|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
144-518 |
0e+00 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 530.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 144 PHQLlegMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVF 222
Cdd:pfam00282 1 PGYL---KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPAC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 223 VLMEQITLKKMREIVGWS----SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEQSHYS 293
Cdd:pfam00282 78 TELENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 294 IKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVD 373
Cdd:pfam00282 158 IEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 374 AAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAI 453
Cdd:pfam00282 235 AAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58331246 454 QCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFngEPEHTNVCFWYI 518
Cdd:pfam00282 311 PLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
187-590 |
1.16e-159 |
|
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: 460.13 E-value: 1.16e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 187 FFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSSKDGDGIFSPGGAISNMYSIMAARYK 266
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 267 YFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAG 346
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 347 TTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKekgilqg 426
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 427 cnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEmvFNG 506
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFE--LLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 507 EPEHTNVCFWYIPQSlrgvpdspqrreKLHKVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAATQSDIDFLIEE 586
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 58331246 587 IERL 590
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
152-593 |
1.62e-131 |
|
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: 392.66 E-value: 1.62e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 152 EGFNLELSDHPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITL 230
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 231 KKMREIVGWSsKDGDGIFSPGGAISNMYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVI 309
Cdd:COG0076 114 RWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 310 LIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHK 389
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 390 LNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWK 469
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 470 AKGTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIPQSLRGVPDSPQRreklhkvapkIKALMMES 549
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKPAGLDEEDALNYA----------LRDRLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 58331246 550 GTTMVGYQPQGDKANfFRMVISNPAATQSDIDFLIEEIERLGQD 593
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
160-519 |
2.26e-38 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 148.71 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 160 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVG 238
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 239 W-----SSKDGDGIFSPGGAISNMYSIMAARYKYFPEVktkGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKC 313
Cdd:PLN02590 185 LpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 314 NERGK--IIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLN 391
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 392 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 471
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58331246 472 GTVGFENQINKCLELAEYLYAKIKNREEFEMVFNgePEHTNVCFWYIP 519
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTT--RYFSLVCFRLAP 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
144-518 |
0e+00 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 530.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 144 PHQLlegMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVF 222
Cdd:pfam00282 1 PGYL---KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPAC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 223 VLMEQITLKKMREIVGWS----SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEQSHYS 293
Cdd:pfam00282 78 TELENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 294 IKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVD 373
Cdd:pfam00282 158 IEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 374 AAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAI 453
Cdd:pfam00282 235 AAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58331246 454 QCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFngEPEHTNVCFWYI 518
Cdd:pfam00282 311 PLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
187-590 |
1.16e-159 |
|
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: 460.13 E-value: 1.16e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 187 FFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSSKDGDGIFSPGGAISNMYSIMAARYK 266
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 267 YFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAG 346
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 347 TTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKekgilqg 426
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 427 cnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEmvFNG 506
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFE--LLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 507 EPEHTNVCFWYIPQSlrgvpdspqrreKLHKVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAATQSDIDFLIEE 586
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 58331246 587 IERL 590
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
152-593 |
1.62e-131 |
|
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: 392.66 E-value: 1.62e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 152 EGFNLELSDHPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITL 230
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 231 KKMREIVGWSsKDGDGIFSPGGAISNMYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVI 309
Cdd:COG0076 114 RWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 310 LIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHK 389
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 390 LNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWK 469
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 470 AKGTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIPQSLRGVPDSPQRreklhkvapkIKALMMES 549
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKPAGLDEEDALNYA----------LRDRLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 58331246 550 GTTMVGYQPQGDKANfFRMVISNPAATQSDIDFLIEEIERLGQD 593
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
160-519 |
2.26e-38 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 148.71 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 160 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVG 238
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 239 W-----SSKDGDGIFSPGGAISNMYSIMAARYKYFPEVktkGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKC 313
Cdd:PLN02590 185 LpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 314 NERGK--IIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLN 391
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 392 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 471
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58331246 472 GTVGFENQINKCLELAEYLYAKIKNREEFEMVFNgePEHTNVCFWYIP 519
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTT--RYFSLVCFRLAP 467
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
160-519 |
5.83e-38 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 146.59 E-value: 5.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 160 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVG 238
Cdd:PLN02880 57 NQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 239 -----WSSKDGDGIFSPGGAISNMYSIMAARYKYfpeVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIK- 312
Cdd:PLN02880 137 lpeqfLSTGNGGGVIQGTASEAVLVVLLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKt 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 313 -CNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLN 391
Cdd:PLN02880 214 dSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYID 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 392 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 471
Cdd:PLN02880 294 GVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLY 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58331246 472 GTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIP 519
Cdd:PLN02880 374 GVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFSLVCFRLVP 419
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
246-498 |
3.19e-24 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 104.74 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 246 GIFSPGGAISNMYSIMAARyKYFPEVktkgmaavpklVLFTSEQSHYSIKKAGAALGFgTDNVILIKCNerGKIIPADFE 325
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRI-KSRVITSLPN--GEIDYDDLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 326 AKILEAKQKGYVpfyVNATAGTTVYGAFDPIQEIADICEKYNL---WLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWN 402
Cdd:PRK02769 152 SKIKENKNQPPI---IFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAIS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 403 PHKMMGVLLQCSAILVKEKGIlqgcnqmcagylfqpDKQY-DVSY-DTGDKAIQCGR--HVDIfkfwLMWKA---KGTVG 475
Cdd:PRK02769 229 GHKFIGSPMPCGIVLAKKKYV---------------ERISvDVDYiGSRDQTISGSRngHTAL----LLWAAirsLGSKG 289
|
250 260
....*....|....*....|...
gi 58331246 476 FENQINKCLELAEYLYAKIKNRE 498
Cdd:PRK02769 290 LRQRVQHCLDMAQYAVDRLQANG 312
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
280-496 |
1.97e-12 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 69.46 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 280 PKLVLFTSEQSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADFEAKILEAKQKgyvPFYVNATAGTTVYGAFDPIQEI 359
Cdd:PLN02263 177 PDGILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDLV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 360 ADICEKY-----NLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGIlqgcNQMCAgy 434
Cdd:PLN02263 251 IKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEHI----NVLSS-- 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58331246 435 lfqpdkqyDVSY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTVGFENQINKCLELAEYLYAKIKN 496
Cdd:PLN02263 325 --------NVEYlASRDATIMGSRngHAPIF-LWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
246-495 |
6.71e-12 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 67.54 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 246 GIFSPGGAISNMYSIMAARYKYfpevktkgmaavPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIkcnERGKIIPADFE 325
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 326 AKILEAKQKgyvPFYVNATAGTTVYGAFDPIQEIADICEKYN-----LWLHVDAAWGGGLLMSRKHRHKLNGIERANSVT 400
Cdd:PLN03032 153 RALAKNRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 401 WNPHKMMGVLLQCSAILVKEKGILQgcnqmcagylFQPDKQYDVSYDTGDKAIQCGrHVDIFkFWLMWKAKGTVGFENQI 480
Cdd:PLN03032 230 VSGHKFLGCPMPCGVALTRKKHVKA----------LSQNVEYLNSRDATIMGSRNG-HAPLY-LWYTLRRKGYRGIKRDV 297
|
250
....*....|....*
gi 58331246 481 NKCLELAEYLYAKIK 495
Cdd:PLN03032 298 QHCMRNAHYLKDRLT 312
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
242-419 |
9.87e-10 |
|
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: 57.78 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 242 KDGDGIFSPGGAISNMYSIMAARykyfpevktkgmaaVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIip 321
Cdd:cd01494 16 GNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 322 adfEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHrhkLNGIERANSVTW 401
Cdd:cd01494 80 ---DVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGADVVTF 153
|
170
....*....|....*...
gi 58331246 402 NPHKMMGVlLQCSAILVK 419
Cdd:cd01494 154 SLHKNLGG-EGGGVVIVK 170
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
348-420 |
2.29e-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: 49.55 E-value: 2.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58331246 348 TVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMS---RKHRHKLNGIERANSVtwnpHKMMGVLLQCSAILVKE 420
Cdd:cd00615 164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKG 235
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
224-514 |
5.05e-06 |
|
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: 48.78 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 224 LMEQiTLKKMREIVGWSSKDgDGIFSPGGAisnmYSIMAARYKYFPEVKTKGMAAVpklvlftSEQSHYSIKKAGAALG- 302
Cdd:pfam00266 44 AYEE-AREKVAEFINAPSND-EIIFTSGTT----EAINLVALSLGRSLKPGDEIVI-------TEMEHHANLVPWQELAk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 303 FGTDNVILIKCNERGKIIPADFEAKILEaKQKgyvpfYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGllm 382
Cdd:pfam00266 111 RTGARVRVLPLDEDGLLDLDELEKLITP-KTK-----LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 383 srkHRH----KLNgierANSVTWNPHKMM-----GVLLQCSAILVKEKGILQGcnqmcAGYLFQPDKQYDVSYDTGDK-- 451
Cdd:pfam00266 182 ---HRPidvqKLG----VDFLAFSGHKLYgptgiGVLYGRRDLLEKMPPLLGG-----GGMIETVSLQESTFADAPWKfe 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58331246 452 --------AIQCGRHVDifkfWLMwkakgTVGFENQINKCLELAEYLYAKIKNREEFEmvFNGEPEHTNVC 514
Cdd:pfam00266 250 agtpniagIIGLGAALE----YLS-----EIGLEAIEKHEHELAQYLYERLLSLPGIR--LYGPERRASII 309
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
234-375 |
6.03e-04 |
|
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: 42.32 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 234 REIVGwsskDGDGIFSPGGAISNMYSIMAarykyfpevktkgMAAVPKLVLfTSEQSHYSIKKAGAALGFGTDNVILIKc 313
Cdd:cd06502 42 AELFG----KEAALFVPSGTAANQLALAA-------------HTQPGGSVI-CHETAHIYTDEAGAPEFLSGVKLLPVP- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331246 314 NERGKIIPADFEAKILEAKQKGYVPFYV----NATAGTTVYgafdPIQEIADICE---KYNLWLHVDAA 375
Cdd:cd06502 103 GENGKLTPEDLEAAIRPRDDIHFPPPSLvsleNTTEGGTVY----PLDELKAISAlakENGLPLHLDGA 167
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
348-423 |
1.30e-03 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 41.64 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 348 TVYGAFDPIQEIADICEKYNLWLHVDAAWGG---------------GLLMSrkhrhklngierANSVtwnpHKMMGVLLQ 412
Cdd:COG1982 171 TYYGVCYDLKAIAELAHEHGIPVLVDEAHGAhfgfhpdlprsameaGADLV------------VQST----HKTLGALTQ 234
|
90
....*....|.
gi 58331246 413 CSAILVKEKGI 423
Cdd:COG1982 235 SSMLHVKGGRV 245
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
232-375 |
3.32e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 39.89 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 232 KMREIVGwssKDGdGIFSPGGAISNMYSIMAArykyfpevktkgmaAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILI 311
Cdd:pfam01212 40 RVAELFG---KEA-ALFVPSGTAANQLALMAH--------------CQRGDEVICGEPAHIHFDETGGHAELGGVQPRPL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331246 312 KCNERGKIIPADFEAKILEAKQKGYVPFYV------NATAGTTVYgAFDPIQEIADICEKYNLWLHVDAA 375
Cdd:pfam01212 102 DGDEAGNMDLEDLEAAIREVGADIFPPTGLislentHNSAGGQVV-SLENLREIAALAREHGIPVHLDGA 170
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
321-381 |
7.87e-03 |
|
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: 38.70 E-value: 7.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58331246 321 PADFEAKILEAKQKgYVPFYVnATAGttVY---GAFDPIQEIADICEKYNLWLHVDAAWGGGLL 381
Cdd:cd06454 117 MEDLEKLLREARRP-YGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| |
