|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
2-394 |
1.03e-143 |
|
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: 411.98 E-value: 1.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 2 VGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWPGGCGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMA 81
Cdd:cd06450 12 PALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDRARKRLKAGGGR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 82 AIPRLVALTSEHSHFSVKKGAAALGIgtdSVILIRCDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGTTVYGAFDPLL 161
Cdd:cd06450 92 GIDKLVIVCSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 162 AIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVReeglmqscnqmhasylfq 241
Cdd:cd06450 169 EIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 242 qdkhydlsydtgdkalqcgrhvdVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFWY 321
Cdd:cd06450 231 -----------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--GEPNLSLVCFRL 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2263230305 322 VPPSlrsmedneermnRLLKVAPVIKARMMEYGTTMVSYQPLGDKvNFFRMVISNPAATHQDIDFLIEEIERL 394
Cdd:cd06450 286 KPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDIERA 345
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
1-322 |
2.70e-142 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 409.50 E-value: 2.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 1 MVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWP----GGCGDGIFSPGGAISNMYAMLIARFKMFPEVK 76
Cdd:pfam00282 52 YPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 77 EKGMAAIP-----RLVALTSEHSHFSVKKGAAALGIGtdsVILIRCDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGT 151
Cdd:pfam00282 132 AAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 152 TVYGAFDPLLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSC 231
Cdd:pfam00282 209 TGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 232 NQMHASYLFqqdkHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVFdgK 311
Cdd:pfam00282 289 FQFNPLYLG----HTDSAYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--E 362
|
330
....*....|.
gi 2263230305 312 PQHTNVCFWYV 322
Cdd:pfam00282 363 VGLGLVCFRLK 373
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
1-397 |
1.27e-137 |
|
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: 400.75 E-value: 1.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 1 MVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWPGGCgDGIFSPGGAISNMYAMLIARFKMFPE-VKEKG 79
Cdd:COG0076 80 PAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGA-GGVFTSGGTEANLLALLAARDRALARrVRAEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 80 MAAIPRLVALTSEHSHFSVKKGAAALGIGTDSVILIRCDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGTTVYGAFDP 159
Cdd:COG0076 159 LPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 160 LLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYL 239
Cdd:COG0076 239 LAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 240 FQQDkhyDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCF 319
Cdd:COG0076 319 GPAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCF 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2263230305 320 WYVPPSLRSM-EDNEErmnrllkvapvIKARMMEYGTTMVSYQPLGDKVNfFRMVISNPAATHQDIDFLIEEIERLGQD 397
Cdd:COG0076 394 RYKPAGLDEEdALNYA-----------LRDRLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
1-384 |
4.06e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 141.39 E-value: 4.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 1 MVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWPG-----GCGDGIFSPGGAISNMYAMLIARFKMFPEV 75
Cdd:PLN02590 143 VAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQLPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 76 kekGMAAIPRLVALTSEHSHFSVKKGAAALGIGTDSVILIRCDERGK--MIPSDLERRIIEAKQKGFVPFLVSATAGTTV 153
Cdd:PLN02590 223 ---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 154 YGAFDPLLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQ 233
Cdd:PLN02590 300 SAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 234 MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQ 313
Cdd:PLN02590 380 TNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRY 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2263230305 314 HTNVCFWYVPpslrsMEDNEERMNRLLKvapVIKARMMEYGTTMVSYQPLGDKVnFFRMVISNPAATHQDI 384
Cdd:PLN02590 458 FSLVCFRLAP-----VDGDEDQCNERNR---ELLAAVNSTGKIFISHTALSGKF-VLRFAVGAPLTEEKHV 519
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
2-394 |
1.03e-143 |
|
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: 411.98 E-value: 1.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 2 VGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWPGGCGDGIFSPGGAISNMYAMLIARFKMFPEVKEKGMA 81
Cdd:cd06450 12 PALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDRARKRLKAGGGR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 82 AIPRLVALTSEHSHFSVKKGAAALGIgtdSVILIRCDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGTTVYGAFDPLL 161
Cdd:cd06450 92 GIDKLVIVCSDQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 162 AIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVReeglmqscnqmhasylfq 241
Cdd:cd06450 169 EIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 242 qdkhydlsydtgdkalqcgrhvdVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCFWY 321
Cdd:cd06450 231 -----------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--GEPNLSLVCFRL 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2263230305 322 VPPSlrsmedneermnRLLKVAPVIKARMMEYGTTMVSYQPLGDKvNFFRMVISNPAATHQDIDFLIEEIERL 394
Cdd:cd06450 286 KPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDIERA 345
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
1-322 |
2.70e-142 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 409.50 E-value: 2.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 1 MVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWP----GGCGDGIFSPGGAISNMYAMLIARFKMFPEVK 76
Cdd:pfam00282 52 YPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPaeflGQEGGGVLQPGSSESNLLALLAARTKWIKRMK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 77 EKGMAAIP-----RLVALTSEHSHFSVKKGAAALGIGtdsVILIRCDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGT 151
Cdd:pfam00282 132 AAGKPADSsgilaKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 152 TVYGAFDPLLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSC 231
Cdd:pfam00282 209 TGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 232 NQMHASYLFqqdkHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVFdgK 311
Cdd:pfam00282 289 FQFNPLYLG----HTDSAYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--E 362
|
330
....*....|.
gi 2263230305 312 PQHTNVCFWYV 322
Cdd:pfam00282 363 VGLGLVCFRLK 373
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
1-397 |
1.27e-137 |
|
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: 400.75 E-value: 1.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 1 MVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWPGGCgDGIFSPGGAISNMYAMLIARFKMFPE-VKEKG 79
Cdd:COG0076 80 PAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGA-GGVFTSGGTEANLLALLAARDRALARrVRAEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 80 MAAIPRLVALTSEHSHFSVKKGAAALGIGTDSVILIRCDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGTTVYGAFDP 159
Cdd:COG0076 159 LPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 160 LLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYL 239
Cdd:COG0076 239 LAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 240 FQQDkhyDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHTNVCF 319
Cdd:COG0076 319 GPAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCF 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2263230305 320 WYVPPSLRSM-EDNEErmnrllkvapvIKARMMEYGTTMVSYQPLGDKVNfFRMVISNPAATHQDIDFLIEEIERLGQD 397
Cdd:COG0076 394 RYKPAGLDEEdALNYA-----------LRDRLRARGRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
1-384 |
4.06e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 141.39 E-value: 4.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 1 MVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWPG-----GCGDGIFSPGGAISNMYAMLIARFKMFPEV 75
Cdd:PLN02590 143 VAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQLPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 76 kekGMAAIPRLVALTSEHSHFSVKKGAAALGIGTDSVILIRCDERGK--MIPSDLERRIIEAKQKGFVPFLVSATAGTTV 153
Cdd:PLN02590 223 ---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 154 YGAFDPLLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQ 233
Cdd:PLN02590 300 SAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 234 MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQ 313
Cdd:PLN02590 380 TNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRY 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2263230305 314 HTNVCFWYVPpslrsMEDNEERMNRLLKvapVIKARMMEYGTTMVSYQPLGDKVnFFRMVISNPAATHQDI 384
Cdd:PLN02590 458 FSLVCFRLAP-----VDGDEDQCNERNR---ELLAAVNSTGKIFISHTALSGKF-VLRFAVGAPLTEEKHV 519
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
3-340 |
8.51e-34 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 131.18 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 3 GLAADWLTSTANTNMFTYEIAPVFVLLEYVTLRKMREMIGWP-----GGCGDGIFSPGGAISNMYAMLIARFKMfpeVKE 77
Cdd:PLN02880 97 GFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLPeqflsTGNGGGVIQGTASEAVLVVLLAARDRV---LRK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 78 KGMAAIPRLVALTSEHSHFSVKKGAAALGIGTDSVILIR--CDERGKMIPSDLERRIIEAKQKGFVPFLVSATAGTTVYG 155
Cdd:PLN02880 174 VGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKtdSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSST 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 156 AFDPLLAIADICKKYKIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMH 235
Cdd:PLN02880 254 AVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 236 ASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAQIDKCLELAEYLYNKIKNREGYEMVfdGKPQHT 315
Cdd:PLN02880 334 PEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFS 411
|
330 340
....*....|....*....|....*
gi 2263230305 316 NVCFWYVPPSlrSMEDNEERMNRLL 340
Cdd:PLN02880 412 LVCFRLVPPK--NNEDNGNKLNHDL 434
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
50-302 |
2.26e-22 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 97.42 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 50 GIFSPGGAISNMYAMLIARfKMFPEVkekgmaaiprlVALTSEHSHFSVKKGAAALGIGTDsviLIRCDERGKMIPSDLE 129
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKSR---VITSLPNGEIDYDDLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 130 RRIIEAKQKgfvPFLVSATAGTTVYGAFDPLLAIADICKKYKI---WMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWN 206
Cdd:PRK02769 152 SKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAIS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 207 PHKMMGVPLQCSALLVREEGLMQscNQMHASYLfqqdkhydlsyDTGDKALQCGR--HVDVFkLWLMWRAKGTTGFEAQI 284
Cdd:PRK02769 229 GHKFIGSPMPCGIVLAKKKYVER--ISVDVDYI-----------GSRDQTISGSRngHTALL-LWAAIRSLGSKGLRQRV 294
|
250
....*....|....*...
gi 2263230305 285 DKCLELAEYLYNKIKNRE 302
Cdd:PRK02769 295 QHCLDMAQYAVDRLQANG 312
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
44-223 |
2.14e-13 |
|
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: 67.79 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 44 PGGCGDGIFSPGGAISNMYAMLIARfkmfpevkekgmaaIPRLVALTSEHSHFSVKKGAAALgIGTDSVIlIRCDERGKM 123
Cdd:cd01494 14 QPGNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAEL-AGAKPVP-VPVDDAGYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 124 IpsdLERRIIEAKQKGFVPFLVSATAGTTVYGAFDPLLAIADICKKYKIWMHVDAAWGGGllmSRKHKWKLNGVERANSV 203
Cdd:cd01494 78 G---LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG---ASPAPGVLIPEGGADVV 151
|
170 180
....*....|....*....|
gi 2263230305 204 TWNPHKMMGVPlQCSALLVR 223
Cdd:cd01494 152 TFSLHKNLGGE-GGGVVIVK 170
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
50-299 |
4.38e-13 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 69.85 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 50 GIFSPGGAISNMYAMLIARFKMfpevkekgmaaiPRLVALTSEHSHFSVKKGAAALGIGTDSVILIrcdERGKMIPSDLE 129
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 130 RRIIEAKQKgfvPFLVSATAGTTVYGAFDPLLAIADICKKYKI-----WMHVDAAWGGGLLMSRKHKWKLNGVERANSVT 204
Cdd:PLN03032 153 RALAKNRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 205 WNPHKMMGVPLQCSALLVREEGLMQscnqmhasylFQQDKHYDLSYDTGDKALQCGrHVDVFkLWLMWRAKGTTGFEAQI 284
Cdd:PLN03032 230 VSGHKFLGCPMPCGVALTRKKHVKA----------LSQNVEYLNSRDATIMGSRNG-HAPLY-LWYTLRRKGYRGIKRDV 297
|
250
....*....|....*
gi 2263230305 285 DKCLELAEYLYNKIK 299
Cdd:PLN03032 298 QHCMRNAHYLKDRLT 312
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
56-300 |
1.75e-11 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 65.61 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 56 GAISNMYAMLIARfKMFPEVkekgmaaiprlVALTSEHSHFSVKKGAAALGIGtdsVILIRCDERGKMIPSDLERRIIEA 135
Cdd:PLN02263 161 GTEGNLHGILVGR-EVFPDG-----------ILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLAN 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 136 KQKgfvPFLVSATAGTTVYGAFDPLLAIADICKKY-----KIWMHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKM 210
Cdd:PLN02263 226 KDK---PAIINVNIGTTVKGAVDDLDLVIKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 211 MGVPLQCSALLVREEglmqscnqmHASYLfQQDKHYDLSYDTGDKALQCGrHVDVFkLWLMWRAKGTTGFEAQIDKCLEL 290
Cdd:PLN02263 303 VGCPMPCGVQITRME---------HINVL-SSNVEYLASRDATIMGSRNG-HAPIF-LWYTLNRKGYRGFQKEVQKCLRN 370
|
250
....*....|
gi 2263230305 291 AEYLYNKIKN 300
Cdd:PLN02263 371 AHYLKDRLRE 380
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
93-179 |
7.27e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 44.13 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 93 HSHFSVKKGAAALGIGTdsVILIRCDERGKMIPSDLERRIIEAKQKGFVPF-LVSAT-----AGTTVYgAFDPLLAIADI 166
Cdd:pfam01212 81 HIHFDETGGHAELGGVQ--PRPLDGDEAGNMDLEDLEAAIREVGADIFPPTgLISLEnthnsAGGQVV-SLENLREIAAL 157
|
90
....*....|...
gi 2263230305 167 CKKYKIWMHVDAA 179
Cdd:pfam01212 158 AREHGIPVHLDGA 170
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
144-319 |
3.55e-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: 42.23 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 144 LVSATAGTTVYGAFDPLLAIADICKKYKIWMHVDAAWGgglLMSRKHKWKLNGVERANSVTwnpHKMMGvPLQCSALLVR 223
Cdd:pfam00266 142 LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA---IGHRPIDVQKLGVDFLAFSG---HKLYG-PTGIGVLYGR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 224 EEGLmqscNQMH-----ASYLFQQDKHYDLSYDTGDK----------ALQCGRHVDvfklWLMwrakgTTGFEAQIDKCL 288
Cdd:pfam00266 215 RDLL----EKMPpllggGGMIETVSLQESTFADAPWKfeagtpniagIIGLGAALE----YLS-----EIGLEAIEKHEH 281
|
170 180 190
....*....|....*....|....*....|.
gi 2263230305 289 ELAEYLYNKIKNREGYEmVFDGKPQHTNVCF 319
Cdd:pfam00266 282 ELAQYLYERLLSLPGIR-LYGPERRASIISF 311
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
152-237 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 152 TVYGAFDPLLAIADICKKYKIWMHVDAAWGGGLLMS---RKHKWKLNGVERANSVtwnpHKMMGVPLQCSALLVREEGL- 227
Cdd:cd00615 164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKGDLVn 239
|
90
....*....|...
gi 2263230305 228 ---MQSCNQMHAS 237
Cdd:cd00615 240 pdrVNEALNLHQS 252
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
82-225 |
4.01e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.97 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 82 AIPRL----VALTSEHSHFSV---------KKGAaalgigtdSVILIRCDERGKMIPSDLERrIIEAKQKgfvpfLVSAT 148
Cdd:COG0520 96 GLGRLkpgdEILITEMEHHSNivpwqelaeRTGA--------EVRVIPLDEDGELDLEALEA-LLTPRTK-----LVAVT 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2263230305 149 AGTTVYGAFDPLLAIADICKKYKIWMHVDAAWGGGLLmsrkhkwKLNgVERANS--VTWNPHKMMGvPLQCSALLVREE 225
Cdd:COG0520 162 HVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHL-------PVD-VQALGCdfYAFSGHKLYG-PTGIGVLYGKRE 231
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
125-185 |
4.45e-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: 4.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2263230305 125 PSDLERRIIEAKQKgFVPFLVsATAGttVY---GAFDPLLAIADICKKYKIWMHVDAAWGGGLL 185
Cdd:cd06454 117 MEDLEKLLREARRP-YGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
89-179 |
6.16e-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: 38.49 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263230305 89 LTS--EHShfSVKKGAAAL---GIgtdSVILIRCDERGKMIPSDLERRIIEAkqkgfvPFLVSATAG---TtvyGAFDPL 160
Cdd:COG1104 94 ITSaiEHP--AVLETARFLekeGF---EVTYLPVDEDGRVDLEALEAALRPD------TALVSVMHAnneT---GTIQPI 159
|
90
....*....|....*....
gi 2263230305 161 LAIADICKKYKIWMHVDAA 179
Cdd:COG1104 160 AEIAEIAKEHGVLFHTDAV 178
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
119-179 |
7.58e-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: 38.08 E-value: 7.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2263230305 119 ERGKMIPSDLERRIIEAKQKGFV-PFLVS---ATAGTTVYgAFDPLLAIADICKKYKIWMHVDAA 179
Cdd:cd06502 104 ENGKLTPEDLEAAIRPRDDIHFPpPSLVSlenTTEGGTVY-PLDELKAISALAKENGLPLHLDGA 167
|
|
| |
