|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
1-364 |
0e+00 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 733.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 1 SDILHAYDQLLQSKSSVHFGYPYNLMFDYTELAQFMKYSINNLGDPFVPSNYGVHSRQFEVAVIDFFAKLWKMETDSYWG 80
Cdd:PLN03032 9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 81 YVTTSGTEGNLHGILLAREKFPDGILYTSQETHYSVFKAARYYRMECQSIPTLPMGEIDYDCLSEAIARNRDKPVILNVN 160
Cdd:PLN03032 89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 161 IGTTVKGAVDNLDRILRILQSLQIPREQFYIHCDGALFALMMPFVEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGVALSR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 241 KEHVKNLEQHIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTAKGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 219115978 321 LERPMDDDLVKRWQLACEEDIAHVVVMPNVTRYKIDLFVEELMQ 364
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVE 372
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
60-362 |
4.83e-47 |
|
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: 165.78 E-value: 4.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 60 EVAVIDFFAKLWKMEtDSYWGYVTTSGTEGNLHGILLAREKF-------------PDGILYTSQETHYSVFKAARYYRME 126
Cdd:COG0076 109 EREVVRWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRAlarrvraeglpgaPRPRIVVSEEAHSSVDKAARLLGLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 127 CQS---IPTLPMGEIDYDCLSEAIARNR---DKPVILNVNIGTTVKGAVDNLDRILRILQslqipREQFYIHCDGA--LF 198
Cdd:COG0076 188 RDAlrkVPVDEDGRMDPDALEAAIDEDRaagLNPIAVVATAGTTNTGAIDPLAEIADIAR-----EHGLWLHVDAAygGF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 199 ALmmpfveFAPEvsFRKPI------DSIAVSGHKMLGCPMPCGVALSRKE--HVKNLEQHIDYLNS--------VDTTIM 262
Cdd:COG0076 263 AL------PSPE--LRHLLdgieraDSITVDPHKWLYVPYGCGAVLVRDPelLREAFSFHASYLGPaddgvpnlGDYTLE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 263 GSRNGQaALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTA-KGLTcRLNDLSSTVVL------ERPMDDDLVKRWQL 335
Cdd:COG0076 335 LSRRFR-ALKLWATLRALGREGYRELIERCIDLARYLAEGIAAlPGFE-LLAPPELNIVCfrykpaGLDEEDALNYALRD 412
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 219115978 336 ACEED--------------IAHVVVMPNVTRYK-IDLFVEEL 362
Cdd:COG0076 413 RLRARgraflsptkldgrvVLRLVVLNPRTTEDdVDALLDDL 454
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
57-362 |
2.29e-38 |
|
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: 140.03 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 57 RQFEVAVIDFFAKLWKMETDSYWGYVTTSGTEGNLHGILLAREKF--------PDGI----LYTSQETHYSVFKAARYYR 124
Cdd:cd06450 37 TEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDRArkrlkaggGRGIdklvIVCSDQAHVSVEKAAAYLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 125 MECQSIPTLPMGEIDYDCLSEAIARNRDK---PVILNVNIGTTVKGAVDNLDRILRILQSLQIPreqfyIHCDGALFALM 201
Cdd:cd06450 117 VKVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLW-----LHVDAAYGGFL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 202 MPFVEFAPEVsFRKP-IDSIAVSGHKMLGCPMPCGVALSRkehvknleqhidylnsvdttimgsrngqaALYLWYSLRKK 280
Cdd:cd06450 192 LPFPEPRHLD-FGIErVDSISVDPHKYGLVPLGCSAVLVR-----------------------------ALKLWATLRRF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 281 GIGGIKRDVMHCMETARYLKDALTAKG-----------LTC-RLNDLSSTVVLERPMDDDLVKR--WQLA--CEEDIAH- 343
Cdd:cd06450 242 GRDGYGEHIDRIVDLAKYLAELIRADPgfellgepnlsLVCfRLKPSVKLDELNYDLSDRLNERggWHVPatTLGGPNVl 321
|
330 340
....*....|....*....|.
gi 219115978 344 --VVVMPNVTRYKIDLFVEEL 362
Cdd:cd06450 322 rfVVTNPLTTRDDADALLEDI 342
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
60-307 |
4.79e-26 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 107.12 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 60 EVAVIDFFAKLW-----KMETDSYwGYVTTSGTEGNLHGILLAREKF------------PDGI-----LYTSQETHYSVF 117
Cdd:pfam00282 81 ENVVMNWLGEMLglpaeFLGQEGG-GVLQPGSSESNLLALLAARTKWikrmkaagkpadSSGIlaklvAYTSDQAHSSIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 118 KAARYYRMECQSIPTLPMGEIDYDCLSEAIAR---NRDKPVILNVNIGTTVKGAVDNLDRILRILQslqipREQFYIHCD 194
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIEEdkeNGLIPFFVVATLGTTGSGAFDDLQELGDICA-----KHNLWLHVD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 195 GAL--FALMMPfvEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGVALSRKEH--VKNLEQHIDYL----NSVDT---TIMG 263
Cdd:pfam00282 235 AAYggSAFICP--EFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEalQQAFQFNPLYLghtdSAYDTghkQIPL 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 219115978 264 SRnGQAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTAKG 307
Cdd:pfam00282 313 SR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDG 355
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
1-364 |
0e+00 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 733.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 1 SDILHAYDQLLQSKSSVHFGYPYNLMFDYTELAQFMKYSINNLGDPFVPSNYGVHSRQFEVAVIDFFAKLWKMETDSYWG 80
Cdd:PLN03032 9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 81 YVTTSGTEGNLHGILLAREKFPDGILYTSQETHYSVFKAARYYRMECQSIPTLPMGEIDYDCLSEAIARNRDKPVILNVN 160
Cdd:PLN03032 89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 161 IGTTVKGAVDNLDRILRILQSLQIPREQFYIHCDGALFALMMPFVEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGVALSR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 241 KEHVKNLEQHIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTAKGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 219115978 321 LERPMDDDLVKRWQLACEEDIAHVVVMPNVTRYKIDLFVEELMQ 364
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVE 372
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
3-364 |
0e+00 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 574.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 3 ILHAYDQLLQSKSSVHFGYPYNLMFDYTELAQFMKYSINNLGDPFVPSNYGVHSRQFEVAVIDFFAKLWKMETDSYWGYV 82
Cdd:PLN02263 78 VLARYRKTLVERTKHHLGYPYNLDFDYGALGQLQHFSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWEIEKNEYWGYI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 83 TTSGTEGNLHGILLAREKFPDGILYTSQETHYSVFKAARYYRMECQSIPTLPMGEIDYDCLSEAIARNRDKPVILNVNIG 162
Cdd:PLN02263 158 TNCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMECVKVDTLVSGEIDCADFKAKLLANKDKPAIINVNIG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 163 TTVKGAVDNLDRILRILQSLQIPREQFYIHCDGALFALMMPFVEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGVALSRKE 242
Cdd:PLN02263 238 TTVKGAVDDLDLVIKTLEECGFSQDRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRME 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 243 HVKNLEQHIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTAKGLTCRLNDLSSTVVLE 322
Cdd:PLN02263 318 HINVLSSNVEYLASRDATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLREAGISAMLNELSSTVVFE 397
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 219115978 323 RPMDDDLVKRWQLACEEDIAHVVVMPNVTRYKIDLFVEELMQ 364
Cdd:PLN02263 398 RPKDEEFVRRWQLACQGNIAHVVVMPSVTIEKLDYFLKELVE 439
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
11-362 |
3.09e-166 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 469.14 E-value: 3.09e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 11 LQSKSSVHFGYPYNLMFDYTELAQFMKYSINNLGDPFVPSNYGVHSRQFEVAVIDFFAKLWKMETDSYWGYVTTSGTEGN 90
Cdd:PRK02769 18 LRHNQYFNVGYPEAADFDYSALKRFFSFSINNCGDPYSKSNYPLNSFDFERDVMNFFAELFKIPFNESWGYITNGGTEGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 91 LHGILLAREKFPDGILYTSQETHYSVFKAARYYRMECQSIPTLPMGEIDYDCLSEAIARNRDKPVILNVNIGTTVKGAVD 170
Cdd:PRK02769 98 LYGCYLARELFPDGTLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENKNQPPIIFANIGTTMTGAID 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 171 NLDRILRILQSLQIprEQFYIHCDGALFALMMPFVEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGVALSRKEHVKNLEQH 250
Cdd:PRK02769 178 NIKEIQEILKKIGI--DDYYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFIGSPMPCGIVLAKKKYVERISVD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 251 IDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTAKGLTCRLNDLSSTVVLERPmDDDLV 330
Cdd:PRK02769 256 VDYIGSRDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRLQANGIPAWRNPNSITVVFPCP-SERIW 334
|
330 340 350
....*....|....*....|....*....|..
gi 219115978 331 KRWQLACEEDIAHVVVMPNVTRYKIDLFVEEL 362
Cdd:PRK02769 335 KKWHLATSGNQAHIITMPHHNKQQIDSLIDEL 366
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
60-362 |
4.83e-47 |
|
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: 165.78 E-value: 4.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 60 EVAVIDFFAKLWKMEtDSYWGYVTTSGTEGNLHGILLAREKF-------------PDGILYTSQETHYSVFKAARYYRME 126
Cdd:COG0076 109 EREVVRWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRAlarrvraeglpgaPRPRIVVSEEAHSSVDKAARLLGLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 127 CQS---IPTLPMGEIDYDCLSEAIARNR---DKPVILNVNIGTTVKGAVDNLDRILRILQslqipREQFYIHCDGA--LF 198
Cdd:COG0076 188 RDAlrkVPVDEDGRMDPDALEAAIDEDRaagLNPIAVVATAGTTNTGAIDPLAEIADIAR-----EHGLWLHVDAAygGF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 199 ALmmpfveFAPEvsFRKPI------DSIAVSGHKMLGCPMPCGVALSRKE--HVKNLEQHIDYLNS--------VDTTIM 262
Cdd:COG0076 263 AL------PSPE--LRHLLdgieraDSITVDPHKWLYVPYGCGAVLVRDPelLREAFSFHASYLGPaddgvpnlGDYTLE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 263 GSRNGQaALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTA-KGLTcRLNDLSSTVVL------ERPMDDDLVKRWQL 335
Cdd:COG0076 335 LSRRFR-ALKLWATLRALGREGYRELIERCIDLARYLAEGIAAlPGFE-LLAPPELNIVCfrykpaGLDEEDALNYALRD 412
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 219115978 336 ACEED--------------IAHVVVMPNVTRYK-IDLFVEEL 362
Cdd:COG0076 413 RLRARgraflsptkldgrvVLRLVVLNPRTTEDdVDALLDDL 454
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
57-362 |
2.29e-38 |
|
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: 140.03 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 57 RQFEVAVIDFFAKLWKMETDSYWGYVTTSGTEGNLHGILLAREKF--------PDGI----LYTSQETHYSVFKAARYYR 124
Cdd:cd06450 37 TEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDRArkrlkaggGRGIdklvIVCSDQAHVSVEKAAAYLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 125 MECQSIPTLPMGEIDYDCLSEAIARNRDK---PVILNVNIGTTVKGAVDNLDRILRILQSLQIPreqfyIHCDGALFALM 201
Cdd:cd06450 117 VKVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLW-----LHVDAAYGGFL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 202 MPFVEFAPEVsFRKP-IDSIAVSGHKMLGCPMPCGVALSRkehvknleqhidylnsvdttimgsrngqaALYLWYSLRKK 280
Cdd:cd06450 192 LPFPEPRHLD-FGIErVDSISVDPHKYGLVPLGCSAVLVR-----------------------------ALKLWATLRRF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 281 GIGGIKRDVMHCMETARYLKDALTAKG-----------LTC-RLNDLSSTVVLERPMDDDLVKR--WQLA--CEEDIAH- 343
Cdd:cd06450 242 GRDGYGEHIDRIVDLAKYLAELIRADPgfellgepnlsLVCfRLKPSVKLDELNYDLSDRLNERggWHVPatTLGGPNVl 321
|
330 340
....*....|....*....|.
gi 219115978 344 --VVVMPNVTRYKIDLFVEEL 362
Cdd:cd06450 322 rfVVTNPLTTRDDADALLEDI 342
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
60-307 |
4.79e-26 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 107.12 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 60 EVAVIDFFAKLW-----KMETDSYwGYVTTSGTEGNLHGILLAREKF------------PDGI-----LYTSQETHYSVF 117
Cdd:pfam00282 81 ENVVMNWLGEMLglpaeFLGQEGG-GVLQPGSSESNLLALLAARTKWikrmkaagkpadSSGIlaklvAYTSDQAHSSIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 118 KAARYYRMECQSIPTLPMGEIDYDCLSEAIAR---NRDKPVILNVNIGTTVKGAVDNLDRILRILQslqipREQFYIHCD 194
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIEEdkeNGLIPFFVVATLGTTGSGAFDDLQELGDICA-----KHNLWLHVD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 195 GAL--FALMMPfvEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGVALSRKEH--VKNLEQHIDYL----NSVDT---TIMG 263
Cdd:pfam00282 235 AAYggSAFICP--EFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEalQQAFQFNPLYLghtdSAYDTghkQIPL 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 219115978 264 SRnGQAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTAKG 307
Cdd:pfam00282 313 SR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDG 355
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
81-248 |
3.17e-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: 48.40 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 81 YVTTSGTEGN---LHGILLAREKfPDGILYTSQEtHYSVF----KAARYYRMECQSIPTLPMGEIDYDCLSEAIarnRDK 153
Cdd:pfam00266 65 IFTSGTTEAInlvALSLGRSLKP-GDEIVITEME-HHANLvpwqELAKRTGARVRVLPLDEDGLLDLDELEKLI---TPK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 154 PVILNVNIGTTVKGAVDNLDRILRILQSLQIpreqfYIHCDGALFALMMPfvefapeVSFRK-PIDSIAVSGHKMLGcPM 232
Cdd:pfam00266 140 TKLVAITHVSNVTGTIQPVPEIGKLAHQYGA-----LVLVDAAQAIGHRP-------IDVQKlGVDFLAFSGHKLYG-PT 206
|
170
....*....|....*.
gi 219115978 233 PCGVALSRKEHVKNLE 248
Cdd:pfam00266 207 GIGVLYGRRDLLEKMP 222
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
81-236 |
9.25e-04 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 40.87 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 81 YVTTSGTEGN---LHGILLAREKFPDGILYTSQEtHYSVFKAARYYRMECQSIPTLPM---GEIDYDCLSEAIarnRDKP 154
Cdd:PRK02948 64 YFTSGGTESNylaIQSLLNALPQNKKHIITTPME-HASIHSYFQSLESQGYTVTEIPVdksGLIRLVDLERAI---TPDT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 155 VILNVNIGTTVKGAVDNLDRILRILQSLQIpreqfYIHCDgalfaLMMPFVEFAPEVsFRKPIDSIAVSGHKMLGcpmPC 234
Cdd:PRK02948 140 VLASIQHANSEIGTIQPIAEIGALLKKYNV-----LFHSD-----CVQTFGKLPIDV-FEMGIDSLSVSAHKIYG---PK 205
|
..
gi 219115978 235 GV 236
Cdd:PRK02948 206 GV 207
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
58-305 |
9.90e-04 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 41.05 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 58 QFEVAVIDFFAKLWK-----METDSYWGYVTTSGTEGNLHGILLAREK---------FPDGILYTSQETHYSVFKAARYY 123
Cdd:PLN02880 122 ELEMIVLDWLAKLLNlpeqfLSTGNGGGVIQGTASEAVLVVLLAARDRvlrkvgknaLEKLVVYASDQTHSALQKACQIA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 124 RMECQSIPTLPMG-----EIDYDCLSEAIARNRDK---PVILNVNIGTTVKGAVDNLDRILRILQSLQIpreqfYIHCDG 195
Cdd:PLN02880 202 GIHPENCRLLKTDsstnyALAPELLSEAISTDLSSgliPFFLCATVGTTSSTAVDPLLELGKIAKSNGM-----WFHVDA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 196 ALF--ALMMPfvEFAPEVSFRKPIDSIAVSGHKMLGCPMPCGV--ALSRKEHVKNLEQHIDYL-------NSV----DTT 260
Cdd:PLN02880 277 AYAgsACICP--EYRHYIDGVEEADSFNMNAHKWFLTNFDCSLlwVKDRNALIQSLSTNPEFLknkasqaNSVvdykDWQ 354
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 219115978 261 I-MGSRNgqAALYLWYSLRKKGIGGIKRDVMHCMETARYLKDALTA 305
Cdd:PLN02880 355 IpLGRRF--RSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQ 398
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
59-349 |
1.21e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 40.37 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 59 FEVAVIDFFAKLWKMETDSYWGYVTTSGTEGNLhGILLAREKFPDGILYTSQETHYSVFKAARYYRMECQSIPTLPM--G 136
Cdd:pfam00155 44 LREALAKFLGRSPVLKLDREAAVVFGSGAGANI-EALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSndF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 137 EIDYDCLSEAIarnRDKPVIL---NVNIGTtvkGAVDNLDRILRILQSLQipREQFYIHCDGALFALMMPFVEFAPEVSF 213
Cdd:pfam00155 123 HLDFDALEAAL---KEKPKVVlhtSPHNPT---GTVATLEELEKLLDLAK--EHNILLLVDEAYAGFVFGSPDAVATRAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 214 RKPIDSIAVSG--HKMLGCP-MPCGVALSRKEhVknleqhIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIGGIKRDVM 290
Cdd:pfam00155 195 LAEGPNLLVVGsfSKAFGLAgWRVGYILGNAA-V------ISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQ 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219115978 291 HCMETARYLKDALTAKGLTCRLND--LSSTVVLERPMDDDLvkrWQLACEEdiAHVVVMPN 349
Cdd:pfam00155 268 RIKERRDYLRDGLQAAGLSVLPSQagFFLLTGLDPETAKEL---AQVLLEE--VGVYVTPG 323
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
80-232 |
1.72e-03 |
|
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: 38.90 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219115978 80 GYVTTSGTEGNLHGILLAREKfPDGILYTSQETHYSVFKAARyyRMECQSIPT----LPMGEIDYDCLSEAIARNRDKPV 155
Cdd:cd01494 20 AVFVPSGTGANEAALLALLGP-GDEVIVDANGHGSRYWVAAE--LAGAKPVPVpvddAGYGGLDVAILEELKAKPNVALI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219115978 156 ILNVNIGTTvkGAVDNLDRILRILQSLQIpreqfYIHCDGALFALMMPFVEFAPEVSFrkpIDSIAVSGHKMLGCPM 232
Cdd:cd01494 97 VITPNTTSG--GVLVPLKEIRKIAKEYGI-----LLLVDAASAGGASPAPGVLIPEGG---ADVVTFSLHKNLGGEG 163
|
|
|