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Conserved domains on  [gi|1229757995|ref|XP_022131455|]
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L-tryptophan--pyruvate aminotransferase 1-like isoform X2 [Momordica charantia]

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) ...
39-405 0e+00

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 pfam04864:

Pssm-ID: 450240  Cd Length: 363  Bit Score: 537.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  39 IDLDPGIPTVFEPYWRRMGDKCRVVIQGCDLMSYRATTTNLcWYLLPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLF 118
Cdd:pfam04864   1 ADLDSGDPLFLEEYWMRHKERTAVLISGWHRMSYFSDTKNL-WFLSPELEREIRRLHRAVGNAVTDDRYIVFGTGSTQLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 119 QAALYALStPAAAAAAPqPINVVSAAPYYSCYPDETDYLCSRLYKWAGDANQYDSKS--GPFIEVVTSPNNPDGCLREPV 196
Cdd:pfam04864  80 QAAVYALS-PNVTPTSP-PVKVVAAVPYYSVYKEQTSYFDSKGYEWKGNASAYVNTDnpGPFIELVTSPNNPDGTLREAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 197 VEAHGqGKLIHDLAYYWPQFTPITRPADHDLMYFTFSKCTGHAGSRIGWALVKDREVAIKMTKYMDLSSIGVSKDSQFRA 276
Cdd:pfam04864 158 IDGSE-AKVIHDLAYYWPHYTPITYPADEDIMLFTMSKYTGHAGSRFGWALVKDEEVAKKMVEYIELNTIGVSKESQLRT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 277 AKIMELLCNNYDQKLGsnfSNNFFEYGKSLMAERWKSLRDVIGRSDVFSLPTFEQQYCCFFGRLSQSYPAFAWLRCK-EE 355
Cdd:pfam04864 237 LKILKVVLATCKTESG---TMDFFDFGYQTMRERWERLRELVSSSTRFSLQKLPPEYCNYFKKIREPSPAYAWLKCEwEE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1229757995 356 IEDCGSFLREHKIEGRSGRRFGADAKYLRISMLSSDDVFQQFLERLSAIK 405
Cdd:pfam04864 314 DTDCYEVLREGKILTRSGERFGADSRYVRLSLIKTQDDFDQLLQRLKSLV 363
 
Name Accession Description Interval E-value
Alliinase_C pfam04864
Allinase; Allicin is a thiosulphinate that gives rise to dithiines, allyl sulphides and ...
39-405 0e+00

Allinase; Allicin is a thiosulphinate that gives rise to dithiines, allyl sulphides and ajoenes, the three groups of active compounds in Allium species. Allicin is synthesized from sulfoxide cysteine derivatives by alliinase (EC:4.4.1.4), whose C-S lyase activity cleaves C(beta)-S(gamma) bonds. It is thought that this enzyme forms part of a primitive plant defence system.


Pssm-ID: 398502  Cd Length: 363  Bit Score: 537.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  39 IDLDPGIPTVFEPYWRRMGDKCRVVIQGCDLMSYRATTTNLcWYLLPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLF 118
Cdd:pfam04864   1 ADLDSGDPLFLEEYWMRHKERTAVLISGWHRMSYFSDTKNL-WFLSPELEREIRRLHRAVGNAVTDDRYIVFGTGSTQLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 119 QAALYALStPAAAAAAPqPINVVSAAPYYSCYPDETDYLCSRLYKWAGDANQYDSKS--GPFIEVVTSPNNPDGCLREPV 196
Cdd:pfam04864  80 QAAVYALS-PNVTPTSP-PVKVVAAVPYYSVYKEQTSYFDSKGYEWKGNASAYVNTDnpGPFIELVTSPNNPDGTLREAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 197 VEAHGqGKLIHDLAYYWPQFTPITRPADHDLMYFTFSKCTGHAGSRIGWALVKDREVAIKMTKYMDLSSIGVSKDSQFRA 276
Cdd:pfam04864 158 IDGSE-AKVIHDLAYYWPHYTPITYPADEDIMLFTMSKYTGHAGSRFGWALVKDEEVAKKMVEYIELNTIGVSKESQLRT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 277 AKIMELLCNNYDQKLGsnfSNNFFEYGKSLMAERWKSLRDVIGRSDVFSLPTFEQQYCCFFGRLSQSYPAFAWLRCK-EE 355
Cdd:pfam04864 237 LKILKVVLATCKTESG---TMDFFDFGYQTMRERWERLRELVSSSTRFSLQKLPPEYCNYFKKIREPSPAYAWLKCEwEE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1229757995 356 IEDCGSFLREHKIEGRSGRRFGADAKYLRISMLSSDDVFQQFLERLSAIK 405
Cdd:pfam04864 314 DTDCYEVLREGKILTRSGERFGADSRYVRLSLIKTQDDFDQLLQRLKSLV 363
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
39-401 9.72e-28

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: 112.43  E-value: 9.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  39 IDLDPGIPTVFEPYWRRmgDKCRVVIQGCDLMSYRATTTnlcwylLPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLF 118
Cdd:cd00609     1 IDLSIGEPDFPPPPEVL--EALAAAALRAGLLGYYPDPG------LPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 119 QAALYALSTPAAaaaapqpiNVVSAAPYYSCYPDETDYLCSRLYKWAGDANQYDSKSGPFIE----------VVTSPNNP 188
Cdd:cd00609    73 SLLLRALLNPGD--------EVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEaaktpktkllYLNNPNNP 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 189 DGCLREP--------VVEAHGqGKLIHDLAYYWPQFTPITRPA-------DHDLMYFTFSKCTGHAGSRIGWALVKDREV 253
Cdd:cd00609   145 TGAVLSEeeleelaeLAKKHG-ILIISDEAYAELVYDGEPPPAlalldayERVIVLRSFSKTFGLPGLRIGYLIAPPEEL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 254 AIKMTKYMDLSSIGVSKDSQFRAAkimELLCNNYDqklgsnfsnnFFEYGKSLMAERWKSLRDVIGRSDvfslptfeqqy 333
Cdd:cd00609   224 LERLKKLLPYTTSGPSTLSQAAAA---AALDDGEE----------HLEELRERYRRRRDALLEALKELG----------- 279
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229757995 334 ccFFGRLSQSYPAFAWLRCKEEI--EDCGSFLREHKIEGRSGRRFGADAK-YLRISMLSSDDVFQQFLERL 401
Cdd:cd00609   280 --PLVVVKPSGGFFLWLDLPEGDdeEFLERLLLEAGVVVRPGSAFGEGGEgFVRLSFATPEEELEEALERL 348
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
84-403 1.48e-11

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 65.54  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  84 LPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLFQAALYALstpaaaaaapqpIN----VVSAAPYYSCYPDETD---- 155
Cdd:COG0436    69 IPELREAIAAYYKRRYGVDLDPDEILVTNGAKEALALALLAL------------LNpgdeVLVPDPGYPSYRAAVRlagg 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 156 ----YLCSRLYKWAGDANQYDSKSGP---FIeVVTSPNNPDGCLREP--------VVEAHGqGKLIHDLAY----Y--WP 214
Cdd:COG0436   137 kpvpVPLDEENGFLPDPEALEAAITPrtkAI-VLNSPNNPTGAVYSReelealaeLAREHD-LLVISDEIYeelvYdgAE 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 215 QFTPITRPADHD--LMYFTFSKCTGHAGSRIGWALVkDREVAIKMTKYMDLSSIGVSKDSQFRAAKIMELLCNNYDQklg 292
Cdd:COG0436   215 HVSILSLPGLKDrtIVINSFSKSYAMTGWRIGYAVG-PPELIAALLKLQSNLTSCAPTPAQYAAAAALEGPQDYVEE--- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 293 snfsnnffeygkslMAERWKSLRDV-------IGrsdvFSLP----TFeqqyccffgrlsqsypaFAWLRCKEEIEDCGS 361
Cdd:COG0436   291 --------------MRAEYRRRRDLlveglneIG----LSVVkpegAF-----------------YLFADVPELGLDSEE 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1229757995 362 F----LREHKIEGRSGRRFGADAK-YLRISMLSSDDVFQQFLERLSA 403
Cdd:COG0436   336 FaerlLEEAGVAVVPGSAFGPAGEgYVRISYATSEERLEEALERLAR 382
GntC_guanitoxin NF041364
guanitoxin biosynthesis PLP-dependent (S)-gamma-hydroxy-L-arginine cyclodehydratase GntC;
84-403 3.49e-08

guanitoxin biosynthesis PLP-dependent (S)-gamma-hydroxy-L-arginine cyclodehydratase GntC;


Pssm-ID: 469255  Cd Length: 354  Bit Score: 55.04  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  84 LPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLFQAALYALSTPAAaaaapqpiNVVSAAPYYSCYPDETDYLCSRLYK 163
Cdd:NF041364   39 SLELREAIAALYKDGYGIEVSPDQVLVTTGASEALFLYFHALLEPGD--------EVVVPVPAFQSLYEVPELLGGRVRP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 164 WA-GDANQydsKSGPFIE-------------VVTSPNNPDGC-LREPVVEA-------HGqGKLIHDLAYywpQFTPITR 221
Cdd:NF041364  111 LPlSPENQ---GFRPDLEalrslitprtraiVINSPNNPTGAvMTEAELEAileiasrHG-LIVLADEHY---RFLPYDD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 222 PADHDLMYF-----------TFSKCTGHAGSRIGWaLVKDREVAIKMTKYMDLSSIGVSKDSQFRAAkimELLCNNYDQK 290
Cdd:NF041364  184 GKHVSPSLYpglservialgSFSKTYGMTGLRVGW-LIGPKELIGAILKFKDYTTHCAPSISQYAAL---EALEQGPQER 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 291 L-GSNFSNnffeygKSLMAERWKSLRDVIG-----RSDVFSLPtfeqqyccffgRLSQSYPAFAWlrCKEEIEDCGSFLR 364
Cdd:NF041364  260 VkGWVREN------VRRRDALVERLERLIGwvcepEGGFYAFP-----------KLKDGLPSAAF--AEELLEKAGVVVL 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1229757995 365 EHKIEGRSGRRfgadakYLRISMLSSDDVFQQFLERLSA 403
Cdd:NF041364  321 PGSAFGRPGEG------YFRIGFANSPTRLKEALERLSR 353
hisC TIGR01141
histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; ...
86-259 1.96e-05

histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; imidazole acetol-phosphate transaminase Histidinol-phosphate aminotransferase is a pyridoxal-phosphate dependent enzyme. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273467  Cd Length: 350  Bit Score: 46.11  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  86 ELEEAIRRLHRV---VGNAV---------VDERHVVVGTGSTQLFQAALYALSTPAaaaaapqpINVVSAAPYYSCYPDE 153
Cdd:TIGR01141  41 ALRAELKKLHRYpdpDPAELkqaladyygVDPEQILLGNGSDEIIDLLIRAFLEPG--------DAVLVPPPTYSMYEIS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 154 TDYL--CSRLYKWAGDaNQYD-------SKSGPFIEVVTSPNNPDG-CLREPVVEA-----HGQGKLIHDLAYY----WP 214
Cdd:TIGR01141 113 AKIHgaEVVKVPLDED-GQLDledilvaIDDKPKLVFLCSPNNPTGnLFSRGDIEAvlertPGDALVVVDEAYGefsgEP 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1229757995 215 QFTPITRPADHDLMYFTFSKCTGHAGSRIGWALVKDrEVAIKMTK 259
Cdd:TIGR01141 192 STLPLLAEYPNLIVLRTLSKAFGLAGLRIGYAIANA-EIIDALNK 235
PRK05166 PRK05166
histidinol-phosphate transaminase;
175-259 1.40e-03

histidinol-phosphate transaminase;


Pssm-ID: 179950  Cd Length: 371  Bit Score: 40.51  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 175 SGPFIEVVTSPNNPDGCLREP-----VVEAHGQGKLIH-DLAYY-------WPQFTPITRPADHDLMYF-TFSKCTGHAG 240
Cdd:PRK05166  158 RAPRMLMFSNPSNPVGSWLTAdqlarVLDATPPETLIVvDEAYAeyaagddYPSALTLLKARGLPWIVLrTFSKAYGLAG 237
                          90
                  ....*....|....*....
gi 1229757995 241 SRIGWALVKDREVAIKMTK 259
Cdd:PRK05166  238 LRVGYGLVSDPELVGLLDR 256
 
Name Accession Description Interval E-value
Alliinase_C pfam04864
Allinase; Allicin is a thiosulphinate that gives rise to dithiines, allyl sulphides and ...
39-405 0e+00

Allinase; Allicin is a thiosulphinate that gives rise to dithiines, allyl sulphides and ajoenes, the three groups of active compounds in Allium species. Allicin is synthesized from sulfoxide cysteine derivatives by alliinase (EC:4.4.1.4), whose C-S lyase activity cleaves C(beta)-S(gamma) bonds. It is thought that this enzyme forms part of a primitive plant defence system.


Pssm-ID: 398502  Cd Length: 363  Bit Score: 537.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  39 IDLDPGIPTVFEPYWRRMGDKCRVVIQGCDLMSYRATTTNLcWYLLPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLF 118
Cdd:pfam04864   1 ADLDSGDPLFLEEYWMRHKERTAVLISGWHRMSYFSDTKNL-WFLSPELEREIRRLHRAVGNAVTDDRYIVFGTGSTQLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 119 QAALYALStPAAAAAAPqPINVVSAAPYYSCYPDETDYLCSRLYKWAGDANQYDSKS--GPFIEVVTSPNNPDGCLREPV 196
Cdd:pfam04864  80 QAAVYALS-PNVTPTSP-PVKVVAAVPYYSVYKEQTSYFDSKGYEWKGNASAYVNTDnpGPFIELVTSPNNPDGTLREAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 197 VEAHGqGKLIHDLAYYWPQFTPITRPADHDLMYFTFSKCTGHAGSRIGWALVKDREVAIKMTKYMDLSSIGVSKDSQFRA 276
Cdd:pfam04864 158 IDGSE-AKVIHDLAYYWPHYTPITYPADEDIMLFTMSKYTGHAGSRFGWALVKDEEVAKKMVEYIELNTIGVSKESQLRT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 277 AKIMELLCNNYDQKLGsnfSNNFFEYGKSLMAERWKSLRDVIGRSDVFSLPTFEQQYCCFFGRLSQSYPAFAWLRCK-EE 355
Cdd:pfam04864 237 LKILKVVLATCKTESG---TMDFFDFGYQTMRERWERLRELVSSSTRFSLQKLPPEYCNYFKKIREPSPAYAWLKCEwEE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1229757995 356 IEDCGSFLREHKIEGRSGRRFGADAKYLRISMLSSDDVFQQFLERLSAIK 405
Cdd:pfam04864 314 DTDCYEVLREGKILTRSGERFGADSRYVRLSLIKTQDDFDQLLQRLKSLV 363
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
39-401 9.72e-28

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: 112.43  E-value: 9.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  39 IDLDPGIPTVFEPYWRRmgDKCRVVIQGCDLMSYRATTTnlcwylLPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLF 118
Cdd:cd00609     1 IDLSIGEPDFPPPPEVL--EALAAAALRAGLLGYYPDPG------LPELREAIAEWLGRRGGVDVPPEEIVVTNGAQEAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 119 QAALYALSTPAAaaaapqpiNVVSAAPYYSCYPDETDYLCSRLYKWAGDANQYDSKSGPFIE----------VVTSPNNP 188
Cdd:cd00609    73 SLLLRALLNPGD--------EVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEaaktpktkllYLNNPNNP 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 189 DGCLREP--------VVEAHGqGKLIHDLAYYWPQFTPITRPA-------DHDLMYFTFSKCTGHAGSRIGWALVKDREV 253
Cdd:cd00609   145 TGAVLSEeeleelaeLAKKHG-ILIISDEAYAELVYDGEPPPAlalldayERVIVLRSFSKTFGLPGLRIGYLIAPPEEL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 254 AIKMTKYMDLSSIGVSKDSQFRAAkimELLCNNYDqklgsnfsnnFFEYGKSLMAERWKSLRDVIGRSDvfslptfeqqy 333
Cdd:cd00609   224 LERLKKLLPYTTSGPSTLSQAAAA---AALDDGEE----------HLEELRERYRRRRDALLEALKELG----------- 279
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229757995 334 ccFFGRLSQSYPAFAWLRCKEEI--EDCGSFLREHKIEGRSGRRFGADAK-YLRISMLSSDDVFQQFLERL 401
Cdd:cd00609   280 --PLVVVKPSGGFFLWLDLPEGDdeEFLERLLLEAGVVVRPGSAFGEGGEgFVRLSFATPEEELEEALERL 348
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
84-403 1.48e-11

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 65.54  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  84 LPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLFQAALYALstpaaaaaapqpIN----VVSAAPYYSCYPDETD---- 155
Cdd:COG0436    69 IPELREAIAAYYKRRYGVDLDPDEILVTNGAKEALALALLAL------------LNpgdeVLVPDPGYPSYRAAVRlagg 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 156 ----YLCSRLYKWAGDANQYDSKSGP---FIeVVTSPNNPDGCLREP--------VVEAHGqGKLIHDLAY----Y--WP 214
Cdd:COG0436   137 kpvpVPLDEENGFLPDPEALEAAITPrtkAI-VLNSPNNPTGAVYSReelealaeLAREHD-LLVISDEIYeelvYdgAE 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 215 QFTPITRPADHD--LMYFTFSKCTGHAGSRIGWALVkDREVAIKMTKYMDLSSIGVSKDSQFRAAKIMELLCNNYDQklg 292
Cdd:COG0436   215 HVSILSLPGLKDrtIVINSFSKSYAMTGWRIGYAVG-PPELIAALLKLQSNLTSCAPTPAQYAAAAALEGPQDYVEE--- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 293 snfsnnffeygkslMAERWKSLRDV-------IGrsdvFSLP----TFeqqyccffgrlsqsypaFAWLRCKEEIEDCGS 361
Cdd:COG0436   291 --------------MRAEYRRRRDLlveglneIG----LSVVkpegAF-----------------YLFADVPELGLDSEE 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1229757995 362 F----LREHKIEGRSGRRFGADAK-YLRISMLSSDDVFQQFLERLSA 403
Cdd:COG0436   336 FaerlLEEAGVAVVPGSAFGPAGEgYVRISYATSEERLEEALERLAR 382
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
81-251 4.29e-09

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 57.70  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  81 WYLLPELEEAIRRLHRVVGNAVVD-ERHVVVGTGSTQLFQAALYALSTPAAaaaapqpiNVVSAAPYYSCYPD------- 152
Cdd:pfam00155  38 TDGHPELREALAKFLGRSPVLKLDrEAAVVFGSGAGANIEALIFLLANPGD--------AILVPAPTYASYIRiarlagg 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 153 ETD-YLCSRLYKWAGDANQYDS--KSGPFIEVVTSPNNPDGC------LRE--PVVEAHGqGKLIHDLAY---YWPQFTP 218
Cdd:pfam00155 110 EVVrYPLYDSNDFHLDFDALEAalKEKPKVVLHTSPHNPTGTvatleeLEKllDLAKEHN-ILLLVDEAYagfVFGSPDA 188
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1229757995 219 ITR-----PADHDLMYFTFSKCTGHAGSRIGWALVKDR 251
Cdd:pfam00155 189 VATrallaEGPNLLVVGSFSKAFGLAGWRVGYILGNAA 226
GntC_guanitoxin NF041364
guanitoxin biosynthesis PLP-dependent (S)-gamma-hydroxy-L-arginine cyclodehydratase GntC;
84-403 3.49e-08

guanitoxin biosynthesis PLP-dependent (S)-gamma-hydroxy-L-arginine cyclodehydratase GntC;


Pssm-ID: 469255  Cd Length: 354  Bit Score: 55.04  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  84 LPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLFQAALYALSTPAAaaaapqpiNVVSAAPYYSCYPDETDYLCSRLYK 163
Cdd:NF041364   39 SLELREAIAALYKDGYGIEVSPDQVLVTTGASEALFLYFHALLEPGD--------EVVVPVPAFQSLYEVPELLGGRVRP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 164 WA-GDANQydsKSGPFIE-------------VVTSPNNPDGC-LREPVVEA-------HGqGKLIHDLAYywpQFTPITR 221
Cdd:NF041364  111 LPlSPENQ---GFRPDLEalrslitprtraiVINSPNNPTGAvMTEAELEAileiasrHG-LIVLADEHY---RFLPYDD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 222 PADHDLMYF-----------TFSKCTGHAGSRIGWaLVKDREVAIKMTKYMDLSSIGVSKDSQFRAAkimELLCNNYDQK 290
Cdd:NF041364  184 GKHVSPSLYpglservialgSFSKTYGMTGLRVGW-LIGPKELIGAILKFKDYTTHCAPSISQYAAL---EALEQGPQER 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 291 L-GSNFSNnffeygKSLMAERWKSLRDVIG-----RSDVFSLPtfeqqyccffgRLSQSYPAFAWlrCKEEIEDCGSFLR 364
Cdd:NF041364  260 VkGWVREN------VRRRDALVERLERLIGwvcepEGGFYAFP-----------KLKDGLPSAAF--AEELLEKAGVVVL 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1229757995 365 EHKIEGRSGRRfgadakYLRISMLSSDDVFQQFLERLSA 403
Cdd:NF041364  321 PGSAFGRPGEG------YFRIGFANSPTRLKEALERLSR 353
hisC TIGR01141
histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; ...
86-259 1.96e-05

histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; imidazole acetol-phosphate transaminase Histidinol-phosphate aminotransferase is a pyridoxal-phosphate dependent enzyme. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273467  Cd Length: 350  Bit Score: 46.11  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  86 ELEEAIRRLHRV---VGNAV---------VDERHVVVGTGSTQLFQAALYALSTPAaaaaapqpINVVSAAPYYSCYPDE 153
Cdd:TIGR01141  41 ALRAELKKLHRYpdpDPAELkqaladyygVDPEQILLGNGSDEIIDLLIRAFLEPG--------DAVLVPPPTYSMYEIS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 154 TDYL--CSRLYKWAGDaNQYD-------SKSGPFIEVVTSPNNPDG-CLREPVVEA-----HGQGKLIHDLAYY----WP 214
Cdd:TIGR01141 113 AKIHgaEVVKVPLDED-GQLDledilvaIDDKPKLVFLCSPNNPTGnLFSRGDIEAvlertPGDALVVVDEAYGefsgEP 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1229757995 215 QFTPITRPADHDLMYFTFSKCTGHAGSRIGWALVKDrEVAIKMTK 259
Cdd:TIGR01141 192 STLPLLAEYPNLIVLRTLSKAFGLAGLRIGYAIANA-EIIDALNK 235
PRK05166 PRK05166
histidinol-phosphate transaminase;
175-259 1.40e-03

histidinol-phosphate transaminase;


Pssm-ID: 179950  Cd Length: 371  Bit Score: 40.51  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 175 SGPFIEVVTSPNNPDGCLREP-----VVEAHGQGKLIH-DLAYY-------WPQFTPITRPADHDLMYF-TFSKCTGHAG 240
Cdd:PRK05166  158 RAPRMLMFSNPSNPVGSWLTAdqlarVLDATPPETLIVvDEAYAeyaagddYPSALTLLKARGLPWIVLrTFSKAYGLAG 237
                          90
                  ....*....|....*....
gi 1229757995 241 SRIGWALVKDREVAIKMTK 259
Cdd:PRK05166  238 LRVGYGLVSDPELVGLLDR 256
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
85-401 1.55e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 40.44  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  85 PELEEAIR-RLHRVVGNAVVDERHVVVGTGSTQLFQAALYALSTPAAaaaapqpiNVVSAAPYY----------SCYPD- 152
Cdd:PRK05957   68 PPLLEAITqKLQQDNGIELNNEQAIVVTAGSNMAFMNAILAITDPGD--------EIILNTPYYfnhemaitmaGCQPIl 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 153 -ETDylcsrlykwagdaNQYDSKSGpFIE---------VVT-SPNNPDGC------LREpVVEAHGQGKL--IHDLAYYW 213
Cdd:PRK05957  140 vPTD-------------DNYQLQPE-AIEqaitpktraIVTiSPNNPTGVvypealLRA-VNQICAEHGIyhISDEAYEY 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 214 ------PQFTPITRP--ADHDLMYFTFSKCTGHAGSRIGWALVKDR-EVAIKmtKYMDLSSIGVSKDSQFRAAKIMellc 284
Cdd:PRK05957  205 ftydgvKHFSPGSIPgsGNHTISLYSLSKAYGFASWRIGYMVIPIHlLEAIK--KIQDTILICPPVVSQYAALGAL---- 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 285 nnydqKLGSNFSNnffEYGKSLMAER---WKSLRDVigrSDVFSLPTFEQQYCCFFgRLSQSYPAFAWLRckeeiedcgS 361
Cdd:PRK05957  279 -----QVGKSYCQ---QHLPEIAQVRqilLKSLGQL---QDRCTLHPANGAFYCFL-KVNTDLNDFELVK---------Q 337
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1229757995 362 FLREHKIEGRSGRRFGADAK-YLRIS--MLSSDDVFQQFlERL 401
Cdd:PRK05957  338 LIREYRVAVIPGTTFGMKNGcYLRIAygALQKATAKEGI-ERL 379
PRK05764 PRK05764
aspartate aminotransferase; Provisional
84-277 1.66e-03

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 40.49  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995  84 LPELEEAIRRLHRVVGNAVVDERHVVVGTGSTQLFQAALYALstpaaaaaapqpIN----VVSAAPYYSCYPD------- 152
Cdd:PRK05764   70 IPELREAIAAKLKRDNGLDYDPSQVIVTTGAKQALYNAFMAL------------LDpgdeVIIPAPYWVSYPEmvklagg 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 153 ---------ETDylcsrlYKWAGDAnqydsksgpfIE----------VVTSPNNPDG---------CLREpVVEAHGqgk 204
Cdd:PRK05764  138 vpvfvptgeENG------FKLTVEQ----------LEaaitpktkalILNSPSNPTGavyspeeleAIAD-VAVEHD--- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229757995 205 LI-------HDLAYYWPQFTPITRPADhDLMYFT-----FSKCTGHAGSRIGWAlVKDREVAIKMTKYMDLSSIGVSKDS 272
Cdd:PRK05764  198 IWvlsdeiyEKLVYDGAEFTSIASLSP-ELRDRTitvngFSKAYAMTGWRLGYA-AGPKELIKAMSKLQSHSTSNPTSIA 275

                  ....*
gi 1229757995 273 QfRAA 277
Cdd:PRK05764  276 Q-YAA 279
 
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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