
Cdd:PRK02948 42 SSLLQVCRKTFAEMIGGEEQGIyFTSGGTESNYLAI---------QSLLNALPQNKKHII-TTPMEHASIHSYFQSLesq 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195031471 297 GFgseNVRKIATNEVGKMRLSDLEEQIQLcldnnwQPLMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDA 369
Cdd:PRK02948 112 GY---TVTEIPVDKSGLIRLVDLERAITP------DTVLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDC 175
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
346-432 |
3.94e-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: 39.54 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 346 GAFDDLVGISELCRKHNMWMHVDAAWGGGALMSKKY--RHLLNGierADSVTWNPHKLLSASQQCSTFLTRHAQILGQcH 423
Cdd:cd00615 167 GICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILpsSAAMAG---ADIVVQSTHKTLPALTQGSMIHVKGDLVNPD-R 242
|
....*....
gi 195031471 424 STNAAYLFQ 432
Cdd:cd00615 243 VNEALNLHQ 251
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
346-418 |
4.44e-03 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 39.71 E-value: 4.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195031471 346 GAFDDLVGISELCRKHNMWMHVDAAWGGGALMSKKYRH--LLNGierADSVTWNPHKLLSASQQCSTFLTRHAQI 418
Cdd:COG1982 174 GVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPRsaMEAG---ADLVVQSTHKTLGALTQSSMLHVKGGRV 245
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
241-370 |
4.93e-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: 39.24 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 241 GIFCPGGSIANGYAIS--CARYnyapESkknglfnakpliIFTSEDAH---YSVEKLAMFMGFgsenvrKIAT--NEVGK 313
Cdd:cd06502 50 ALFVPSGTAANQLALAahTQPG----GS------------VICHETAHiytDEAGAPEFLSGV------KLLPvpGENGK 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 195031471 314 MRLSDLEEQIQLCLDNNWQP---LMVSATAGTTVLGAFDDLVGISELCRKHNMWMHVDAA 370
Cdd:cd06502 108 LTPEDLEAAIRPRDDIHFPPpslVSLENTTEGGTVYPLDELKAISALAKENGLPLHLDGA 167
|
|
| |
