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Conserved domains on  [gi|31982936|ref|NP_003892|]
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sphingosine-1-phosphate lyase 1 [Homo sapiens]

Protein Classification

aspartate aminotransferase family protein( domain architecture ID 10157828)

aspartate aminotransferase family protein is a pyridoxal phosphate (PLP)-dependent enzyme similar to cysteine sulfinic acid decarboxylase that catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine, and taurine, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 144-507 1.88e-112

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: 338.79  E-value: 1.88e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 144 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 222
Cdd:cd06450   1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 223 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 289
Cdd:cd06450  79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 290 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLYSdk 369
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 370 kyrnyqffvdtdwqggiyasptiagsrpggiSAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLS 449
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982936 450 VIALGSR-----DFDIYRLSNLMTAKG-WNLNQLQF--PPSIHFCITLLHARKRVAIQFLKDIRES 507
Cdd:cd06450 280 LVCFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 144-507 1.88e-112

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: 338.79  E-value: 1.88e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 144 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 222
Cdd:cd06450   1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 223 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 289
Cdd:cd06450  79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 290 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLYSdk 369
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 370 kyrnyqffvdtdwqggiyasptiagsrpggiSAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLS 449
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982936 450 VIALGSR-----DFDIYRLSNLMTAKG-WNLNQLQF--PPSIHFCITLLHARKRVAIQFLKDIRES 507
Cdd:cd06450 280 LVCFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 115-508 2.87e-88

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: 280.18  E-value: 2.87e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 115 ALPSQGLSSSAVLEKLKE-YSSMDAFWQEGRASGTVYSG---EEKLTELLVKAYGdfawSNPLHPDIFPGLRKIEAEIVR 190
Cdd:COG0076  39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEK--------GIKTPEIVAPQSAHAAFNKAASYFGMK---IVRV 259
Cdd:COG0076 115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 260 PLTKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEkagypL 333
Cdd:COG0076 195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPE-----L 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 334 EHPFDfRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVD-----TDWQGGI-YASPTIAGSRPGGIsAACWAA 407
Cdd:COG0076 270 RHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHasylgPADDGVPnLGDYTLELSRRFRA-LKLWAT 347

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 408 LMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIA-------LGSRDFDIYRLSNLMTAKGwnlnQLQFP 480
Cdd:COG0076 348 LRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARG----RAFLS 423

                       410       420       430
                ....*....|....*....|....*....|....*
gi 31982936 481 PS-------IHFCITLLHARKRVAIQFLKDIRESV 508
Cdd:COG0076 424 PTkldgrvvLRLVVLNPRTTEDDVDALLDDLREAA 458
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 122-506 4.55e-82

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: 261.13  E-value: 4.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   122 SSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTellVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 201
Cdd:TIGR03812   1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   202 SCGCVTSGGTESILMACKAYRDLAFEKGiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTA 281
Cdd:TIGR03812  77 AYGYIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   282 MLV--CSTPQFphGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLehPFDFRVKGVTSISADTHKYGYAPK 359
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   360 GSSLVLYSDKKYRNYqFFVDTDWQGGIYASpTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKG 439
Cdd:TIGR03812 232 PAGGILFRSKSYLKY-LSVDAPYLTVKKQA-TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGF 309

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982936   440 IFVFgNPQLSVIALGSRDFDiyRLSNLMTAKGWNLNQLQFPPSIHFcITLLHARKRVAIQFLKDIRE 506
Cdd:TIGR03812 310 EPVI-EPVLNIVAFEVDDPE--EVRKKLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
PRK02769 PRK02769
histidine decarboxylase; Provisional
 201-453 5.68e-14

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 73.54  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  201 DSCGCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT 280
Cdd:PRK02769  84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  281 ---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP---LHVDACLGGFLIVFMEKagyplEHPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769 159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  355 GYAPKGSSLVLySDKKYRNyQFFVDTDWQGGiyASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSEL 434
Cdd:PRK02769 233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308

                        250
                 ....*....|....*....
gi 31982936  435 ENIkGIFVFGNPQLSVIAL 453
Cdd:PRK02769 309 QAN-GIPAWRNPNSITVVF 326
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 207-452 1.54e-13

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: 72.28  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   207 TSGGTESILMACKAYRDlAFEKGiktPEIVAPQS-AHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAm 282
Cdd:pfam00266  67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMeHHANLVpwqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   283 LVCSTP-QFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmekAGYPlEHPFDFRVKGVTSISADTHKYgYAPKGS 361
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   362 SlVLY------------------SDKKYRNYQFFVDTDW--QGGiyaSPTIAGsrpggiSAACWAALMHFGENGYVEATK 421
Cdd:pfam00266 209 G-VLYgrrdllekmppllggggmIETVSLQESTFADAPWkfEAG---TPNIAG------IIGLGAALEYLSEIGLEAIEK 278

                         250       260       270
                  ....*....|....*....|....*....|..
gi 31982936   422 QIIKTARFLKSELENIKGIFVFGNPQL-SVIA 452
Cdd:pfam00266 279 HEHELAQYLYERLLSLPGIRLYGPERRaSIIS 310
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 144-507 1.88e-112

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: 338.79  E-value: 1.88e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 144 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 222
Cdd:cd06450   1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 223 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 289
Cdd:cd06450  79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 290 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLYSdk 369
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 370 kyrnyqffvdtdwqggiyasptiagsrpggiSAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLS 449
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982936 450 VIALGSR-----DFDIYRLSNLMTAKG-WNLNQLQF--PPSIHFCITLLHARKRVAIQFLKDIRES 507
Cdd:cd06450 280 LVCFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 115-508 2.87e-88

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: 280.18  E-value: 2.87e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 115 ALPSQGLSSSAVLEKLKE-YSSMDAFWQEGRASGTVYSG---EEKLTELLVKAYGdfawSNPLHPDIFPGLRKIEAEIVR 190
Cdd:COG0076  39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEK--------GIKTPEIVAPQSAHAAFNKAASYFGMK---IVRV 259
Cdd:COG0076 115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 260 PLTKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEkagypL 333
Cdd:COG0076 195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPE-----L 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 334 EHPFDfRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVD-----TDWQGGI-YASPTIAGSRPGGIsAACWAA 407
Cdd:COG0076 270 RHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHasylgPADDGVPnLGDYTLELSRRFRA-LKLWAT 347

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 408 LMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIA-------LGSRDFDIYRLSNLMTAKGwnlnQLQFP 480
Cdd:COG0076 348 LRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARG----RAFLS 423

                       410       420       430
                ....*....|....*....|....*....|....*
gi 31982936 481 PS-------IHFCITLLHARKRVAIQFLKDIRESV 508
Cdd:COG0076 424 PTkldgrvvLRLVVLNPRTTEDDVDALLDDLREAA 458
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 122-506 4.55e-82

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: 261.13  E-value: 4.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   122 SSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTellVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 201
Cdd:TIGR03812   1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   202 SCGCVTSGGTESILMACKAYRDLAFEKGiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTA 281
Cdd:TIGR03812  77 AYGYIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   282 MLV--CSTPQFphGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLehPFDFRVKGVTSISADTHKYGYAPK 359
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   360 GSSLVLYSDKKYRNYqFFVDTDWQGGIYASpTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKG 439
Cdd:TIGR03812 232 PAGGILFRSKSYLKY-LSVDAPYLTVKKQA-TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGF 309

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982936   440 IFVFgNPQLSVIALGSRDFDiyRLSNLMTAKGWNLNQLQFPPSIHFcITLLHARKRVAIQFLKDIRE 506
Cdd:TIGR03812 310 EPVI-EPVLNIVAFEVDDPE--EVRKKLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
PRK02769 PRK02769
histidine decarboxylase; Provisional
 201-453 5.68e-14

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 73.54  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  201 DSCGCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT 280
Cdd:PRK02769  84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  281 ---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP---LHVDACLGGFLIVFMEKagyplEHPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769 159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  355 GYAPKGSSLVLySDKKYRNyQFFVDTDWQGGiyASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSEL 434
Cdd:PRK02769 233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308

                        250
                 ....*....|....*....
gi 31982936  435 ENIkGIFVFGNPQLSVIAL 453
Cdd:PRK02769 309 QAN-GIPAWRNPNSITVVF 326
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 207-452 1.54e-13

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: 72.28  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   207 TSGGTESILMACKAYRDlAFEKGiktPEIVAPQS-AHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAm 282
Cdd:pfam00266  67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMeHHANLVpwqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   283 LVCSTP-QFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmekAGYPlEHPFDFRVKGVTSISADTHKYgYAPKGS 361
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   362 SlVLY------------------SDKKYRNYQFFVDTDW--QGGiyaSPTIAGsrpggiSAACWAALMHFGENGYVEATK 421
Cdd:pfam00266 209 G-VLYgrrdllekmppllggggmIETVSLQESTFADAPWkfEAG---TPNIAG------IIGLGAALEYLSEIGLEAIEK 278

                         250       260       270
                  ....*....|....*....|....*....|..
gi 31982936   422 QIIKTARFLKSELENIKGIFVFGNPQL-SVIA 452
Cdd:pfam00266 279 HEHELAQYLYERLLSLPGIRLYGPERRaSIIS 310
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
191-436 2.50e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 68.60  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAF----EKG--------IKTPEIVAPQSAHAAFNKAASYFGMKIVR 258
Cdd:pfam00282  92 LGLPAEFLGQEGGGVLQPGSSESNLLALLAARTKWIkrmkAAGkpadssgiLAKLVAYTSDQAHSSIEKAALYGGVKLRE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   259 VPLTKMMEVDVRAMRRAISRN-----TAMLVCSTPQFP-HGVIDPVPEVAKLAVKYKIPLHVDACLGGFLivFMEkagyP 332
Cdd:pfam00282 172 IPSDDNGKMRGMDLEKAIEEDkenglIPFFVVATLGTTgSGAFDDLQELGDICAKHNLWLHVDAAYGGSA--FIC----P 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   333 LEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASP-----TIAGSRPGGIsAACWAA 407
Cdd:pfam00282 246 EFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLSRRFRI-LKLWFV 324

                         250       260
                  ....*....|....*....|....*....
gi 31982936   408 LMHFGENGYVEATKQIIKTARFLKSELEN 436
Cdd:pfam00282 325 IRSLGVEGLQNQIRRHVELAQYLEALIRK 353
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 207-450 6.99e-12

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: 67.38  E-value: 6.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 207 TSGGTESILMACKAyrdLAFEKGIKTPEIVAPQSAHAAFNKAASYF---GMKIVRVPLTKMMEVDVRAMRRAISRNTA-- 281
Cdd:COG1104  68 TSGGTEANNLAIKG---AARAYRKKGKHIITSAIEHPAVLETARFLekeGFEVTYLPVDEDGRVDLEALEAALRPDTAlv 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 282 --MLVCS-TpqfphGVIDPVPEVAKLAVKYKIPLHVDAC--LGgflivfmekagypleH-PFDFRVKGVTSISADTHKYg 355
Cdd:COG1104 145 svMHANNeT-----GTIQPIAEIAEIAKEHGVLFHTDAVqaVG---------------KiPVDVKELGVDLLSLSAHKI- 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 356 YAPKGSSlVLYSDKkyrnyqffvdtdwqgGIYASPTIAGS------RPG--------GISAACWAALMHF-GENGYVEAT 420
Cdd:COG1104 204 YGPKGVG-ALYVRK---------------GVRLEPLIHGGgqerglRSGtenvpgivGLGKAAELAAEELeEEAARLRAL 267

                       250       260       270
                ....*....|....*....|....*....|
gi 31982936 421 KQiiktaRFLKSELENIKGIFVFGNPQLSV 450
Cdd:COG1104 268 RD-----RLEEGLLAAIPGVVINGDPENRL 292
PLN03032 PLN03032
serine decarboxylase; Provisional
 182-435 3.51e-10

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 61.77  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  182 RKIEAEIVRIACSLFNGGPDS-CGCVTSGGTESILMACKAYRDlAFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVP 260
Cdd:PLN03032  65 RQFEVGVLDWFARLWELEKDEyWGYITTCGTEGNLHGILVGRE-VFPDGI----LYASRESHYSVFKAARMYRMEAVKVP 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  261 LTKMMEVDVRAMRRAISRNT---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP-----LHVDACLGGFLIVFMEKAgyP 332
Cdd:PLN03032 140 TLPSGEIDYDDLERALAKNRdkpAILNVNIGTTVKGAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSRA--P 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  333 LehpFDFRvKGVTSISADTHKYGYAPKGSSLVLySDKKY-----RNYQFFVDTDwqggiyasPTIAGSRPGGISAACWAA 407
Cdd:PLN03032 218 E---VTFR-KPIGSVSVSGHKFLGCPMPCGVAL-TRKKHvkalsQNVEYLNSRD--------ATIMGSRNGHAPLYLWYT 284

                        250       260
                 ....*....|....*....|....*...
gi 31982936  408 LMHFGENGYVEATKQIIKTARFLKSELE 435
Cdd:PLN03032 285 LRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 235-446 2.54e-08

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: 56.09  E-value: 2.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 235 IVAPQSAHAaFNKA-----ASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFpHGVI-DPVPEVAKLAVKY 308
Cdd:cd00613 111 VLVPDSAHP-TNPAvartrGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNT-LGVFeDLIKEIADIAHSA 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 309 KIPLHVDA---CLGGflivfmekagypLEHPFDFrvkGVTSISADTHKYG------------------YAPK--GsSLVL 365
Cdd:cd00613 189 GALVYVDGdnlNLTG------------LKPPGEY---GADIVVGNLQKTGvphggggpgagffavkkeLVRFlpG-RLVG 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 366 YSDKKYRNYQFFVDtdwqggiYASPTIAGSRPGGISAACWA-----------ALMHfGENGYVEATKQIIKTARFLKSEL 434
Cdd:cd00613 253 VTKDAEGNRAFRLA-------LQTREQHIRREKATSNICTGqallalmaamyIVYL-GPEGLKEIAERAHLNANYLAKRL 324

                       250
                ....*....|..
gi 31982936 435 ENIKGIFVFGNP 446
Cdd:cd00613 325 KEVGGVLPFNGP 336
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 205-321 3.42e-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: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 205 CVTSGGTESILMACKAYRDlafekgiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTK--MMEVDVRAMRRAISRNTAM 282
Cdd:cd00609  63 VVTNGAQEALSLLLRALLN-------PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEegGFLLDLELLEAAKTPKTKL 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 31982936 283 LVCSTPQFPHGVIDPVPE---VAKLAVKYKIPLHVDACLGGF 321
Cdd:cd00609 136 LYLNNPNNPTGAVLSEEEleeLAELAKKHGILIISDEAYAEL 177
PLN02651 PLN02651
cysteine desulfurase
 207-360 7.02e-08

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 54.66  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  207 TSGGTES----ILMACKAYRDlafekgiKTPEIVAPQSAHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRN 279
Cdd:PLN02651  66 TSGATESnnlaIKGVMHFYKD-------KKKHVITTQTEHKCVLdscRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPD 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  280 TAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmEKAGyplEHPFDFRVKGVTSISADTHKYgYAPK 359
Cdd:PLN02651 139 TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA---------QAVG---KIPVDVDDLGVDLMSISGHKI-YGPK 205


                 .
gi 31982936  360 G 360
Cdd:PLN02651 206 G 206
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 185-339 1.45e-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: 51.61  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 185 EAEIVRIACSLFNGGpDSCGCVTSGGTESILMACKAYRdlafekGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVP--LT 262
Cdd:cd01494   2 LEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLALL------GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPvdDA 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982936 263 KMMEVDVRAMR-RAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFmeKAGYPLEHPFDF 339
Cdd:cd01494  75 GYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPA--PGVLIPEGGADV 150
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
207-317 3.98e-07

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.45  E-value: 3.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936 207 TSGGTESILMACKAYRDLafEKGiktPEIVAPQSAHAA----FNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAM 282
Cdd:COG0520  83 TRGTTEAINLVAYGLGRL--KPG---DEILITEMEHHSnivpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKL 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31982936 283 LVCStpqfpH-----GVIDPVPEVAKLAVKYKIPLHVDAC 317
Cdd:COG0520 158 VAVT-----HvsnvtGTVNPVKEIAALAHAHGALVLVDGA 192
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
205-315 5.35e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.84  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   205 CVTSGGTESILMACKayrdLAFEKGiktPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKM--MEVDVRAMRRAISRNTAM 282
Cdd:pfam00155  67 VFGSGAGANIEALIF----LLANPG---DAILVPAPTYASYIRIARLAGGEVVRYPLYDSndFHLDFDALEAALKEKPKV 139

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 31982936   283 LVCSTPQFPHGVIDPVPE---VAKLAVKYKIPLHVD 315
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVD 175
PLN02590 PLN02590
probable tyrosine decarboxylase
 197-369 9.38e-06

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 48.55  E-value: 9.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  197 NGGpdscGCVTSGGTESILMACKAYRDLAFEKGIKT--PEIVAPQS--AHAAFNKAASYFGM-----KIVRVPLTKMMEV 267
Cdd:PLN02590 194 NGG----GVIQGTGCEAVLVVVLAARDRILKKVGKTllPQLVVYGSdqTHSSFRKACLIGGIheeniRLLKTDSSTNYGM 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  268 DVRAMRRAISRNTA-----MLVCST-PQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFmekagyPLEHPFDFRV 341
Cdd:PLN02590 270 PPESLEEAISHDLAkgfipFFICATvGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIC------PEYRKFIDGI 343

                        170       180
                 ....*....|....*....|....*...
gi 31982936  342 KGVTSISADTHKYGYAPKGSSLVLYSDK 369
Cdd:PLN02590 344 ENADSFNMNAHKWLFANQTCSPLWVKDR 371
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
207-407 1.39e-05

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 47.42  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  207 TSGGTESILMACKAYRDLAFEKG---IKTPeiVAPQSAHAAFNKAASYfGMKIVRVPLTKMMEVDVRAMRRAISRNTAML 283
Cdd:PRK02948  66 TSGGTESNYLAIQSLLNALPQNKkhiITTP--MEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  284 VCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDaCLGGFLIVfmekagyplehPFDFRVKGVTSISADTHKYgYAPKGSSL 363
Cdd:PRK02948 143 SIQHANSEIGTIQPIAEIGALLKKYNVLFHSD-CVQTFGKL-----------PIDVFEMGIDSLSVSAHKI-YGPKGVGA 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 31982936  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 3.47e-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: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936   206 VTSGGTESILMACKayrdLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTK---MMEVDVRAMRRAISR---N 279
Cdd:pfam05889  79 VVPLATGMSLALCL----SALRKRPKAKYVIWPRIDQKSSIKAAERAGFEPRLVETVLdgdYLITDVNDVETIIEEkgeE 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 31982936   280 TAMLVCSTPQ-FPHGVIDPVPEVAKLAVKYKIPLHVDACLG 319
Cdd:pfam05889 155 VILAVLSTTScFAPRSPDNVKEIAKICAEYDVPHLVNGAYG 195
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
209-305 5.09e-04

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 42.82  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  209 GGT---ESILMACKAYrdlafekgiKTPEIVAPQSAHA-AFNKAASYF---GMKIVRVPLTKMMeVDVRAMRRAISRNTA 281
Cdd:PRK00451 137 GATalaEAALMAVRIT---------KRKKVLVSGAVHPeYREVLKTYLkgqGIEVVEVPYEDGV-TDLEALEAAVDDDTA 206

                         90       100
                 ....*....|....*....|....
gi 31982936  282 MLVCSTPQFpHGVIDPVPEVAKLA 305
Cdd:PRK00451 207 AVVVQYPNF-FGVIEDLEEIAEIA 229
PLN02263 PLN02263
serine decarboxylase
 204-436 9.84e-04

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 41.73  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  204 GCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT--- 280
Cdd:PLN02263 155 GYITNCGTEGNLHGILVGREV-FPDGI----LYASRESHYSVFKAARMYRMECVKVDTLVSGEIDCADFKAKLLANKdkp 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  281 AMLVCSTPQFPHGVIDPVPEVAKLA-----VKYKIPLHVDACLGGFLIVFMEKAgyPLehpFDFRvKGVTSISADTHKYG 355
Cdd:PLN02263 230 AIINVNIGTTVKGAVDDLDLVIKTLeecgfSQDRFYIHCDGALFGLMMPFVKRA--PK---VTFK-KPIGSVSVSGHKFV 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  356 YAPKGSSLVL----YSDKKYRNYQFFVDTDwqggiyasPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLK 431
Cdd:PLN02263 304 GCPMPCGVQItrmeHINVLSSNVEYLASRD--------ATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQKCLRNAHYLK 375


                 ....*
gi 31982936  432 SELEN 436
Cdd:PLN02263 376 DRLRE 380
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 212-310 2.67e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 40.25  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982936  212 ESILMACKAYRD--LAFEKGIKT-PEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMME--VDVRAMRRAISRNTAMLVCS 286
Cdd:PRK08361  94 DNVIVTAGAYEAtyLAFESLLEEgDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENEfqPDPDELLELITKRTRMIVIN 173

                         90       100
                 ....*....|....*....|....*..
gi 31982936  287 TPQFPHGVI---DPVPEVAKLAVKYKI 310
Cdd:PRK08361 174 YPNNPTGATldkEVAKAIADIAEDYNI 200
PRK09105 PRK09105
pyridoxal phosphate-dependent aminotransferase;
231-304 4.26e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181651  Cd Length: 370  Bit Score: 39.64  E-value: 4.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982936  231 KTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAiSRNTAMLVCSTPQFPHGVIDPVPEVAKL 304
Cdd:PRK09105 118 PTAGLVTADPTYEAGWRAADAQGAPVAKVPLRADGAHDVKAMLAA-DPNAGLIYICNPNNPTGTVTPRADIEWL 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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