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Conserved domains on  [gi|2264344907|gb|UTB60179|]
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D-amino acid aminotransferase, partial [Staphylococcus lugdunensis]

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

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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, ...
 1-138 2.82e-79

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: 235.02  E-value: 2.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:TIGR01121  29 VYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNLNTGHVYFQVTRGVAPRNHQFPAGTVKP 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2264344907  81 VITAFAKSYDRPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:TIGR01121 109 VITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGAYEA 166
 
Name Accession Description Interval E-value
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 1-138 2.82e-79

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: 235.02  E-value: 2.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:TIGR01121  29 VYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNLNTGHVYFQVTRGVAPRNHQFPAGTVKP 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2264344907  81 VITAFAKSYDRPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:TIGR01121 109 VITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGAYEA 166
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 1-138 7.93e-54

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: 170.09  E-value: 7.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPeVKP 80
Cdd:cd01558    27 VYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGGEGDVYIQVTRGVGPRGHDFPKC-VKP 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2264344907  81 VITAFAKSYDRPYEEL-QNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:cd01558   106 TVVIITQPLPLPPAELlEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAGADEA 164
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 1-138 7.01e-46

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 150.08  E-value: 7.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:PRK06680   32 IYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVREGLVYLQVTRGVARRDHVFPAADVKP 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907  81 --VITAFAKSYDRPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:PRK06680  112 svVVFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEAGAQEA 171
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 1-138 9.19e-42

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: 139.55  E-value: 9.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHsfPTPEVKP 80
Cdd:COG0115    30 VFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGLEDGYIRPQVTRGVGGRGV--FAEEYEP 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2264344907  81 VITAFAKSYDRPYEEL-QNGVSAVTVEDIRW---LRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:COG0115   108 TVIIIASPLPAYPAEAyEKGVRVITSPYRRAapgGLGGIKTGNYLNNVLAKQEAKEAGADEA 169
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 1-138 7.83e-22

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: 86.64  E-value: 7.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:pfam01063   2 VFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGLPTSDPTLAI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2264344907  81 VITAFAKSydrPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:pfam01063  82 FVSALPPP---PESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDA 136
 
Name Accession Description Interval E-value
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 1-138 2.82e-79

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: 235.02  E-value: 2.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:TIGR01121  29 VYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNLNTGHVYFQVTRGVAPRNHQFPAGTVKP 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2264344907  81 VITAFAKSYDRPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:TIGR01121 109 VITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGAYEA 166
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 1-138 7.93e-54

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: 170.09  E-value: 7.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPeVKP 80
Cdd:cd01558    27 VYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGGEGDVYIQVTRGVGPRGHDFPKC-VKP 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2264344907  81 VITAFAKSYDRPYEEL-QNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:cd01558   106 TVVIITQPLPLPPAELlEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAGADEA 164
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 1-138 7.01e-46

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 150.08  E-value: 7.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:PRK06680   32 IYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVREGLVYLQVTRGVARRDHVFPAADVKP 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907  81 --VITAFAKSYDRPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:PRK06680  112 svVVFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEAGAQEA 171
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 1-138 9.19e-42

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: 139.55  E-value: 9.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHsfPTPEVKP 80
Cdd:COG0115    30 VFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGLEDGYIRPQVTRGVGGRGV--FAEEYEP 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2264344907  81 VITAFAKSYDRPYEEL-QNGVSAVTVEDIRW---LRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:COG0115   108 TVIIIASPLPAYPAEAyEKGVRVITSPYRRAapgGLGGIKTGNYLNNVLAKQEAKEAGADEA 169
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 1-138 6.77e-40

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: 133.88  E-value: 6.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPtPEVKP 80
Cdd:cd00449    10 VFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPLLTRGVGGLGVAPP-PSPEP 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2264344907  81 VITAFAKSYDRPYEELQNGVSAVTVEDIR----WLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:cd00449    89 TFVVFASPVGAYAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEA 150
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 1-138 3.54e-35

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 122.82  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQI-ETGGIYIQATRGVSPRNHSFpTPEVK 79
Cdd:PRK12400   36 VYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFhEDGTIYLQVSRGVQARTHTF-SYDVP 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2264344907  80 PVITAFAKSYDRPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:PRK12400  115 PTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNILAATKAERKGCKEA 173
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 1-138 7.83e-22

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: 86.64  E-value: 7.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSFPTPEVKP 80
Cdd:pfam01063   2 VFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGLPTSDPTLAI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2264344907  81 VITAFAKSydrPYEELQNGVSAVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:pfam01063  82 FVSALPPP---PESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDA 136
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 1-138 1.85e-19

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 81.46  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGV-----SPRNHSfpt 75
Cdd:PRK08320   32 VFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNNLRDAYIRLVVSRGVgdlglDPRKCP--- 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2264344907  76 pevKPVITAFAKSYDRPYEEL-QNGVSAVTVEdIRWLRCD-----IKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:PRK08320  109 ---KPTVVCIAEPIGLYPGELyEKGLKVITVS-TRRNRPDalspqVKSLNYLNNILAKIEANLAGVDEA 173
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 1-138 5.16e-19

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: 79.66  E-value: 5.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGkTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHSfPTPEVKP 80
Cdd:cd01559    10 VFETMRALDGRLFLLDAHLARLERSARRLGIPEP-DLPRLRAALESLLAANDIDEGRIRLILSRGPGGRGYA-PSVCPGP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2264344907  81 VITAFAKSYdrPYEELQNGVSAVTVE---DIRWLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:cd01559    88 ALYVSVIPL--PPAWRQDGVRLITCPvrlGEQPLLAGLKHLNYLENVLAKREARDRGADEA 146
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
1-138 3.21e-13

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 64.59  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATR-----GVSPRNHSFPT 75
Cdd:PRK12479   33 VFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNEYADAYIRLIVSRgkgdlGLDPRSCVKPS 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2264344907  76 pevkpVITAFAKSYDRPYEELQNGVSAVTVEDIR----WLRCDIKSLNLLGNVLAKEYAVKYNATEA 138
Cdd:PRK12479  113 -----VIIIAEQLKLFPQEFYDNGLSVVSVASRRntpdALDPRIKSMNYLNNVLVKIEAAQAGVLEA 174
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 1-127 4.76e-08

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 49.97  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRGVSPRNHsFPTPEVKP 80
Cdd:PRK07650   29 VFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNGLENAYVRFNVSAGIGEIGL-QTEMYEEP 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2264344907  81 VITAFAKSYDRPYEELQN-GVSAVTVE-----DIRwlrcdIKSLNLLGNVLAK 127
Cdd:PRK07650  108 TVIVYMKPLAPPGLPAEKeGVVLKQRRntpegAFR-----LKSHHYLNNILGK 155
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 1-52 2.58e-07

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: 47.96  E-value: 2.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2264344907   1 IYEYIRAYKGK-----LFTVEEHFDRFLRSADEIGLDlGKTKEELIDITRQLLKENQ 52
Cdd:cd01557    15 VFEGLKAYRTPdgkivLFRPDENAERLNRSARRLGLP-PFSVEEFIDAIKELVKLDA 70
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 1-65 3.18e-07

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 47.66  E-value: 3.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2264344907   1 IYEYIRAYKGKLFTVEEHFDRFLRSADEIGLDLGKTKEELIDITRQLLKENQIETGGIYIQATRG 65
Cdd:PRK07544   38 VFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANGLTDAYVRPVAWRG 102
 
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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