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Conserved domains on  [gi|18410169|ref|NP_567011|]
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D-aminoacid aminotransferase-like PLP-dependent enzymes superfamily protein [Arabidopsis thaliana]

Protein Classification

aminotransferase class IV( domain architecture ID 10087399)

aminotransferase class IV family protein similar to Thermotoga maritima probable branched-chain amino acid aminotransferase IlvE which may catalyze the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
27-339 4.97e-47

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: 160.07  E-value: 4.97e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  27 TGAYTTTRTiNNGTSFlFWERHMKRLSSSIRILlksnpellfssgssprfWMNQPvpgssiYDRVNgsMSEALKSVVVKE 106
Cdd:cd00449   8 DGVFEGLRA-GKGRLF-RLDEHLDRLNRSAKRL-----------------GLPIP------YDREE--LREALKELVAAN 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 107 serlYGEELAVTVLVTGNVEKLNRL-DVGNNWDFLDVWLHIGAYSPLGPLGVgenaaSLALVGRGR-----DVAAAKYSD 180
Cdd:cd00449  61 ----NGASLYIRPLLTRGVGGLGVApPPSPEPTFVVFASPVGAYAKGGEKGV-----RLITSPDRRraapgGTGDAKTGG 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 181 WVRLRKPLEKFRPPLTTELLLSNDGDHLLEGCITNFFVVCRrvkssenlyggslseFEVQTAPITDGVLAGVIRDLVIEV 260
Cdd:cd00449 132 NLNSVLAKQEAAEAGADEALLLDDNGYVTEGSASNVFIVKD---------------GELVTPPLDGGILPGITRDSVIEL 196
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18410169 261 CLSEGIPYRERAPSWSERELWEEAFITSSLRILqhvgtikVPVGsmeglacnkpeEIQWKEKrFKERPGMITELIKKAI 339
Cdd:cd00449 197 AKELGIKVEERPISLDELYAADEVFLTGTAAEV-------TPVT-----------EIDGRGI-GDGKPGPVTRKLRELL 256
 
Name Accession Description Interval E-value
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
27-339 4.97e-47

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: 160.07  E-value: 4.97e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  27 TGAYTTTRTiNNGTSFlFWERHMKRLSSSIRILlksnpellfssgssprfWMNQPvpgssiYDRVNgsMSEALKSVVVKE 106
Cdd:cd00449   8 DGVFEGLRA-GKGRLF-RLDEHLDRLNRSAKRL-----------------GLPIP------YDREE--LREALKELVAAN 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 107 serlYGEELAVTVLVTGNVEKLNRL-DVGNNWDFLDVWLHIGAYSPLGPLGVgenaaSLALVGRGR-----DVAAAKYSD 180
Cdd:cd00449  61 ----NGASLYIRPLLTRGVGGLGVApPPSPEPTFVVFASPVGAYAKGGEKGV-----RLITSPDRRraapgGTGDAKTGG 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 181 WVRLRKPLEKFRPPLTTELLLSNDGDHLLEGCITNFFVVCRrvkssenlyggslseFEVQTAPITDGVLAGVIRDLVIEV 260
Cdd:cd00449 132 NLNSVLAKQEAAEAGADEALLLDDNGYVTEGSASNVFIVKD---------------GELVTPPLDGGILPGITRDSVIEL 196
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18410169 261 CLSEGIPYRERAPSWSERELWEEAFITSSLRILqhvgtikVPVGsmeglacnkpeEIQWKEKrFKERPGMITELIKKAI 339
Cdd:cd00449 197 AKELGIKVEERPISLDELYAADEVFLTGTAAEV-------TPVT-----------EIDGRGI-GDGKPGPVTRKLRELL 256
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
28-291 1.50e-16

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: 77.40  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169    28 GAYTTTRTINNgtSFLFWERHMKRLSSSIRILLKSNPEllfssgsSPRFWMNqpvpgssiydrvngsmseALKSVVVKES 107
Cdd:pfam01063   1 GVFETLRVYNG--KIFFLDEHLARLRRSAKLLGIPLPF-------DEEDLRK------------------IIEELLKANG 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169   108 ERLYGeelaVTVLVTGNVEKLNRLDVGNNWdfldvWLHIGAYSPLGPLGVGENAASLALVGRGRDVAAAK-----YSDWV 182
Cdd:pfam01063  54 LGVGR----LRLTVSRGPGGFGLPTSDPTL-----AIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKtlnylENVLA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169   183 RLRKPLEKFRpplttELLLSNDGDHLLEGCITNFFVVCrrvkssenlyGGslsefEVQTAPITDGVLAGVIRDLVIEVCL 262
Cdd:pfam01063 125 RREAKAQGAD-----DALLLDEDGNVTEGSTSNVFLVK----------GG-----TLYTPPLESGILPGITRQALLDLAK 184
                         250       260
                  ....*....|....*....|....*....
gi 18410169   263 SEGIPYRERAPSWSERELWEEAFITSSLR 291
Cdd:pfam01063 185 ALGLEVEERPITLADLQEADEAFLTNSLR 213
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
5-305 8.26e-16

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: 76.77  E-value: 8.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169   5 RFLYHNGVVLEAPPVTTFLESH-----TGAYTTTRTINNgtSFLFWERHMKRLSSSIRILLksnpellfssgssprfwMN 79
Cdd:COG0115   1 RLIWLNGELVPEEEATISVLDRglhygDGVFEGIRAYDG--RLFRLDEHLARLNRSAKRLG-----------------IP 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  80 QPvpgssiYDRvngsmsEALKSVVVKESERLYGEELAVTVLVTGNVEKLNRLDVGNNWDFldvwlhIGAYSPLGPLGVGE 159
Cdd:COG0115  62 IP------YTE------EELLEAIRELVAANGLEDGYIRPQVTRGVGGRGVFAEEYEPTV------IIIASPLPAYPAEA 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 160 NAASLALV------GRGRDVAAAK---YSDWVRLRKplekfrpplttE---------LLLSNDGdHLLEGCITNFFVVcr 221
Cdd:COG0115 124 YEKGVRVItspyrrAAPGGLGGIKtgnYLNNVLAKQ-----------EakeagadeaLLLDTDG-YVAEGSGSNVFIV-- 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 222 rvkssenlYGGslsefEVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERapSWSERELW--EEAFITSSLRILQHVGTI 299
Cdd:COG0115 190 --------KDG-----VLVTPPLSGGILPGITRDSVIELARELGIPVEER--PISLEELYtaDEVFLTGTAAEVTPVTEI 254

                ....*..
gi 18410169 300 -KVPVGS 305
Cdd:COG0115 255 dGRPIGD 261
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
199-345 1.04e-04

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 43.40  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  199 LLLSNDGdHLLEGCITNFFVVcrrvkssenlyggslSEFEVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERAPSWSER 278
Cdd:PRK12479 175 LMLNQQG-YVCEGSGDNVFVV---------------KDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDV 238
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18410169  279 ELWEEAFITSSLRILqhvgtikVPVGSMEG--LACNKPEEIQwkeKRfkerpgmITELIKKAIMERGIK 345
Cdd:PRK12479 239 YVADEVFLTGTAAEL-------IPVVKVDSreIGDGKPGSVT---KQ-------LTEEFKKLTRERGVR 290
 
Name Accession Description Interval E-value
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
27-339 4.97e-47

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: 160.07  E-value: 4.97e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  27 TGAYTTTRTiNNGTSFlFWERHMKRLSSSIRILlksnpellfssgssprfWMNQPvpgssiYDRVNgsMSEALKSVVVKE 106
Cdd:cd00449   8 DGVFEGLRA-GKGRLF-RLDEHLDRLNRSAKRL-----------------GLPIP------YDREE--LREALKELVAAN 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 107 serlYGEELAVTVLVTGNVEKLNRL-DVGNNWDFLDVWLHIGAYSPLGPLGVgenaaSLALVGRGR-----DVAAAKYSD 180
Cdd:cd00449  61 ----NGASLYIRPLLTRGVGGLGVApPPSPEPTFVVFASPVGAYAKGGEKGV-----RLITSPDRRraapgGTGDAKTGG 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 181 WVRLRKPLEKFRPPLTTELLLSNDGDHLLEGCITNFFVVCRrvkssenlyggslseFEVQTAPITDGVLAGVIRDLVIEV 260
Cdd:cd00449 132 NLNSVLAKQEAAEAGADEALLLDDNGYVTEGSASNVFIVKD---------------GELVTPPLDGGILPGITRDSVIEL 196
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18410169 261 CLSEGIPYRERAPSWSERELWEEAFITSSLRILqhvgtikVPVGsmeglacnkpeEIQWKEKrFKERPGMITELIKKAI 339
Cdd:cd00449 197 AKELGIKVEERPISLDELYAADEVFLTGTAAEV-------TPVT-----------EIDGRGI-GDGKPGPVTRKLRELL 256
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
28-291 1.50e-16

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: 77.40  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169    28 GAYTTTRTINNgtSFLFWERHMKRLSSSIRILLKSNPEllfssgsSPRFWMNqpvpgssiydrvngsmseALKSVVVKES 107
Cdd:pfam01063   1 GVFETLRVYNG--KIFFLDEHLARLRRSAKLLGIPLPF-------DEEDLRK------------------IIEELLKANG 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169   108 ERLYGeelaVTVLVTGNVEKLNRLDVGNNWdfldvWLHIGAYSPLGPLGVGENAASLALVGRGRDVAAAK-----YSDWV 182
Cdd:pfam01063  54 LGVGR----LRLTVSRGPGGFGLPTSDPTL-----AIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKtlnylENVLA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169   183 RLRKPLEKFRpplttELLLSNDGDHLLEGCITNFFVVCrrvkssenlyGGslsefEVQTAPITDGVLAGVIRDLVIEVCL 262
Cdd:pfam01063 125 RREAKAQGAD-----DALLLDEDGNVTEGSTSNVFLVK----------GG-----TLYTPPLESGILPGITRQALLDLAK 184
                         250       260
                  ....*....|....*....|....*....
gi 18410169   263 SEGIPYRERAPSWSERELWEEAFITSSLR 291
Cdd:pfam01063 185 ALGLEVEERPITLADLQEADEAFLTNSLR 213
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
5-305 8.26e-16

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: 76.77  E-value: 8.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169   5 RFLYHNGVVLEAPPVTTFLESH-----TGAYTTTRTINNgtSFLFWERHMKRLSSSIRILLksnpellfssgssprfwMN 79
Cdd:COG0115   1 RLIWLNGELVPEEEATISVLDRglhygDGVFEGIRAYDG--RLFRLDEHLARLNRSAKRLG-----------------IP 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  80 QPvpgssiYDRvngsmsEALKSVVVKESERLYGEELAVTVLVTGNVEKLNRLDVGNNWDFldvwlhIGAYSPLGPLGVGE 159
Cdd:COG0115  62 IP------YTE------EELLEAIRELVAANGLEDGYIRPQVTRGVGGRGVFAEEYEPTV------IIIASPLPAYPAEA 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 160 NAASLALV------GRGRDVAAAK---YSDWVRLRKplekfrpplttE---------LLLSNDGdHLLEGCITNFFVVcr 221
Cdd:COG0115 124 YEKGVRVItspyrrAAPGGLGGIKtgnYLNNVLAKQ-----------EakeagadeaLLLDTDG-YVAEGSGSNVFIV-- 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 222 rvkssenlYGGslsefEVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERapSWSERELW--EEAFITSSLRILQHVGTI 299
Cdd:COG0115 190 --------KDG-----VLVTPPLSGGILPGITRDSVIELARELGIPVEER--PISLEELYtaDEVFLTGTAAEVTPVTEI 254

                ....*..
gi 18410169 300 -KVPVGS 305
Cdd:COG0115 255 dGRPIGD 261
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
199-299 1.07e-08

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: 55.39  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 199 LLLSNDGdHLLEGCITNFFVVcrrvkssenlYGGslsefEVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERAPSWSER 278
Cdd:cd01559 147 LFLDTDG-RVIEGTASNLFFV----------KDG-----ELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDL 210
                        90       100
                ....*....|....*....|.
gi 18410169 279 ELWEEAFITSSLRILQHVGTI 299
Cdd:cd01559 211 LAADEAFLTNSLLGVAPVTAI 231
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
198-314 1.33e-06

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: 49.13  E-value: 1.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 198 ELLLSNDGDHLLEGCITNFFVVCRRVkssenlyggslsefeVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERapSWSE 277
Cdd:cd01558 163 EAILLDADGLVTEGSSSNVFIVKNGV---------------LVTPPLDNGILPGITRATVIELAKELGIPVEER--PFSL 225
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18410169 278 RELWE--EAFITSSLRILQHVGTIKvpvGSMEGLACNKP 314
Cdd:cd01558 226 EELYTadEVFLTSTTAEVMPVVEID---GRPIGDGKPGP 261
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
199-347 3.41e-05

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: 44.88  E-value: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169 199 LLLSNDGDHLLEGCITNFFVVcrrvkssenlYGGslsefEVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERAPSWSER 278
Cdd:cd01557 165 LWLDGAHGYVAEVGTMNIFFV----------KDG-----ELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDEL 229
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18410169 279 ELWEEAFITsslrilqhvGT--IKVPVGsmeglacnkpeEIQWKEKRFK-ERPGMITELIKKAIMerGIKEG 347
Cdd:cd01557 230 YEADEVFAT---------GTaaVVTPVG-----------EIDYRGKEPGeGEVGPVTKKLYDLLT--DIQYG 279
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
199-345 1.04e-04

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 43.40  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  199 LLLSNDGdHLLEGCITNFFVVcrrvkssenlyggslSEFEVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERAPSWSER 278
Cdd:PRK12479 175 LMLNQQG-YVCEGSGDNVFVV---------------KDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDV 238
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18410169  279 ELWEEAFITSSLRILqhvgtikVPVGSMEG--LACNKPEEIQwkeKRfkerpgmITELIKKAIMERGIK 345
Cdd:PRK12479 239 YVADEVFLTGTAAEL-------IPVVKVDSreIGDGKPGSVT---KQ-------LTEEFKKLTRERGVR 290
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
204-308 2.80e-04

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 42.22  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  204 DGdHLLEGCITNFFVVCRRVKssenlyggslsefeVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERAPSWSERELWEE 283
Cdd:PRK06680 176 DG-FVTEGASSNAWIVTKDGK--------------LVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAARE 240
                         90       100
                 ....*....|....*....|....*
gi 18410169  284 AFITSSlrilqhvGTIKVPVGSMEG 308
Cdd:PRK06680 241 AFITAA-------SSFVFPVVQIDG 258
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
201-308 7.58e-03

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 37.64  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410169  201 LSNDGdHLLEGCITNFFVVCRRVkssenlyggslsefeVQTAPITDGVLAGVIRDLVIEVCLSEGIPYRERAPSWSEREL 280
Cdd:PRK07650 169 LTEEG-YVAEGIVSNLFWVKGDI---------------VYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLS 232
                         90       100
                 ....*....|....*....|....*...
gi 18410169  281 WEEAFITSSlriLQHVgtikVPVGSMEG 308
Cdd:PRK07650 233 ADEVFVTNS---IQEI----VPLTRIEE 253
 
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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