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Conserved domains on  [gi|550544201|ref|NP_001272378|]
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pyridoxal-dependent decarboxylase domain-containing protein 1 isoform 6 [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) ...
172-394 1.32e-21

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: 95.73  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 172 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 248
Cdd:cd06450   94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 249 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 321
Cdd:cd06450  163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550544201 322 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 394
Cdd:cd06450  227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
172-394 1.32e-21

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: 95.73  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 172 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 248
Cdd:cd06450   94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 249 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 321
Cdd:cd06450  163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550544201 322 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 394
Cdd:cd06450  227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
164-394 2.49e-18

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];


Pssm-ID: 223154 [Multi-domain]  Cd Length: 460  Bit Score: 87.43  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 164 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 243
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 244 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 312
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 313 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 378
Cdd:COG0076  288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                        250
                 ....*....|....*.
gi 550544201 379 ILVEDELssPVVVFRF 394
Cdd:COG0076  366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
171-393 1.34e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 68.98  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  171 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 249
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  250 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 327
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  328 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 392
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 550544201  393 R 393
Cdd:pfam00282 371 R 371
PLN02880 PLN02880
tyrosine decarboxylase
172-429 1.22e-06

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 50.68  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 172 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGRLPLLLVANAGTAAVG 248
Cdd:PLN02880 180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 249 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AAAKCDSMTMTPGPWLgLPAVPAVTLYKHDDP 319
Cdd:PLN02880 254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 320 ALTLVAG----LTSNKPTD----------------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQEslkkvnyiki 379
Cdd:PLN02880 325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 550544201 380 LVEDELSSPVVVFRFFqelpgSDPVFKAVPVPNMTPSGVGRERHSCDALN 429
Cdd:PLN02880 395 LVAQDSRFEVVTPRIF-----SLVCFRLVPPKNNEDNGNKLNHDLLDAVN 439
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
172-394 1.32e-21

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: 95.73  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 172 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 248
Cdd:cd06450   94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 249 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 321
Cdd:cd06450  163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550544201 322 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 394
Cdd:cd06450  227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
164-394 2.49e-18

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];


Pssm-ID: 223154 [Multi-domain]  Cd Length: 460  Bit Score: 87.43  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 164 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 243
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 244 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 312
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 313 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 378
Cdd:COG0076  288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                        250
                 ....*....|....*.
gi 550544201 379 ILVEDELssPVVVFRF 394
Cdd:COG0076  366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
171-393 1.34e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 68.98  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  171 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 249
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  250 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 327
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  328 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 392
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 550544201  393 R 393
Cdd:pfam00282 371 R 371
PLN02880 PLN02880
tyrosine decarboxylase
172-429 1.22e-06

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 50.68  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 172 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGRLPLLLVANAGTAAVG 248
Cdd:PLN02880 180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 249 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AAAKCDSMTMTPGPWLgLPAVPAVTLYKHDDP 319
Cdd:PLN02880 254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 320 ALTLVAG----LTSNKPTD----------------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQEslkkvnyiki 379
Cdd:PLN02880 325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 550544201 380 LVEDELSSPVVVFRFFqelpgSDPVFKAVPVPNMTPSGVGRERHSCDALN 429
Cdd:PLN02880 395 LVAQDSRFEVVTPRIF-----SLVCFRLVPPKNNEDNGNKLNHDLLDAVN 439
PRK02769 PRK02769
histidine decarboxylase; Provisional
201-376 3.69e-05

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 45.80  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 201 LCRVPCNTVfGSQH--QMDVAFLEKLIKDDIERgrlPLLLVANAGTAAVGHTDKIGRLKELCEQYGI---WLHVEGVnLA 275
Cdd:PRK02769 129 LLRIKSRVI-TSLPngEIDYDDLISKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAA-LS 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 276 TLALGYV--SSSVLAAAKCDSMTMTPGPWLGLPaVPA---VTLYKHDDPALTLVAGLTSNKPT-----DKLRALPLWLSL 345
Cdd:PRK02769 204 GMILPFVnnPPPFSFADGIDSIAISGHKFIGSP-MPCgivLAKKKYVERISVDVDYIGSRDQTisgsrNGHTALLLWAAI 282
                        170       180       190
                 ....*....|....*....|....*....|.
gi 550544201 346 QYLGLDGFVERIKHACQLSQRLQESLKKVNY 376
Cdd:PRK02769 283 RSLGSKGLRQRVQHCLDMAQYAVDRLQANGI 313
PLN02590 PLN02590
probable tyrosine decarboxylase
221-408 1.87e-04

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 43.93  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 221 LEKLIKDDIERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLAL-GYVSSSVLAAAKCDSMTMTP 299
Cdd:PLN02590 274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIcPEYRKFIDGIENADSFNMNA 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 300 GPWLgLPAVPAVTLYKHDDPALtlvagltsnkpTDKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQeSLKKVNYIKI 379
Cdd:PLN02590 354 HKWL-FANQTCSPLWVKDRYSL-----------IDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFR-SLKLWMVLRL 420
                        170       180       190
                 ....*....|....*....|....*....|...
gi 550544201 380 LVEDELSS----PVVVFRFFQELPGSDPVFKAV 408
Cdd:PLN02590 421 YGSENLRNfirdHVNLAKHFEDYVAQDPSFEVV 453
PLN03032 PLN03032
serine decarboxylase; Provisional
235-414 4.47e-04

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 42.51  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 235 PLLLVANAGTAAVGHTDKIGRLKELCEQYGI-----WLHVEGVnLATLALGYVSSSVLAAAK--CDSMTMTPGPWLGLPa 307
Cdd:PLN03032 162 PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGA-LFGLMMPFVSRAPEVTFRkpIGSVSVSGHKFLGCP- 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 308 VP---AVTLYKHDDPALTLVAGLTSNKPT-----DKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKI 379
Cdd:PLN03032 240 MPcgvALTRKKHVKALSQNVEYLNSRDATimgsrNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCR 319
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 550544201 380 LveDELSSPVVVFRFFQE-------LPGSDPVFKAVPVPNMT 414
Cdd:PLN03032 320 L--NELSSTVVFERPMDEafikkwqLACEGDIAHVVVMPNVT 359
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
208-296 6.09e-03

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 38.85  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201 208 TVFGSQHQMDVAFLEKLI--KDDIERGRLPLLLVANAGTAAVGHT-DKIGRLKELCEQYGIWLHVEGVNLAtlalgyvss 284
Cdd:cd06502  100 PVPGENGKLTPEDLEAAIrpRDDIHFPPPSLVSLENTTEGGTVYPlDELKAISALAKENGLPLHLDGARLA--------- 170
                         90
                 ....*....|..
gi 550544201 285 SVLAAAKCDSMT 296
Cdd:cd06502  171 NAAAALGVALKT 182
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
216-297 9.57e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 37.97  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544201  216 MDVAFLEKLIK--DDIERGRLPLLLVANAGTAAVGHT---DKIGRLKELCEQYGIWLHVEGVNLATLAlgyVSSSVLAA- 289
Cdd:pfam01212 109 MDLEDLEAAIRevGADIFPPTGLISLENTHNSAGGQVvslENLREIAALAREHGIPVHLDGARFANAA---VALGVIVKe 185
                          90
                  ....*....|
gi 550544201  290 --AKCDSMTM 297
Cdd:pfam01212 186 itSYADSVTM 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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