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Conserved domains on  [gi|1176773529|gb|OQY91405|]
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MAG: hypothetical protein B6D38_02015 [Anaerolineae bacterium UTCFX1]

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
IlvE super family cl42528
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
91-208 4.78e-27

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


The actual alignment was detected with superfamily member COG0115:

Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 104.12  E-value: 4.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLV-KNGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITS 167
Cdd:COG0115   168 EALLLdTDGYVAEGSGSNVFIVkdGVL----VTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFLTG 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1176773529 168 SSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAYAAYVEERSE 208
Cdd:COG0115   244 TAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIVRGEAE 284
 
Name Accession Description Interval E-value
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
91-208 4.78e-27

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: 104.12  E-value: 4.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLV-KNGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITS 167
Cdd:COG0115   168 EALLLdTDGYVAEGSGSNVFIVkdGVL----VTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFLTG 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1176773529 168 SSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAYAAYVEERSE 208
Cdd:COG0115   244 TAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIVRGEAE 284
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
88-199 9.82e-23

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: 92.28  E-value: 9.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  88 NIFEALLV-KNGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAF 164
Cdd:cd00449   146 GADEALLLdDNGYVTEGSASNVFIVkdGEL----VTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVF 221
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1176773529 165 ITSSSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAY 199
Cdd:cd00449   222 LTGTAAEVTPVTEIDGRGIGDGKPGPVTRKLRELL 256
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
81-178 7.82e-20

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: 83.56  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  81 RERLTRENIFEALLV-KNGKILEGLTSNFFWIgqIGNLPYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSL 159
Cdd:pfam01063 125 RREAKAQGADDALLLdEDGNVTEGSTSNVFLV--KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQE 202
                          90
                  ....*....|....*....
gi 1176773529 160 AKEAFITSSSRGVVPVVQI 178
Cdd:pfam01063 203 ADEAFLTNSLRGVTPVSSI 221
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
91-199 1.35e-18

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 81.52  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLVKNGKILEGLTSNFFWIGQIGNL---PylatAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITS 167
Cdd:PRK06680  170 EAWMVDDGFVTEGASSNAWIVTKDGKLvtrP----ADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITA 245
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1176773529 168 SSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAY 199
Cdd:PRK06680  246 ASSFVFPVVQIDGKQIGNGKPGPIAKRLREAY 277
 
Name Accession Description Interval E-value
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
91-208 4.78e-27

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: 104.12  E-value: 4.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLV-KNGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITS 167
Cdd:COG0115   168 EALLLdTDGYVAEGSGSNVFIVkdGVL----VTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFLTG 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1176773529 168 SSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAYAAYVEERSE 208
Cdd:COG0115   244 TAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIVRGEAE 284
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
88-199 9.82e-23

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: 92.28  E-value: 9.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  88 NIFEALLV-KNGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAF 164
Cdd:cd00449   146 GADEALLLdDNGYVTEGSASNVFIVkdGEL----VTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVF 221
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1176773529 165 ITSSSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAY 199
Cdd:cd00449   222 LTGTAAEVTPVTEIDGRGIGDGKPGPVTRKLRELL 256
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
90-199 3.60e-20

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: 85.34  E-value: 3.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  90 FEALLVK-NGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFIT 166
Cdd:cd01558   162 DEAILLDaDGLVTEGSSSNVFIVknGVL----VTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1176773529 167 SSSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAY 199
Cdd:cd01558   238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
81-178 7.82e-20

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: 83.56  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  81 RERLTRENIFEALLV-KNGKILEGLTSNFFWIgqIGNLPYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSL 159
Cdd:pfam01063 125 RREAKAQGADDALLLdEDGNVTEGSTSNVFLV--KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQE 202
                          90
                  ....*....|....*....
gi 1176773529 160 AKEAFITSSSRGVVPVVQI 178
Cdd:pfam01063 203 ADEAFLTNSLRGVTPVSSI 221
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
91-199 1.35e-18

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 81.52  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLVKNGKILEGLTSNFFWIGQIGNL---PylatAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITS 167
Cdd:PRK06680  170 EAWMVDDGFVTEGASSNAWIVTKDGKLvtrP----ADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITA 245
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1176773529 168 SSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAY 199
Cdd:PRK06680  246 ASSFVFPVVQIDGKQIGNGKPGPIAKRLREAY 277
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
86-208 2.75e-18

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 80.78  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  86 RENIFealLVKNGKILEGLTSNFFWI-GQIGNLPYLATaqrGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAF 164
Cdd:PRK07650  164 KEGIF---LTEEGYVAEGIVSNLFWVkGDIVYTPSLET---GILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVF 237
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1176773529 165 ITSSSRGVVPVVQIDDaQVGQGMVGVWTKRLSLAYAAYVE---ERSE 208
Cdd:PRK07650  238 VTNSIQEIVPLTRIEE-RDFPGKVGMVTKRLQNLYEMQREklwSRNE 283
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
88-199 3.31e-15

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: 71.57  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  88 NIFEALLVK-NGKILEGLTSNFFWIgqIGNLPYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFIT 166
Cdd:cd01559   142 GADEALFLDtDGRVIEGTASNLFFV--KDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLT 219
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1176773529 167 SSSRGVVPVVQIDDaqvGQGMVGVWTKRLSLAY 199
Cdd:cd01559   220 NSLLGVAPVTAIDD---HDGPPGPLTRALRELL 249
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
85-205 8.73e-12

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 62.58  E-value: 8.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  85 TRENIFealLVKNGKILEgltsnffwigqignlPYLATaqrGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAF 164
Cdd:PRK08320  186 TGDNIF---IVKNGKLIT---------------PPTYA---GALEGITRNAVIEIAKELGIPVREELFTLHDLYTADEVF 244
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1176773529 165 ITSSSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAYAAYVEE 205
Cdd:PRK08320  245 LTGTAAEVIPVVKVDGRVIGDGKPGPITKKLLEEFRELTKK 285
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
85-206 1.47e-10

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 59.20  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  85 TRENIFEALLV-KNGKILEGLTSNFFWI--GQIGNLP-YLataqrGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLA 160
Cdd:PRK12479  167 AQAGVLEALMLnQQGYVCEGSGDNVFVVkdGKVLTPPsYL-----GALEGITRNSVIELCERLSIPCEERPFTRHDVYVA 241
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1176773529 161 KEAFITSSSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAYAAYVEER 206
Cdd:PRK12479  242 DEVFLTGTAAELIPVVKVDSREIGDGKPGSVTKQLTEEFKKLTRER 287
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
91-203 2.86e-10

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: 58.36  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLV--KNGKILEGLTSNFF--WIGQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFIT 166
Cdd:cd01557   163 QALWLdgAHGYVAEVGTMNIFfvKDGEL----ITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1176773529 167 SSSRGVVPVVQID--DAQVGQGMVGVWTKRLSLAYAAYV 203
Cdd:cd01557   239 GTAAVVTPVGEIDyrGKEPGEGEVGPVTKKLYDLLTDIQ 277
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
86-200 4.52e-10

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 57.72  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  86 RENIFEALLVKNGKILEGLTSNFFWIGQiGNLpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFI 165
Cdd:PRK12400  167 RKGCKEALFVRNGTVTEGSHSNFFLIKN-GTL-YTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFF 244
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1176773529 166 TSSSRGVVPVVQIDDAQVGQGMVGVWTKRLSLAYA 200
Cdd:PRK12400  245 TGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFS 279
PRK09266 PRK09266
hypothetical protein; Provisional
91-210 2.13e-08

hypothetical protein; Provisional


Pssm-ID: 236438  Cd Length: 266  Bit Score: 52.68  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EALLV-KNGKILEGLTSNF-FWIGQIGNLPylataQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITSS 168
Cdd:PRK09266  155 DALFVdPDGRVSEGATWNLgFWDGGAVVWP-----QAPALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAGAFACNA 229
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1176773529 169 SRGVVPVVQIDDAQVGQGmvgvwTKRLSLAYAAYVEERSESI 210
Cdd:PRK09266  230 WRGQRAVSAIDDVALPDS-----HALLELLRRAYEAEPWQAI 266
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
91-180 2.80e-07

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 49.45  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  91 EAL-LVKNGKILEGLTSNFFWIGqiGNLPYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITSSS 169
Cdd:PRK06092  161 EALvLDSEGWVIECCAANLFWRK--GGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSL 238
                          90
                  ....*....|.
gi 1176773529 170 RGVVPVVQIDD 180
Cdd:PRK06092  239 MPVWPVRAIGE 249
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
127-208 1.73e-06

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 47.28  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529 127 ILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITSSSRGVVPVVQIDDAQVGqgmVGVWTKRLSLAYAAYVEER 206
Cdd:PRK07544  213 FLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSECFLTGTAAEVTPVSEIGEYRFT---PGAITRDLMDDYEALVRPR 289

                  ..
gi 1176773529 207 SE 208
Cdd:PRK07544  290 AA 291
PRK07849 PRK07849
aminodeoxychorismate lyase;
98-185 2.93e-05

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 43.79  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  98 GKILEGLTSNFFWIgqigNLPYLATAQR--GILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITSSSRGVVPV 175
Cdd:PRK07849  188 GYVLEGPTSTVVIA----TDDRLLTPPPwyGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAARV 263
                          90
                  ....*....|
gi 1176773529 176 VQIDDAQVGQ 185
Cdd:PRK07849  264 HTLDGRPLPR 273
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
97-196 3.40e-05

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 43.46  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  97 NGKILEGLTSNFFWIGQIGNLPYLATAQrgILLGVT--RTM-IIRAARGRGL--EVRFSPLRLDQLSLAKEAFITSSSRG 171
Cdd:PLN02845  213 EGFVAEGPNMNVAFLTNDGELVLPPFDK--ILSGCTarRVLeLAPRLVSPGDlrGVKQRKISVEEAKAADEMMLIGSGVP 290
                          90       100
                  ....*....|....*....|....*
gi 1176773529 172 VVPVVQIDDAQVGQGMVGVWTKRLS 196
Cdd:PLN02845  291 VLPIVSWDGQPIGDGKVGPITLALH 315
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
127-195 3.86e-04

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 40.60  E-value: 3.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176773529 127 ILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITSSSRGVVPVVQI----DDAQVGQGMVGVWTKRL 195
Cdd:PLN02782  308 ILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSItykgKRVSYGEGGFGTVSQQL 380
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
97-201 3.89e-04

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 40.32  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773529  97 NGKILEGLTSNFFWI--GQIgnlpYLATAQRGILLGVTRTMIIRAARGRGLEVRFSPLRLDQLSLAKEAFITSSSRGVVP 174
Cdd:PRK13356  181 LGNVAETATSNVFMVkdGVV----FTPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYSKVVP 256
                          90       100
                  ....*....|....*....|....*..
gi 1176773529 175 VVQIDDAQVGQGMVGVWTKRLSLAYAA 201
Cdd:PRK13356  257 VTRFDDRSLQPGPVTRRARELYWDWAH 283
 
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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