NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2592117350|ref|WP_316002336|]
View 

aminotransferase class IV, partial [Listeria monocytogenes]

Protein Classification

aminotransferase class IV( domain architecture ID 1051)

aminotransferase class IV is a pyridoxaL 5'-phosphate dependent enzyme (PLPDE), similar to Staphylococcus D-alanine aminotransferase

Gene Ontology:  GO:0030170
PubMed:  31989227

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLPDE_IV super family cl00224
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 2-127 5.72e-80

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


The actual alignment was detected with superfamily member TIGR01121:

Pssm-ID: 444764  Cd Length: 276  Bit Score: 236.17  E-value: 5.72e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   2 EGGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITR 81
Cdd:TIGR01121 126 KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITR 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2592117350  82 QVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:TIGR01121 206 MVILACAEENGIPVKEEPFTKEELLNADEVFVSSTTAEITPVIEID 251
 
Name Accession Description Interval E-value
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 2-127 5.72e-80

D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130191  Cd Length: 276  Bit Score: 236.17  E-value: 5.72e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   2 EGGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITR 81
Cdd:TIGR01121 126 KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITR 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2592117350  82 QVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:TIGR01121 206 MVILACAEENGIPVKEEPFTKEELLNADEVFVSSTTAEITPVIEID 251
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 3-127 7.79e-64

D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.


Pssm-ID: 238799 [Multi-domain]  Cd Length: 270  Bit Score: 195.12  E-value: 7.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   3 GGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILNGITR 81
Cdd:cd01558   125 GVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAGADEAILLDADgLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITR 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2592117350  82 QVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:cd01558   205 ATVIELAKELGIPVEERPFSLEELYTADEVFLTSTTAEVMPVVEID 250
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 2-127 5.30e-54

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 170.37  E-value: 5.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   2 EGGSAITEEDVRW---LRCDIKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILN 77
Cdd:COG0115   126 KGVRVITSPYRRAapgGLGGIKTGNYLNNVLAKQEAKEAGADEALLLDTDgYVAEGSGSNVFIVKDGVLVTPPLSGGILP 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2592117350  78 GITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:COG0115   206 GITRDSVIELARELGIPVEERPISLEELYTADEVFLTGTAAEVTPVTEID 255
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 3-127 4.09e-47

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 153.25  E-value: 4.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   3 GGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQ 82
Cdd:PRK12400  134 GVRAISEPDTRWLRCDIKSLNLLPNILAATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQ 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2592117350  83 VIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK12400  214 YVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLD 258
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 11-126 3.58e-36

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 123.24  E-value: 3.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  11 DVRWLRCDIKSLNLLGNILAKNKAHQQNALEAIL-HRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAK 89
Cdd:pfam01063 105 NPPSPLPGAKTLNYLENVLARREAKAQGADDALLlDEDGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAK 184

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2592117350  90 KNGIPVKEADFTLTDLREADEVFISSTTIEITPITHI 126
Cdd:pfam01063 185 ALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 2-127 5.72e-80

D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130191  Cd Length: 276  Bit Score: 236.17  E-value: 5.72e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   2 EGGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITR 81
Cdd:TIGR01121 126 KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITR 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2592117350  82 QVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:TIGR01121 206 MVILACAEENGIPVKEEPFTKEELLNADEVFVSSTTAEITPVIEID 251
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 3-127 7.79e-64

D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.


Pssm-ID: 238799 [Multi-domain]  Cd Length: 270  Bit Score: 195.12  E-value: 7.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   3 GGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILNGITR 81
Cdd:cd01558   125 GVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAGADEAILLDADgLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITR 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2592117350  82 QVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:cd01558   205 ATVIELAKELGIPVEERPFSLEELYTADEVFLTSTTAEVMPVVEID 250
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 2-127 5.30e-54

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 170.37  E-value: 5.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   2 EGGSAITEEDVRW---LRCDIKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILN 77
Cdd:COG0115   126 KGVRVITSPYRRAapgGLGGIKTGNYLNNVLAKQEAKEAGADEALLLDTDgYVAEGSGSNVFIVKDGVLVTPPLSGGILP 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2592117350  78 GITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:COG0115   206 GITRDSVIELARELGIPVEERPISLEELYTADEVFLTGTAAEVTPVTEID 255
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 3-127 5.14e-50

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


Pssm-ID: 238254 [Multi-domain]  Cd Length: 256  Bit Score: 159.30  E-value: 5.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   3 GGSAITEEDVR----WLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILN 77
Cdd:cd00449   107 GVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNgYVTEGSASNVFIVKDGELVTPPLDGGILP 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2592117350  78 GITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:cd00449   187 GITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEID 236
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 3-127 4.09e-47

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 153.25  E-value: 4.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   3 GGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQ 82
Cdd:PRK12400  134 GVRAISEPDTRWLRCDIKSLNLLPNILAATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQ 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2592117350  83 VIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK12400  214 YVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLD 258
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 2-127 2.11e-46

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 151.24  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350   2 EGGSAITEEDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGEQVTECSASNVSII-KDGVLWTHAADNLILNGIT 80
Cdd:PRK06680  131 TGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEAGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGIT 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2592117350  81 RQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK06680  211 RHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAASSFVFPVVQID 257
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 11-126 3.58e-36

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 123.24  E-value: 3.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  11 DVRWLRCDIKSLNLLGNILAKNKAHQQNALEAIL-HRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAK 89
Cdd:pfam01063 105 NPPSPLPGAKTLNYLENVLARREAKAQGADDALLlDEDGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAK 184

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2592117350  90 KNGIPVKEADFTLTDLREADEVFISSTTIEITPITHI 126
Cdd:pfam01063 185 ALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 19-127 5.62e-36

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 124.21  E-value: 5.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAIL--HRGEqVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVK 96
Cdd:PRK08320  150 VKSLNYLNNILAKIEANLAGVDEAIMlnDEGY-VAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVR 228

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2592117350  97 EADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK08320  229 EELFTLHDLYTADEVFLTGTAAEVIPVVKVD 259
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 19-127 4.55e-29

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 105.47  E-value: 4.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKE 97
Cdd:cd01559   123 LKHLNYLENVLAKREARDRGADEALFLDTDgRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDE 202

                          90       100       110
                  ....*....|....*....|....*....|
gi 2592117350  98 ADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:cd01559   203 RPLRLEDLLAADEAFLTNSLLGVAPVTAID 232
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 23-127 4.87e-27

BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.


Pssm-ID: 238798  Cd Length: 279  Bit Score: 100.73  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  23 NLLGNILAKNKAHQQNALEAIL--HRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADF 100
Cdd:cd01557   145 NYAASLLAQKEAAEKGYDQALWldGAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPI 224

                          90       100
                  ....*....|....*....|....*..
gi 2592117350 101 TLTDLREADEVFISSTTIEITPITHID 127
Cdd:cd01557   225 TRDELYEADEVFATGTAAVVTPVGEID 251
PRK06606 PRK06606
branched-chain amino acid transaminase;
23-127 9.27e-27

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 100.61  E-value: 9.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  23 NLLGNILAKNKAHQQNALEAIL--HRGeQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADF 100
Cdd:PRK06606  163 NYLNSILAKTEARRNGYDEALLldVEG-YVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRI 241

                          90       100
                  ....*....|....*....|....*..
gi 2592117350 101 TLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK06606  242 TRDELYIADEVFFTGTAAEVTPIREVD 268
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 19-127 2.16e-25

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 96.57  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAI-LHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKE 97
Cdd:PRK07650  143 LKSHHYLNNILGKREIGNDPNKEGIfLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKE 222

                          90       100       110
                  ....*....|....*....|....*....|
gi 2592117350  98 ADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK07650  223 GFYTKEELLSADEVFVTNSIQEIVPLTRIE 252
ilvE_I TIGR01122
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ...
 19-127 1.18e-23

branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family more strongly similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130192  Cd Length: 298  Bit Score: 92.42  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNL-LGNILAKNKAHQQNALEAI-LHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVK 96
Cdd:TIGR01122 150 AKAGGNyLNSLLAKSEARRHGYDEAIlLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVV 229

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2592117350  97 EADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:TIGR01122 230 EQPISREELYTADEAFFTGTAAEITPIREVD 260
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
19-127 4.71e-23

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 90.78  E-value: 4.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEA-ILHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKE 97
Cdd:PRK12479  151 IKSMNYLNNVLVKIEAAQAGVLEAlMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEE 230

                          90       100       110
                  ....*....|....*....|....*....|
gi 2592117350  98 ADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK12479  231 RPFTRHDVYVADEVFLTGTAAELIPVVKVD 260
pabC_Proteo TIGR03461
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ...
 19-127 5.09e-20

aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 132501  Cd Length: 261  Bit Score: 82.25  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAI-LHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKE 97
Cdd:TIGR03461 137 IKHLNRLEQVLIKAELENSEADEALvLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEE 216

                          90       100       110
                  ....*....|....*....|....*....|
gi 2592117350  98 ADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:TIGR03461 217 VKAGLEELLSADEVFITNSLMGVVPVNAIG 246
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 29-126 1.02e-18

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 79.25  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  29 LAKNKAHQQNALEAIL--HRGeQVTECSASNVSIIKDGVLWTHAADnLILNGITRQVIIDVAKKNGIPVKEADFTLTDLR 106
Cdd:PRK07544  167 ISKHAAEAKGYADALMldYRG-YVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTVIELAKRRGIEVVERHIMPEELA 244

                          90       100
                  ....*....|....*....|
gi 2592117350 107 EADEVFISSTTIEITPITHI 126
Cdd:PRK07544  245 GFSECFLTGTAAEVTPVSEI 264
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
50-127 4.99e-18

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 77.30  E-value: 4.99e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2592117350  50 VTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PRK13356  184 VAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFD 261
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 19-126 1.30e-17

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 75.65  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAI-LHRGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKE 97
Cdd:PRK06092  139 IKHLNRLEQVLIRAELEQTEADEALvLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVE 218

                          90       100
                  ....*....|....*....|....*....
gi 2592117350  98 ADFTLTDLREADEVFISSTTIEITPITHI 126
Cdd:PRK06092  219 VDASLEELLQADEVFICNSLMPVWPVRAI 247
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
 48-126 4.88e-15

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 69.88  E-value: 4.88e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2592117350  48 EQVTECsasNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHI 126
Cdd:PLN02782  284 EEVSSC---NIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSI 359
PRK07849 PRK07849
aminodeoxychorismate lyase;
10-127 6.45e-14

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 66.14  E-value: 6.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  10 EDVRWLRCDIKSLNLLGNILAKNKAHQQNALEAILHRGE-QVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVA 88
Cdd:PRK07849  149 ERAPWLLAGAKTLSYAVNMAALRYAARRGADDVIFTSTDgYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVA 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2592117350  89 KKNGIPVKEADFTLTDLREADEVF-ISSTTIeITPITHID 127
Cdd:PRK07849  229 REKGWDCEYRALRPADLFAADGVWlVSSVRL-AARVHTLD 267
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 47-123 1.10e-10

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 57.25  E-value: 1.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2592117350  47 GEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPI 123
Cdd:PLN03117  229 GKNIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 305
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
 19-126 2.04e-10

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 56.65  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAILH----RGEQVTECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIP 94
Cdd:PLN02883  230 VKAISNYGPVLEVMRRAKSRGFSDVLYldadTGKNIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYK 309

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2592117350  95 VKEADFTLTDLREADEVFISSTTIEITPITHI 126
Cdd:PLN02883  310 VEERRVPVEELKEAEEVFCTGTAAGVASVGSI 341
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 19-127 2.73e-09

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 53.48  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592117350  19 IKSLNLLGNILAKNKAHQQNALEAILHRGEQ-VTECSASNVSII-KDGVLWTHAADNlILNGITRQVIIDVAK---KNGI 93
Cdd:PLN02845  184 VKSVNYLPNALSQMEAEERGAFAGIWLDEEGfVAEGPNMNVAFLtNDGELVLPPFDK-ILSGCTARRVLELAPrlvSPGD 262

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2592117350  94 --PVKEADFTLTDLREADEVFISSTTIEITPITHID 127
Cdd:PLN02845  263 lrGVKQRKISVEEAKAADEMMLIGSGVPVLPIVSWD 298
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
 52-126 8.23e-09

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 52.03  E-value: 8.23e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2592117350  52 ECSASNVSIIKDGVLWTHAADNLILNGITRQVIIDVAKKNGIPVKEADFTLTDLREADEVFISSTTIEITPITHI 126
Cdd:PLN02259  271 EASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTI 345
PRK07101 PRK07101
hypothetical protein; Provisional
 34-111 2.06e-04

hypothetical protein; Provisional


Pssm-ID: 235934  Cd Length: 187  Bit Score: 39.15  E-value: 2.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2592117350  34 AHQQNALEAILHRGEQVTECSASNVsIIKDGVLWtHAADNLILNGITRQVIIDvakkNGIpVKEADFTLTDLREADEV 111
Cdd:PRK07101  108 AQKGECDEIIIIKNGLVTDTSIGNL-AFFDGKQW-FTPKKPLLKGTQRARLLD----EGK-IKEKDITVEDLLQYEEI 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH