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Conserved domains on  [gi|2217279324|ref|XP_047281938|]
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sphingosine-1-phosphate lyase 1 isoform X3 [Homo sapiens]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 144-366 4.08e-85

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).


The actual alignment was detected with superfamily member cd06450:

Pssm-ID: 450240 [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
 
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
 
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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