|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
144-366 |
4.08e-85 |
|
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: 264.45 E-value: 4.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 144 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 222
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 223 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 289
Cdd:cd06450 79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217279324 290 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLY 366
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLV 229
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
115-411 |
7.66e-73 |
|
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: 236.27 E-value: 7.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 115 ALPSQGLSSSAVLEKLKE-YSSMDAFWQEGRASGTVYSG---EEKLTELLVKAYGdfawSNPLHPDIFPGLRKIEAEIVR 190
Cdd:COG0076 39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEK--------GIKTPEIVAPQSAHAAFNKAASYFGMK---IVRV 259
Cdd:COG0076 115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 260 PLTKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEkagypL 333
Cdd:COG0076 195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPE-----L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 334 EHPFDfRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVD-----TDWQGGI-YASPTIAGSRPGGIsAACWAA 407
Cdd:COG0076 270 RHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHasylgPADDGVPnLGDYTLELSRRFRA-LKLWAT 347
|
....
gi 2217279324 408 LMHF 411
Cdd:COG0076 348 LRAL 351
|
|
| tyr_de_CO2_Arch |
TIGR03812 |
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ... |
122-411 |
6.89e-70 |
|
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274796 Cd Length: 373 Bit Score: 226.08 E-value: 6.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 122 SSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTellVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 201
Cdd:TIGR03812 1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 202 SCGCVTSGGTESILMACKAYRDLAFEKGiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTA 281
Cdd:TIGR03812 77 AYGYIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 282 MLV--CSTPQFphGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLehPFDFRVKGVTSISADTHKYGYAPK 359
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217279324 360 GSSLVLYSDKKYRNYqFFVDTDWQGGIYASpTIAGSRPGGISAACWAALMHF 411
Cdd:TIGR03812 232 PAGGILFRSKSYLKY-LSVDAPYLTVKKQA-TITGTRSGASAAATYAVIKYL 281
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
207-366 |
2.57e-11 |
|
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: 64.96 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 207 TSGGTESILMACKAYRDlAFEKGiktPEIVAPQS-AHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAm 282
Cdd:pfam00266 67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMeHHANLVpwqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 283 LVCSTP-QFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmekAGYPlEHPFDFRVKGVTSISADTHKYgYAPKGS 361
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208
|
....*
gi 2217279324 362 SlVLY 366
Cdd:pfam00266 209 G-VLY 212
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
201-408 |
8.92e-10 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 60.06 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 201 DSCGCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT 280
Cdd:PRK02769 84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 281 ---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP---LHVDACLGGFLIVFMEKagyplEHPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769 159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217279324 355 GYAPKGSSLVLySDKKYRNyQFFVDTDWQGGiyASPTIAGSRPGGISAACWAAL 408
Cdd:PRK02769 233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAI 282
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
144-366 |
4.08e-85 |
|
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: 264.45 E-value: 4.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 144 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 222
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 223 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 289
Cdd:cd06450 79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217279324 290 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLY 366
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLV 229
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
115-411 |
7.66e-73 |
|
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: 236.27 E-value: 7.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 115 ALPSQGLSSSAVLEKLKE-YSSMDAFWQEGRASGTVYSG---EEKLTELLVKAYGdfawSNPLHPDIFPGLRKIEAEIVR 190
Cdd:COG0076 39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEK--------GIKTPEIVAPQSAHAAFNKAASYFGMK---IVRV 259
Cdd:COG0076 115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 260 PLTKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEkagypL 333
Cdd:COG0076 195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPE-----L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 334 EHPFDfRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVD-----TDWQGGI-YASPTIAGSRPGGIsAACWAA 407
Cdd:COG0076 270 RHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHasylgPADDGVPnLGDYTLELSRRFRA-LKLWAT 347
|
....
gi 2217279324 408 LMHF 411
Cdd:COG0076 348 LRAL 351
|
|
| tyr_de_CO2_Arch |
TIGR03812 |
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ... |
122-411 |
6.89e-70 |
|
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274796 Cd Length: 373 Bit Score: 226.08 E-value: 6.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 122 SSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTellVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 201
Cdd:TIGR03812 1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 202 SCGCVTSGGTESILMACKAYRDLAFEKGiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTA 281
Cdd:TIGR03812 77 AYGYIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 282 MLV--CSTPQFphGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLehPFDFRVKGVTSISADTHKYGYAPK 359
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217279324 360 GSSLVLYSDKKYRNYqFFVDTDWQGGIYASpTIAGSRPGGISAACWAALMHF 411
Cdd:TIGR03812 232 PAGGILFRSKSYLKY-LSVDAPYLTVKKQA-TITGTRSGASAAATYAVIKYL 281
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
207-360 |
1.46e-11 |
|
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: 65.45 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 207 TSGGTESILMACKAyrdLAFEKGIKTPEIVAPQSAHAAFNKAASYF---GMKIVRVPLTKMMEVDVRAMRRAISRNTA-- 281
Cdd:COG1104 68 TSGGTEANNLAIKG---AARAYRKKGKHIITSAIEHPAVLETARFLekeGFEVTYLPVDEDGRVDLEALEAALRPDTAlv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 282 --MLVCS-TpqfphGVIDPVPEVAKLAVKYKIPLHVDAC--LGgflivfmekagypleH-PFDFRVKGVTSISADTHKYg 355
Cdd:COG1104 145 svMHANNeT-----GTIQPIAEIAEIAKEHGVLFHTDAVqaVG---------------KiPVDVKELGVDLLSLSAHKI- 203
|
....*
gi 2217279324 356 YAPKG 360
Cdd:COG1104 204 YGPKG 208
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
207-366 |
2.57e-11 |
|
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: 64.96 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 207 TSGGTESILMACKAYRDlAFEKGiktPEIVAPQS-AHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAm 282
Cdd:pfam00266 67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMeHHANLVpwqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 283 LVCSTP-QFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmekAGYPlEHPFDFRVKGVTSISADTHKYgYAPKGS 361
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208
|
....*
gi 2217279324 362 SlVLY 366
Cdd:pfam00266 209 G-VLY 212
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
191-369 |
2.80e-11 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 64.75 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAF----EKG--------IKTPEIVAPQSAHAAFNKAASYFGMKIVR 258
Cdd:pfam00282 92 LGLPAEFLGQEGGGVLQPGSSESNLLALLAARTKWIkrmkAAGkpadssgiLAKLVAYTSDQAHSSIEKAALYGGVKLRE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 259 VPLTKMMEVDVRAMRRAISRN-----TAMLVCSTPQFP-HGVIDPVPEVAKLAVKYKIPLHVDACLGGFLivFMEkagyP 332
Cdd:pfam00282 172 IPSDDNGKMRGMDLEKAIEEDkenglIPFFVVATLGTTgSGAFDDLQELGDICAKHNLWLHVDAAYGGSA--FIC----P 245
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217279324 333 LEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDK 369
Cdd:pfam00282 246 EFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDK 282
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
201-408 |
8.92e-10 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 60.06 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 201 DSCGCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT 280
Cdd:PRK02769 84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 281 ---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP---LHVDACLGGFLIVFMEKagyplEHPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769 159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217279324 355 GYAPKGSSLVLySDKKYRNyQFFVDTDWQGGiyASPTIAGSRPGGISAACWAAL 408
Cdd:PRK02769 233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAI 282
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
205-321 |
2.30e-08 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 55.43 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 205 CVTSGGTESILMACKAYRDlafekgiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTK--MMEVDVRAMRRAISRNTAM 282
Cdd:cd00609 63 VVTNGAQEALSLLLRALLN-------PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEegGFLLDLELLEAAKTPKTKL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2217279324 283 LVCSTPQFPHGVIDPVPE---VAKLAVKYKIPLHVDACLGGF 321
Cdd:cd00609 136 LYLNNPNNPTGAVLSEEEleeLAELAKKHGILIISDEAYAEL 177
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
207-360 |
4.71e-08 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 54.66 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 207 TSGGTES----ILMACKAYRDlafekgiKTPEIVAPQSAHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRN 279
Cdd:PLN02651 66 TSGATESnnlaIKGVMHFYKD-------KKKHVITTQTEHKCVLdscRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 280 TAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmEKAGyplEHPFDFRVKGVTSISADTHKYgYAPK 359
Cdd:PLN02651 139 TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA---------QAVG---KIPVDVDDLGVDLMSISGHKI-YGPK 205
|
.
gi 2217279324 360 G 360
Cdd:PLN02651 206 G 206
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
185-339 |
1.14e-07 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 51.23 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 185 EAEIVRIACSLFNGGpDSCGCVTSGGTESILMACKAYRdlafekGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVP--LT 262
Cdd:cd01494 2 LEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLALL------GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPvdDA 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217279324 263 KMMEVDVRAMR-RAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFmeKAGYPLEHPFDF 339
Cdd:cd01494 75 GYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPA--PGVLIPEGGADV 150
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
235-316 |
1.41e-07 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 53.39 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 235 IVAPQSAHAaFNKA-----ASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFpHGVI-DPVPEVAKLAVKY 308
Cdd:cd00613 111 VLVPDSAHP-TNPAvartrGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNT-LGVFeDLIKEIADIAHSA 188
|
....*...
gi 2217279324 309 KIPLHVDA 316
Cdd:cd00613 189 GALVYVDG 196
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
207-317 |
2.68e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 52.45 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 207 TSGGTESILMACKAYRDLafEKGiktPEIVAPQSAHAA----FNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAM 282
Cdd:COG0520 83 TRGTTEAINLVAYGLGRL--KPG---DEILITEMEHHSnivpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2217279324 283 LVCStpqfpH-----GVIDPVPEVAKLAVKYKIPLHVDAC 317
Cdd:COG0520 158 VAVT-----HvsnvtGTVNPVKEIAALAHAHGALVLVDGA 192
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
182-408 |
3.54e-07 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 52.14 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 182 RKIEAEIVRIACSLFNGGPDS-CGCVTSGGTESILMACKAYRDlAFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVP 260
Cdd:PLN03032 65 RQFEVGVLDWFARLWELEKDEyWGYITTCGTEGNLHGILVGRE-VFPDGI----LYASRESHYSVFKAARMYRMEAVKVP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 261 LTKMMEVDVRAMRRAISRNT---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP-----LHVDACLGGFLIVFMEKAgyP 332
Cdd:PLN03032 140 TLPSGEIDYDDLERALAKNRdkpAILNVNIGTTVKGAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSRA--P 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 333 LehpFDFRvKGVTSISADTHKYGYAPKGSSLVLySDKKY-----RNYQFFVDTDwqggiyasPTIAGSRPGGISAACWAA 407
Cdd:PLN03032 218 E---VTFR-KPIGSVSVSGHKFLGCPMPCGVAL-TRKKHvkalsQNVEYLNSRD--------ATIMGSRNGHAPLYLWYT 284
|
.
gi 2217279324 408 L 408
Cdd:PLN03032 285 L 285
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
205-315 |
3.69e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 48.84 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 205 CVTSGGTESILMACKayrdLAFEKGiktPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKM--MEVDVRAMRRAISRNTAM 282
Cdd:pfam00155 67 VFGSGAGANIEALIF----LLANPG---DAILVPAPTYASYIRIARLAGGEVVRYPLYDSndFHLDFDALEAALKEKPKV 139
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217279324 283 LVCSTPQFPHGVIDPVPE---VAKLAVKYKIPLHVD 315
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVD 175
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
197-369 |
7.87e-06 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 48.17 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 197 NGGpdscGCVTSGGTESILMACKAYRDLAFEKGIKT--PEIVAPQS--AHAAFNKAASYFGM-----KIVRVPLTKMMEV 267
Cdd:PLN02590 194 NGG----GVIQGTGCEAVLVVVLAARDRILKKVGKTllPQLVVYGSdqTHSSFRKACLIGGIheeniRLLKTDSSTNYGM 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 268 DVRAMRRAISRNTA-----MLVCST-PQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFmekagyPLEHPFDFRV 341
Cdd:PLN02590 270 PPESLEEAISHDLAkgfipFFICATvGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIC------PEYRKFIDGI 343
|
170 180
....*....|....*....|....*...
gi 2217279324 342 KGVTSISADTHKYGYAPKGSSLVLYSDK 369
Cdd:PLN02590 344 ENADSFNMNAHKWLFANQTCSPLWVKDR 371
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
207-407 |
9.63e-06 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 47.42 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 207 TSGGTESILMACKAYRDLAFEKG---IKTPeiVAPQSAHAAFNKAASYfGMKIVRVPLTKMMEVDVRAMRRAISRNTAML 283
Cdd:PRK02948 66 TSGGTESNYLAIQSLLNALPQNKkhiITTP--MEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 284 VCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDaCLGGFLIVfmekagyplehPFDFRVKGVTSISADTHKYgYAPKGSSL 363
Cdd:PRK02948 143 SIQHANSEIGTIQPIAEIGALLKKYNVLFHSD-CVQTFGKL-----------PIDVFEMGIDSLSVSAHKI-YGPKGVGA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217279324 364 VlYSDKKYRNYQFFVDTDWQGGIyasptiagsRPG-----GISAACWAA 407
Cdd:PRK02948 210 V-YINPQVRWKPVFPGTTHEKGF---------RPGtvnvpGIAAFLTAA 248
|
|
| SepSecS |
pfam05889 |
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ... |
206-319 |
2.44e-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: 42.96 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 206 VTSGGTESILMACKayrdLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTK---MMEVDVRAMRRAISR---N 279
Cdd:pfam05889 79 VVPLATGMSLALCL----SALRKRPKAKYVIWPRIDQKSSIKAAERAGFEPRLVETVLdgdYLITDVNDVETIIEEkgeE 154
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2217279324 280 TAMLVCSTPQ-FPHGVIDPVPEVAKLAVKYKIPLHVDACLG 319
Cdd:pfam05889 155 VILAVLSTTScFAPRSPDNVKEIAKICAEYDVPHLVNGAYG 195
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
209-305 |
3.56e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 42.82 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 209 GGT---ESILMACKAYrdlafekgiKTPEIVAPQSAHA-AFNKAASYF---GMKIVRVPLTKMMeVDVRAMRRAISRNTA 281
Cdd:PRK00451 137 GATalaEAALMAVRIT---------KRKKVLVSGAVHPeYREVLKTYLkgqGIEVVEVPYEDGV-TDLEALEAAVDDDTA 206
|
90 100
....*....|....*....|....
gi 2217279324 282 MLVCSTPQFpHGVIDPVPEVAKLA 305
Cdd:PRK00451 207 AVVVQYPNF-FGVIEDLEEIAEIA 229
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
212-310 |
1.93e-03 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 40.25 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279324 212 ESILMACKAYRD--LAFEKGIKT-PEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMME--VDVRAMRRAISRNTAMLVCS 286
Cdd:PRK08361 94 DNVIVTAGAYEAtyLAFESLLEEgDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENEfqPDPDELLELITKRTRMIVIN 173
|
90 100
....*....|....*....|....*..
gi 2217279324 287 TPQFPHGVI---DPVPEVAKLAVKYKI 310
Cdd:PRK08361 174 YPNNPTGATldkEVAKAIADIAEDYNI 200
|
|
| PRK09105 |
PRK09105 |
pyridoxal phosphate-dependent aminotransferase; |
231-304 |
3.29e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181651 Cd Length: 370 Bit Score: 39.64 E-value: 3.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217279324 231 KTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAiSRNTAMLVCSTPQFPHGVIDPVPEVAKL 304
Cdd:PRK09105 118 PTAGLVTADPTYEAGWRAADAQGAPVAKVPLRADGAHDVKAMLAA-DPNAGLIYICNPNNPTGTVTPRADIEWL 190
|
|
|