|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
205-608 |
3.25e-154 |
|
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: 447.04 E-value: 3.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 205 FFNQLSTGLDIVGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIVGWPDGEGDGIFSPGGAISNMYSVMIARYK 284
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 285 FFPEVKTKGMAAAPRLVLFTSEHSHYSIKKASAALGfgtENLILLNTDERGRVIPADLEAKVIEAKRKGYVPLFVTATAG 364
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 365 TTVYGAFDPINEIADICEKYNMWLHVDGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRergllqg 444
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 445 cnsmcagylfqpdkqydvtydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkG 524
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--G 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 525 EPQHTNVCFWYIPPSlrslpdgeerrqRLHKVAPKIKAMMMESGTTMVGYQPQGDKvNFFRMVISNPAATRSDIDFLVEE 604
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 2062400780 605 IERL 608
Cdd:cd06450 342 IERA 345
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
202-536 |
3.29e-154 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 448.02 E-value: 3.29e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 202 HPRFFNQLSTGLDIVGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIVGWPDG----EGDGIFSPGGAISNMYS 277
Cdd:pfam00282 39 SPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPAEflgqEGGGVLQPGSSESNLLA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 278 VMIARYKFFPEVKTKGMAAAP-----RLVLFTSEHSHYSIKKASAALGFGtenLILLNTDERGRVIPADLEAKVIEAKRK 352
Cdd:pfam00282 119 LLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKEN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 353 GYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHVDGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCS 432
Cdd:pfam00282 196 GLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 433 AILVRERGLLQGCNSMCAGYLFQPDKqydvTYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKI 512
Cdd:pfam00282 276 AVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALI 351
|
330 340
....*....|....*....|....
gi 2062400780 513 KNREGFKMVFkgEPQHTNVCFWYI 536
Cdd:pfam00282 352 RKDGRFEICA--EVGLGLVCFRLK 373
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
157-611 |
1.35e-129 |
|
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: 388.42 E-value: 1.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 157 KKHLVKHLPDNELSKDEVIPEILQQsesvtpirsrgqIASSSIAG-HPRFFNQLSTGLDIVGLAGEWLTSTANTNMFTYE 235
Cdd:COG0076 33 RAALDEPLPEEGLPPEEALAELEDL------------VLPGSVDWnHPRFLAFVTGGTTPAALAADLLASALNQNMGDWD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 236 IAPVFVLMEQLTLKKMREIVGWPDGeGDGIFSPGGAISNMYSVMIARYKFFPE-VKTKGMAAAPRLVLFTSEHSHYSIKK 314
Cdd:COG0076 101 TSPAATELEREVVRWLADLLGLPEG-AGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 315 ASAALGFGTENLILLNTDERGRVIPADLEAKVIEAKRKGYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHVDGAW 394
Cdd:COG0076 180 AARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 395 GGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRERGLLQGCNSMCAGYLFQPDkqyDVTYDTGDKAIQCG 474
Cdd:COG0076 260 GGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 475 RHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkGEPQHTNVCFWYIPPSLrslpdgEERRQRLH 554
Cdd:COG0076 337 RRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKPAGL------DEEDALNY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2062400780 555 KVApkikAMMMESGTTMVGYQPQGDKVNfFRMVISNPAATRSDIDFLVEEIERLGHD 611
Cdd:COG0076 409 ALR----DRLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
159-591 |
9.57e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 144.47 E-value: 9.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 159 HLVKHLPDNELSKDEVIPEILQQ-SESVTPIRSRGQiasssiagHPRFFNQLSTGLDIVGLAGEWLTSTANTNMFTYEIA 237
Cdd:PLN02590 94 YLRDMLPDSAPERPESLKELLDDvSKKIMPGITHWQ--------SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 238 PVFVLMEQLTLKKMREIVGWPD-----GEGDGIFSPGGAISNMYSVMIARYKFFPEVktkGMAAAPRLVLFTSEHSHYSI 312
Cdd:PLN02590 166 PAATELEIIVLDWLAKLLQLPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 313 KKASAALGFGTENLILLNTDERGR--VIPADLEAKVIEAKRKGYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHV 390
Cdd:PLN02590 243 RKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 391 DGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRERGLLQGCNSMCAGYLFQPDKQYDVTYDTGDKA 470
Cdd:PLN02590 323 DAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQ 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 471 IQCGRHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkGEPQHTNVCFWYIPpslrslPDGEErr 550
Cdd:PLN02590 403 ISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRYFSLVCFRLAP------VDGDE-- 472
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2062400780 551 QRLHKVAPKIKAMMMESGTTMVGYQPQGDKVnFFRMVISNP 591
Cdd:PLN02590 473 DQCNERNRELLAAVNSTGKIFISHTALSGKF-VLRFAVGAP 512
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
205-608 |
3.25e-154 |
|
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: 447.04 E-value: 3.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 205 FFNQLSTGLDIVGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIVGWPDGEGDGIFSPGGAISNMYSVMIARYK 284
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 285 FFPEVKTKGMAAAPRLVLFTSEHSHYSIKKASAALGfgtENLILLNTDERGRVIPADLEAKVIEAKRKGYVPLFVTATAG 364
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 365 TTVYGAFDPINEIADICEKYNMWLHVDGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRergllqg 444
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 445 cnsmcagylfqpdkqydvtydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkG 524
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--G 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 525 EPQHTNVCFWYIPPSlrslpdgeerrqRLHKVAPKIKAMMMESGTTMVGYQPQGDKvNFFRMVISNPAATRSDIDFLVEE 604
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 2062400780 605 IERL 608
Cdd:cd06450 342 IERA 345
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
202-536 |
3.29e-154 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 448.02 E-value: 3.29e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 202 HPRFFNQLSTGLDIVGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIVGWPDG----EGDGIFSPGGAISNMYS 277
Cdd:pfam00282 39 SPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPAEflgqEGGGVLQPGSSESNLLA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 278 VMIARYKFFPEVKTKGMAAAP-----RLVLFTSEHSHYSIKKASAALGFGtenLILLNTDERGRVIPADLEAKVIEAKRK 352
Cdd:pfam00282 119 LLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKEN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 353 GYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHVDGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCS 432
Cdd:pfam00282 196 GLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 433 AILVRERGLLQGCNSMCAGYLFQPDKqydvTYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKI 512
Cdd:pfam00282 276 AVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALI 351
|
330 340
....*....|....*....|....
gi 2062400780 513 KNREGFKMVFkgEPQHTNVCFWYI 536
Cdd:pfam00282 352 RKDGRFEICA--EVGLGLVCFRLK 373
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
157-611 |
1.35e-129 |
|
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: 388.42 E-value: 1.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 157 KKHLVKHLPDNELSKDEVIPEILQQsesvtpirsrgqIASSSIAG-HPRFFNQLSTGLDIVGLAGEWLTSTANTNMFTYE 235
Cdd:COG0076 33 RAALDEPLPEEGLPPEEALAELEDL------------VLPGSVDWnHPRFLAFVTGGTTPAALAADLLASALNQNMGDWD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 236 IAPVFVLMEQLTLKKMREIVGWPDGeGDGIFSPGGAISNMYSVMIARYKFFPE-VKTKGMAAAPRLVLFTSEHSHYSIKK 314
Cdd:COG0076 101 TSPAATELEREVVRWLADLLGLPEG-AGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 315 ASAALGFGTENLILLNTDERGRVIPADLEAKVIEAKRKGYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHVDGAW 394
Cdd:COG0076 180 AARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 395 GGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRERGLLQGCNSMCAGYLFQPDkqyDVTYDTGDKAIQCG 474
Cdd:COG0076 260 GGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 475 RHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkGEPQHTNVCFWYIPPSLrslpdgEERRQRLH 554
Cdd:COG0076 337 RRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKPAGL------DEEDALNY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2062400780 555 KVApkikAMMMESGTTMVGYQPQGDKVNfFRMVISNPAATRSDIDFLVEEIERLGHD 611
Cdd:COG0076 409 ALR----DRLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
159-591 |
9.57e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 144.47 E-value: 9.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 159 HLVKHLPDNELSKDEVIPEILQQ-SESVTPIRSRGQiasssiagHPRFFNQLSTGLDIVGLAGEWLTSTANTNMFTYEIA 237
Cdd:PLN02590 94 YLRDMLPDSAPERPESLKELLDDvSKKIMPGITHWQ--------SPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 238 PVFVLMEQLTLKKMREIVGWPD-----GEGDGIFSPGGAISNMYSVMIARYKFFPEVktkGMAAAPRLVLFTSEHSHYSI 312
Cdd:PLN02590 166 PAATELEIIVLDWLAKLLQLPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 313 KKASAALGFGTENLILLNTDERGR--VIPADLEAKVIEAKRKGYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHV 390
Cdd:PLN02590 243 RKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 391 DGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRERGLLQGCNSMCAGYLFQPDKQYDVTYDTGDKA 470
Cdd:PLN02590 323 DAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQ 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 471 IQCGRHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkGEPQHTNVCFWYIPpslrslPDGEErr 550
Cdd:PLN02590 403 ISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRYFSLVCFRLAP------VDGDE-- 472
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2062400780 551 QRLHKVAPKIKAMMMESGTTMVGYQPQGDKVnFFRMVISNP 591
Cdd:PLN02590 473 DQCNERNRELLAAVNSTGKIFISHTALSGKF-VLRFAVGAP 512
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
159-539 |
9.22e-34 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 134.65 E-value: 9.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 159 HLVKHLPDNELSKDEVIPEILQQSES-----VTPIRSRGQIA----SSSIAGhprFFNQ-LSTGLDIVGLAgeWLTSTAN 228
Cdd:PLN02880 46 YLRELLPDSAPNQPETLDQVLDDVQAkilpgVTHWQSPNYFAyypsNSSVAG---FLGEmLSAGLNIVGFS--WITSPAA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 229 TNMftyeiapvfvlmEQLTLKKMREIVGWPD-----GEGDGIFSPGGAISNMYSVMIARYKFfpeVKTKGMAAAPRLVLF 303
Cdd:PLN02880 121 TEL------------EMIVLDWLAKLLNLPEqflstGNGGGVIQGTASEAVLVVLLAARDRV---LRKVGKNALEKLVVY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 304 TSEHSHYSIKKASAALGFGTENLILLNTDERGR--VIPADLEAKVIEAKRKGYVPLFVTATAGTTVYGAFDPINEIADIC 381
Cdd:PLN02880 186 ASDQTHSALQKACQIAGIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 382 EKYNMWLHVDGAWGGGLLMSRKHRHKLNGVERANSVTWNPHKMMGVPLQCSAILVRERGLLQGCNSMCAGYLFQPDKQYD 461
Cdd:PLN02880 266 KSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQAN 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2062400780 462 VTYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFEQHIDKCLDLSAYLYNKIKNREGFKMVfkGEPQHTNVCFWYIPPS 539
Cdd:PLN02880 346 SVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFSLVCFRLVPPK 421
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
264-516 |
1.57e-21 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 97.03 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 264 GIFSPGGAISNMYSVMIARyKFFPEVktkgmaaaprlVLFTSEHSHYSIKKASAALGFGTEnliLLNTDERGRVIPADLE 343
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKSR---VITSLPNGEIDYDDLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 344 AKVIEAKRKGYVplfVTATAGTTVYGAFDPINEIADICEKYNM---WLHVDGAWGGGLLMSRKHRHKLNGVERANSVTWN 420
Cdd:PRK02769 152 SKIKENKNQPPI---IFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAIS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 421 PHKMMGVPLQCSAILVRergllqgcnsmcagylfqpdKQY------DVTY-DTGDKAIQCGR--HVDIfkfwLMWKA--- 488
Cdd:PRK02769 229 GHKFIGSPMPCGIVLAK--------------------KKYverisvDVDYiGSRDQTISGSRngHTAL----LLWAAirs 284
|
250 260
....*....|....*....|....*...
gi 2062400780 489 KGTVGFEQHIDKCLDLSAYLYNKIKNRE 516
Cdd:PRK02769 285 LGSKGLRQRVQHCLDMAQYAVDRLQANG 312
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
264-513 |
2.88e-12 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 68.70 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 264 GIFSPGGAISNMYSVMIARYKFfpevktkgmaaaPRLVLFTSEHSHYSIKKASAALGFGTENLillNTDERGRVIPADLE 343
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKV---PTLPSGEIDYDDLE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 344 AKVIEAKRKgyvPLFVTATAGTTVYGAFDPINEIADICEKYNM-----WLHVDGAWGGGLLMSRKHRHKLNGVERANSVT 418
Cdd:PLN03032 153 RALAKNRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 419 WNPHKMMGVPLQCSAILVRERGLlqgcNSMcagylfqpdkQYDVTY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTVGFE 495
Cdd:PLN03032 230 VSGHKFLGCPMPCGVALTRKKHV----KAL----------SQNVEYlNSRDATIMGSRngHAPLY-LWYTLRRKGYRGIK 294
|
250
....*....|....*...
gi 2062400780 496 QHIDKCLDLSAYLYNKIK 513
Cdd:PLN03032 295 RDVQHCMRNAHYLKDRLT 312
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
257-514 |
1.21e-11 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 67.15 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 257 WPDGEGD--GIFSPGGAISNMYSVMIARYKFfpevktkgmaaaPRLVLFTSEHSHYSIKKASAALGFGTENLillNTDER 334
Cdd:PLN02263 146 WEIEKNEywGYITNCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMECVKV---DTLVS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 335 GRVIPADLEAKVIEAKRKgyvPLFVTATAGTTVYGAFDPINEIADICEKY-----NMWLHVDGAWGGGLLMSRKHRHKLN 409
Cdd:PLN02263 211 GEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDLVIKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 410 GVERANSVTWNPHKMMGVPLQCSAILVRerglLQGCNSMCAgylfqpdkqyDVTY-DTGDKAIQCGR--HVDIFkFWLMW 486
Cdd:PLN02263 288 FKKPIGSVSVSGHKFVGCPMPCGVQITR----MEHINVLSS----------NVEYlASRDATIMGSRngHAPIF-LWYTL 352
|
250 260
....*....|....*....|....*...
gi 2062400780 487 KAKGTVGFEQHIDKCLDLSAYLYNKIKN 514
Cdd:PLN02263 353 NRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
258-437 |
2.79e-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: 56.62 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 258 PDGEGDGIFSPGGAISNMYSVMIARykffpevktkgmaaAPRLVLFTSEHSHYSIKKASAALGFGTENLILLNTDERGRV 337
Cdd:cd01494 14 QPGNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 338 IPADLEakviEAKRKGYVPLFVTaTAGTTVYGAFDPINEIADICEKYNMWLHVDGAWGGGLLMSRKHrhkLNGVERANSV 417
Cdd:cd01494 80 DVAILE----ELKAKPNVALIVI-TPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGADVV 151
|
170 180
....*....|....*....|
gi 2062400780 418 TWNPHKMMGVPlQCSAILVR 437
Cdd:cd01494 152 TFSLHKNLGGE-GGGVVIVK 170
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
339-399 |
1.63e-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: 44.09 E-value: 1.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062400780 339 PADLEaKVIEAKRKGYVPLFVtATAGttVY---GAFDPINEIADICEKYNMWLHVDGAWGGGLL 399
Cdd:cd06454 117 MEDLE-KLLREARRPYGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
304-393 |
1.68e-04 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 44.16 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 304 TSEHSHYSIKKASAALG-FGTENLILLNTDERGRVIPADLEaKVIEAKRKgyvplFVTATAGTTVYGAFDPINEIADICE 382
Cdd:pfam00266 93 ITEMEHHANLVPWQELAkRTGARVRVLPLDEDGLLDLDELE-KLITPKTK-----LVAITHVSNVTGTIQPVPEIGKLAH 166
|
90
....*....|.
gi 2062400780 383 KYNMWLHVDGA 393
Cdd:pfam00266 167 QYGALVLVDAA 177
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
366-438 |
2.26e-04 |
|
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: 43.39 E-value: 2.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2062400780 366 TVYGAFDPINEIADICEKYNMWLHVDGAWGGGLLMS---RKHRHKLNGVERANSVtwnpHKMMGVPLQCSAILVRE 438
Cdd:cd00615 164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKG 235
|
|
| SepSecS |
pfam05889 |
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ... |
311-409 |
6.26e-04 |
|
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes.
Pssm-ID: 399111 Cd Length: 389 Bit Score: 42.58 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062400780 311 SIKKASAAlgfGTENLILLNTDERGRVIPADLEAKVIEAKRKGYVPLFVTATAGTTVYGAFDPINEIADICEKYNMWLHV 390
Cdd:pfam05889 114 SIKAAERA---GFEPRLVETVLDGDYLITDVNDVETIIEEKGEEVILAVLSTTSCFAPRSPDNVKEIAKICAEYDVPHLV 190
|
90
....*....|....*....
gi 2062400780 391 DGAWGgglLMSRKHRHKLN 409
Cdd:pfam05889 191 NGAYG---IQSEEYIRKIA 206
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
331-394 |
3.49e-03 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 40.05 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2062400780 331 TDERGRVIPADLEAkVIEAKRKGYVP---LFVT-ATAGTTVYgAFDPINEIADICEKYNMWLHVDGAW 394
Cdd:COG2008 105 PGEDGKLTPEDLEA-AIRPGDVHFPQpglVSLEnTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
366-396 |
6.67e-03 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 39.32 E-value: 6.67e-03
10 20 30
....*....|....*....|....*....|.
gi 2062400780 366 TVYGAFDPINEIADICEKYNMWLHVDGAWGG 396
Cdd:COG1982 171 TYYGVCYDLKAIAELAHEHGIPVLVDEAHGA 201
|
|
| |
