NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370468122|ref|XP_024305964|]
View 

pyridoxal-dependent decarboxylase domain-containing protein 1 isoform X9 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
181-403 1.34e-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: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 181 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 330
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468122 331 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 403
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 ...
181-403 1.34e-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: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 181 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 330
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468122 331 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 403
Cdd:cd06450   227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
173-403 2.54e-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: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 173 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 252
Cdd:COG0076   148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 253 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 321
Cdd:COG0076   217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 322 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 387
Cdd:COG0076   288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                         250
                  ....*....|....*.
gi 1370468122 388 ILVEDELssPVVVFRF 403
Cdd:COG0076   366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
180-402 1.42e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 68.98  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 180 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 258
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 259 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 336
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 337 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 401
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 1370468122 402 R 402
Cdd:pfam00282 371 R 371
PLN02880 PLN02880
tyrosine decarboxylase
181-438 1.37e-06

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 50.68  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 181 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:PLN02880  180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AAAKCDSMTMTPGPWLgLPAVPAVTLYKHDDP 328
Cdd:PLN02880  254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 329 ALTLVAG----LTSNKPTD----------------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQEslkkvnyiki 388
Cdd:PLN02880  325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370468122 389 LVEDELSSPVVVFRFFqelpgSDPVFKAVPVPNMTPSGVGRERHSCDALN 438
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 ...
181-403 1.34e-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: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 181 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 330
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468122 331 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 403
Cdd:cd06450   227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
173-403 2.54e-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: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 173 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 252
Cdd:COG0076   148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 253 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 321
Cdd:COG0076   217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 322 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 387
Cdd:COG0076   288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                         250
                  ....*....|....*.
gi 1370468122 388 ILVEDELssPVVVFRF 403
Cdd:COG0076   366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
180-402 1.42e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 68.98  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 180 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 258
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 259 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 336
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 337 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 401
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 1370468122 402 R 402
Cdd:pfam00282 371 R 371
PLN02880 PLN02880
tyrosine decarboxylase
181-438 1.37e-06

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 50.68  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 181 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:PLN02880  180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AAAKCDSMTMTPGPWLgLPAVPAVTLYKHDDP 328
Cdd:PLN02880  254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 329 ALTLVAG----LTSNKPTD----------------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQEslkkvnyiki 388
Cdd:PLN02880  325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370468122 389 LVEDELSSPVVVFRFFqelpgSDPVFKAVPVPNMTPSGVGRERHSCDALN 438
Cdd:PLN02880  395 LVAQDSRFEVVTPRIF-----SLVCFRLVPPKNNEDNGNKLNHDLLDAVN 439
PRK02769 PRK02769
histidine decarboxylase; Provisional
210-385 3.73e-05

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 45.80  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 210 LCRVPCNTVfGSQH--QMDVAFLEKLIKDDIERgrlPLLLVANAGTAAVGHTDKIGRLKELCEQYGI---WLHVEGVnLA 284
Cdd:PRK02769  129 LLRIKSRVI-TSLPngEIDYDDLISKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAA-LS 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 285 TLALGYV--SSSVLAAAKCDSMTMTPGPWLGLPaVPA---VTLYKHDDPALTLVAGLTSNKPT-----DKLRALPLWLSL 354
Cdd:PRK02769  204 GMILPFVnnPPPFSFADGIDSIAISGHKFIGSP-MPCgivLAKKKYVERISVDVDYIGSRDQTisgsrNGHTALLLWAAI 282
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370468122 355 QYLGLDGFVERIKHACQLSQRLQESLKKVNY 385
Cdd:PRK02769  283 RSLGSKGLRQRVQHCLDMAQYAVDRLQANGI 313
PLN02590 PLN02590
probable tyrosine decarboxylase
230-417 1.89e-04

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 43.93  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 230 LEKLIKDDIERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLAL-GYVSSSVLAAAKCDSMTMTP 308
Cdd:PLN02590  274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIcPEYRKFIDGIENADSFNMNA 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 309 GPWLgLPAVPAVTLYKHDDPALtlvagltsnkpTDKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQeSLKKVNYIKI 388
Cdd:PLN02590  354 HKWL-FANQTCSPLWVKDRYSL-----------IDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFR-SLKLWMVLRL 420
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370468122 389 LVEDELSS----PVVVFRFFQELPGSDPVFKAV 417
Cdd:PLN02590  421 YGSENLRNfirdHVNLAKHFEDYVAQDPSFEVV 453
PLN03032 PLN03032
serine decarboxylase; Provisional
244-423 4.28e-04

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 42.51  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 244 PLLLVANAGTAAVGHTDKIGRLKELCEQYGI-----WLHVEGVnLATLALGYVSSSVLAAAK--CDSMTMTPGPWLGLPa 316
Cdd:PLN03032  162 PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGA-LFGLMMPFVSRAPEVTFRkpIGSVSVSGHKFLGCP- 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 317 VP---AVTLYKHDDPALTLVAGLTSNKPT-----DKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKI 388
Cdd:PLN03032  240 MPcgvALTRKKHVKALSQNVEYLNSRDATimgsrNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCR 319
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370468122 389 LveDELSSPVVVFRFFQE-------LPGSDPVFKAVPVPNMT 423
Cdd:PLN03032  320 L--NELSSTVVFERPMDEafikkwqLACEGDIAHVVVMPNVT 359
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
217-305 6.14e-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: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 217 TVFGSQHQMDVAFLEKLI--KDDIERGRLPLLLVANAGTAAVGHT-DKIGRLKELCEQYGIWLHVEGVNLAtlalgyvss 293
Cdd:cd06502   100 PVPGENGKLTPEDLEAAIrpRDDIHFPPPSLVSLENTTEGGTVYPlDELKAISALAKENGLPLHLDGARLA--------- 170
                          90
                  ....*....|..
gi 1370468122 294 SVLAAAKCDSMT 305
Cdd:cd06502   171 NAAAALGVALKT 182
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
225-306 9.64e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 37.97  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468122 225 MDVAFLEKLIK--DDIERGRLPLLLVANAGTAAVGHT---DKIGRLKELCEQYGIWLHVEGVNLATLAlgyVSSSVLAA- 298
Cdd:pfam01212 109 MDLEDLEAAIRevGADIFPPTGLISLENTHNSAGGQVvslENLREIAALAREHGIPVHLDGARFANAA---VALGVIVKe 185
                          90
                  ....*....|
gi 1370468122 299 --AKCDSMTM 306
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH