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Conserved domains on  [gi|1958649257|ref|XP_038945432|]
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branched-chain-amino-acid aminotransferase, mitochondrial isoform X1 [Rattus norvegicus]

Protein Classification

branched-chain amino acid aminotransferase( domain architecture ID 10107512)

branched-chain amino acid 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 103-398 9.73e-127

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: 366.91  E-value: 9.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 103 TLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTS 182
Cdd:cd01557     1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 183 LYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGdSMTPVSLLADpSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQK 262
Cdd:cd01557    81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 263 KGCEQVLWLYGPDHQLTEVGTMNIFVYWtheDGelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRA 342
Cdd:cd01557   159 KGYDQALWLDGAHGYVAEVGTMNIFFVK---DG--ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649257 343 LeegrvrEVFGSGTACQVCPVHQILYEGKQlhiPTMENGPELILRFQKELKAIQYG 398
Cdd:cd01557   233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
 
Name Accession Description Interval E-value
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 103-398 9.73e-127

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: 366.91  E-value: 9.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 103 TLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTS 182
Cdd:cd01557     1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 183 LYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGdSMTPVSLLADpSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQK 262
Cdd:cd01557    81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 263 KGCEQVLWLYGPDHQLTEVGTMNIFVYWtheDGelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRA 342
Cdd:cd01557   159 KGYDQALWLDGAHGYVAEVGTMNIFFVK---DG--ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649257 343 LeegrvrEVFGSGTACQVCPVHQILYEGKQlhiPTMENGPELILRFQKELKAIQYG 398
Cdd:cd01557   233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
 57-408 3.06e-124

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 363.31  E-value: 3.06e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  57 TREPQKKPAPSQPLlFGKTFTDHMLMVEWnSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRP 136
Cdd:PRK13357   10 TSDEKRAIDWANLG-FGYVFTDHMVVIDY-KDGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 137 WLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWV-PDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGS 215
Cdd:PRK13357   88 DANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 216 YFPGDsMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWLYGPDHQ-LTEVGTMNIF-VYwthE 293
Cdd:PRK13357  168 YFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFfIT---K 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 294 DGELelaTPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQL 373
Cdd:PRK13357  244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958649257 374 HIPTMENGPeLILRFQKELKAIQYGTSA--HDWMLRV 408
Cdd:PRK13357  320 VIGDGEVGP-VTQKLYDELTGIQFGDVEdpHGWIVKV 355
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
 91-408 3.40e-97

branched-chain amino acid aminotransferase, group II; 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 less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 233278  Cd Length: 313  Bit Score: 292.82  E-value: 3.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  91 WGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEV 170
Cdd:TIGR01123   1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 171 DKDWVPD-GNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSmTPVSLLADPSFVRAWIGGVGDCKLGGN 249
Cdd:TIGR01123  81 NKDWVPPyGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 250 YGPTVAVQQEAQKKGCEQVLWLYGPDHQ-LTEVGTMNIF-VYwthedGELELATPPLDGIILPGVVRQSLLDLARTWGeF 327
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTyIEEVGAMNFFfIT-----GDGELVTPPLSGSILPGITRDSLLQLAKDLG-M 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 328 RVAERKVTMKELKRALEEGrvREVFGSGTACQVCPVHQILYEGKQLHIPTMENGpELILRFQKELKAIQYGTSA--HDWM 405
Cdd:TIGR01123 234 EVEERRIDIDELKAFVEAG--EIVFACGTAAVITPVGEIQHGGKEVVFASGQPG-EVTKALYDELTDIQYGDFEdpYGWI 310


                  ...
gi 1958649257 406 LRV 408
Cdd:TIGR01123 311 VEV 313
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 91-401 2.86e-70

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: 222.76  E-value: 2.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  91 WGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGrdkqvRLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIE 169
Cdd:COG0115     4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 170 VDKDwvpdgngTSLYVRPVLIGNEPSLGVGMVT-QALLFVILCPVGSYFPGDSMTPVSLLADPsFVRAWIGGVGDCKlGG 248
Cdd:COG0115    79 ANGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 249 NYGPTVAVQQEAQKKGCEQVLWLyGPDHQLTEVGTMNIFVYwthEDGelELATPPLDGIILPGVVRQSLLDLARTWGeFR 328
Cdd:COG0115   150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDG--VLVTPPLSGGILPGITRDSVIELARELG-IP 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958649257 329 VAERKVTMKELKRAleegrvREVFGSGTACQVCPVHQIlyEGKQlhIPTMENGPeLILRFQKELKAIQYGTSA 401
Cdd:COG0115   223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGRP--IGDGKPGP-VTRRLRELYTDIVRGEAE 284
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 116-366 8.60e-34

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: 125.55  E-value: 8.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 116 QLFEGLKAYKGRdkqvrLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIEVDKDWVPdgngtslYVRPVLIGNEP 194
Cdd:pfam01063   1 GVFETLRVYNGK-----IFFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 195 SLGV-GMVTQALLFVILCPVGSYFPGDSMTPVSLLADPSFVRAwiggvgDCKlGGNYGPTVAVQQEAQKKGCEQVLwLYG 273
Cdd:pfam01063  69 GFGLpTSDPTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 274 PDHQLTEVGTMNIFvyWTHEDgelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRAleegrvREVFG 353
Cdd:pfam01063 141 EDGNVTEGSTSNVF--LVKGG---TLYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFL 208

                         250
                  ....*....|...
gi 1958649257 354 SGTACQVCPVHQI 366
Cdd:pfam01063 209 TNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 103-398 9.73e-127

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: 366.91  E-value: 9.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 103 TLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDGNGTS 182
Cdd:cd01557     1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 183 LYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGdSMTPVSLLADpSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQK 262
Cdd:cd01557    81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 263 KGCEQVLWLYGPDHQLTEVGTMNIFVYWtheDGelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRA 342
Cdd:cd01557   159 KGYDQALWLDGAHGYVAEVGTMNIFFVK---DG--ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649257 343 LeegrvrEVFGSGTACQVCPVHQILYEGKQlhiPTMENGPELILRFQKELKAIQYG 398
Cdd:cd01557   233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
 57-408 3.06e-124

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 363.31  E-value: 3.06e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  57 TREPQKKPAPSQPLlFGKTFTDHMLMVEWnSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRP 136
Cdd:PRK13357   10 TSDEKRAIDWANLG-FGYVFTDHMVVIDY-KDGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 137 WLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWV-PDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGS 215
Cdd:PRK13357   88 DANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 216 YFPGDsMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWLYGPDHQ-LTEVGTMNIF-VYwthE 293
Cdd:PRK13357  168 YFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFfIT---K 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 294 DGELelaTPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRALEEGRVREVFGSGTACQVCPVHQILYEGKQL 373
Cdd:PRK13357  244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958649257 374 HIPTMENGPeLILRFQKELKAIQYGTSA--HDWMLRV 408
Cdd:PRK13357  320 VIGDGEVGP-VTQKLYDELTGIQFGDVEdpHGWIVKV 355
ilvE_II TIGR01123
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ...
 91-408 3.40e-97

branched-chain amino acid aminotransferase, group II; 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 less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 233278  Cd Length: 313  Bit Score: 292.82  E-value: 3.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  91 WGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEV 170
Cdd:TIGR01123   1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 171 DKDWVPD-GNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSmTPVSLLADPSFVRAWIGGVGDCKLGGN 249
Cdd:TIGR01123  81 NKDWVPPyGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 250 YGPTVAVQQEAQKKGCEQVLWLYGPDHQ-LTEVGTMNIF-VYwthedGELELATPPLDGIILPGVVRQSLLDLARTWGeF 327
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTyIEEVGAMNFFfIT-----GDGELVTPPLSGSILPGITRDSLLQLAKDLG-M 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 328 RVAERKVTMKELKRALEEGrvREVFGSGTACQVCPVHQILYEGKQLHIPTMENGpELILRFQKELKAIQYGTSA--HDWM 405
Cdd:TIGR01123 234 EVEERRIDIDELKAFVEAG--EIVFACGTAAVITPVGEIQHGGKEVVFASGQPG-EVTKALYDELTDIQYGDFEdpYGWI 310


                  ...
gi 1958649257 406 LRV 408
Cdd:TIGR01123 311 VEV 313
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 109-392 1.53e-78

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: 242.89  E-value: 1.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 109 SGLHYSLQLFEGLKAYKGRdkqvrLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIEVdkdwvpdGNGTSLYVRP 187
Cdd:cd00449     2 RGLHYGDGVFEGLRAGKGR-----LFRLDEHLDRLNRSAKRLGLPiPYDREELREALKELVAA-------NNGASLYIRP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 188 VLIGNEPSLGVGM--VTQALLFVILCPVGSYFPGdSMTPVSLLADPSFVRAWIGGVGDCKLGGNYgPTVAVQQEAQKKGC 265
Cdd:cd00449    70 LLTRGVGGLGVAPppSPEPTFVVFASPVGAYAKG-GEKGVRLITSPDRRRAAPGGTGDAKTGGNL-NSVLAKQEAAEAGA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 266 EQVLWLYGpDHQLTEVGTMNIFVYWtheDGELelATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRAlee 345
Cdd:cd00449   148 DEALLLDD-NGYVTEGSASNVFIVK---DGEL--VTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA--- 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958649257 346 grvREVFGSGTACQVCPVHQILYEGKqlhipTMENGPELILRFQKEL 392
Cdd:cd00449   218 ---DEVFLTGTAAEVTPVTEIDGRGI-----GDGKPGPVTRKLRELL 256
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 91-401 2.86e-70

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: 222.76  E-value: 2.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  91 WGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGrdkqvRLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIE 169
Cdd:COG0115     4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 170 VDKDwvpdgngTSLYVRPVLIGNEPSLGVGMVT-QALLFVILCPVGSYFPGDSMTPVSLLADPsFVRAWIGGVGDCKlGG 248
Cdd:COG0115    79 ANGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 249 NYGPTVAVQQEAQKKGCEQVLWLyGPDHQLTEVGTMNIFVYwthEDGelELATPPLDGIILPGVVRQSLLDLARTWGeFR 328
Cdd:COG0115   150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDG--VLVTPPLSGGILPGITRDSVIELARELG-IP 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958649257 329 VAERKVTMKELKRAleegrvREVFGSGTACQVCPVHQIlyEGKQlhIPTMENGPeLILRFQKELKAIQYGTSA 401
Cdd:COG0115   223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGRP--IGDGKPGP-VTRRLRELYTDIVRGEAE 284
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
 8-373 2.16e-60

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 200.85  E-value: 2.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257   8 TLPRLGAGRSNFPTPQVWARKLLPIPWRLCVPGRCVSSNFKA-ADLQVQVTREPQKKPAPSQPLLFGKTFTDHMLMVEWN 86
Cdd:PLN02782   12 TRLHSSSRRLNFPPPSSLSLRHSNSSVSSNPISSKAISLTRCdAVSSSSYTEVTELADIDWDNLGFGLVPTDYMYIMKCN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  87 SKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQ 166
Cdd:PLN02782   92 RDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRNGAERMCMPAPTVEQFVEAVKE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 167 LIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPgDSMTPVSLLADPSFVRAWIGGVGDCKL 246
Cdd:PLN02782  172 TVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFK-EGVAPINLIVENEFHRATPGGTGGVKT 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 247 GGNYGPTVAVQQEAQKKGCEQVLWLygpD--HQ--LTEVGTMNIFVYWTHedgelELATPPLDGIILPGVVRQSLLDLAR 322
Cdd:PLN02782  251 IGNYAAVLKAQSIAKAKGYSDVLYL---DcvHKkyLEEVSSCNIFIVKDN-----VISTPAIKGTILPGITRKSIIDVAR 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958649257 323 TWGeFRVAERKVTMKELKRAleegrvREVFGSGTACQVCPVHQILYEGKQL 373
Cdd:PLN02782  323 SQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRV 366
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 70-408 2.29e-54

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 183.98  E-value: 2.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  70 LLFGKTFTDHMLMVEWNSKTGWGPPRIQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARR 149
Cdd:PLN03117   25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGADR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 150 LCLPDFDKQELLECIRQLIEVDKDWVPDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPGDSmtPVSLLA 229
Cdd:PLN03117  105 LCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASS--GLNLKV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 230 DPSFVRAWIGGVGDCKLGGNYGPTVAVQQEAQKKGCEQVLWL-YGPDHQLTEVGTMNIFVYwtheDGELeLATPPLDGII 308
Cdd:PLN03117  183 DHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdAATGKNIEELSACNIFIL----KGNI-VSTPPTSGTI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 309 LPGVVRQSLLDLARTWGeFRVAERKVTMKELKRAleegrvREVFGSGTACQVCPVHQILYEGKQLHIPTMENGpeLILRF 388
Cdd:PLN03117  258 LPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--LSTKL 328

                         330       340
                  ....*....|....*....|..
gi 1958649257 389 QKELKAIQYGT--SAHDWMLRV 408
Cdd:PLN03117  329 HLILTNIQMGVveDKKGWMVEI 350
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
 99-408 4.41e-47

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 165.66  E-value: 4.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  99 FQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWVPDG 178
Cdd:PLN02883   86 YGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPP 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 179 NGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPgDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVAVQQ 258
Cdd:PLN02883  166 GKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFK-EGTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMR 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 259 EAQKKGCEQVLWLYG-PDHQLTEVGTMNIFVYWTHedgelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMK 337
Cdd:PLN02883  245 RAKSRGFSDVLYLDAdTGKNIEEVSAANIFLVKGN-----IIVTPATSGTILGGITRKSIIEIALDLG-YKVEERRVPVE 318

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958649257 338 ELKRAleegrvREVFGSGTACQVCPVHQILYEGKQLHIPTMENGPELILRfqKELKAIQYGT--SAHDWMLRV 408
Cdd:PLN02883  319 ELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLR--SILLGIQTGSiqDTKDWVLQI 383
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
 27-398 2.47e-46

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 163.74  E-value: 2.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  27 RKLLPIPWRLCVpgRCVSSNFKAADLQVQVTREPQKKPAPSQ-----------PLLFGKTFTDHMLMVEWNSKTGWGPPR 95
Cdd:PLN02259    9 RKTLVLPLHLHI--RTLQTFAKYNAQAASALREERKKPLYQNgddvyadldwdNLGFGLNPADYMYVMKCSKDGEFTQGE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  96 IQPFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVRLFRPWLNMDRMLRSARRLCLPDFDKQELLECIRQLIEVDKDWV 175
Cdd:PLN02259   87 LSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 176 PDGNGTSLYVRPVLIGNEPSLGVGMVTQALLFVILCPVGSYFPgDSMTPVSLLADPSFVRAWIGGVGDCKLGGNYGPTVA 255
Cdd:PLN02259  167 PPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFK-EGMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLK 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 256 VQQEAQKKGCEQVLWLYGPDHQ-LTEVGTMNIFVYWTHedgelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKV 334
Cdd:PLN02259  246 ALSRAKSRGFSDVLYLDSVKKKyLEEASSCNVFVVKGR-----TISTPATNGTILEGITRKSVMEIASDQG-YQVVEKAV 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958649257 335 TMKELKRAleegrvREVFGSGTACQVCPVHQILYEGKQLHIPTMENgpELILRFQKELKAIQYG 398
Cdd:PLN02259  320 HVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SVCQKLRSVLVGIQTG 375
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 116-366 8.60e-34

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: 125.55  E-value: 8.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 116 QLFEGLKAYKGRdkqvrLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIEVDKDWVPdgngtslYVRPVLIGNEP 194
Cdd:pfam01063   1 GVFETLRVYNGK-----IFFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 195 SLGV-GMVTQALLFVILCPVGSYFPGDSMTPVSLLADPSFVRAwiggvgDCKlGGNYGPTVAVQQEAQKKGCEQVLwLYG 273
Cdd:pfam01063  69 GFGLpTSDPTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 274 PDHQLTEVGTMNIFvyWTHEDgelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRAleegrvREVFG 353
Cdd:pfam01063 141 EDGNVTEGSTSNVF--LVKGG---TLYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFL 208

                         250
                  ....*....|...
gi 1958649257 354 SGTACQVCPVHQI 366
Cdd:pfam01063 209 TNSLRGVTPVSSI 221
ilvE_I TIGR01122
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ...
 98-366 3.95e-24

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: 101.28  E-value: 3.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  98 PFQNLTLHPACSGLHYSLQLFEGLKAYKGrDKQVRLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIEVDkdwvp 176
Cdd:TIGR01122   8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEiPYSKEELMEATRETLRKN----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 177 dgNGTSLYVRPVLIGNEPSLGVGMVTQAL--LFVILCPVGSYFpGDSMTPVSLLAD-PSFVRAWIGGV-GDCKLGGNYGP 252
Cdd:TIGR01122  82 --NLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYL-GEEALEKGIDAKvSSWRRNAPNTIpTAAKAGGNYLN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 253 TVAVQQEAQKKGCEQVLWLyGPDHQLTEVGTMNIFVYwthEDGelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAER 332
Cdd:TIGR01122 159 SLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIFIV---KDG--VLFTPPVTSSILPGITRDTVITLAKELG-IEVVEQ 231

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958649257 333 KVTMKELKRAleegrvREVFGSGTACQVCPVHQI 366
Cdd:TIGR01122 232 PISREELYTA------DEAFFTGTAAEITPIREV 259
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 109-366 5.29e-24

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: 100.37  E-value: 5.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 109 SGLHYSLQLFEGLKAYKGRdkqvrLFRPWLNMDRMLRSARRLCLPD-FDKQELLECIRQLIEvdKDWVPDGNGtslYVRP 187
Cdd:cd01558    19 RGFLFGDGVYEVIRVYNGK-----PFALDEHLDRLYRSAKELRIDIpYTREELKELIRELVA--KNEGGEGDV---YIQV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 188 vlignepSLGVGMV-------TQALLFVILCPVGSYFPGDSMTPVSLLADPsfVRAWiggvGDCKL-GGNYGPTVAVQQE 259
Cdd:cd01558    89 -------TRGVGPRghdfpkcVKPTVVIITQPLPLPPAELLEKGVRVITVP--DIRW----LRCDIkSLNLLNNVLAKQE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 260 AQKKGCEQVlWLYGPDHQLTEVGTMNIFVYwthEDGELElaTPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKEL 339
Cdd:cd01558   156 AKEAGADEA-ILLDADGLVTEGSSSNVFIV---KNGVLV--TPPLDNGILPGITRATVIELAKELG-IPVEERPFSLEEL 228

                         250       260
                  ....*....|....*....|....*..
gi 1958649257 340 KRAleegrvREVFGSGTACQVCPVHQI 366
Cdd:cd01558   229 YTA------DEVFLTSTTAEVMPVVEI 249
PRK06606 PRK06606
branched-chain amino acid transaminase;
98-366 2.25e-23

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 99.07  E-value: 2.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  98 PFQNLTLHPACSGLHYSLQLFEGLKAYKGRDKQVrLFRPWLNMDRMLRSARRLCLP-DFDKQELLECIRQLIEVdkdwvp 176
Cdd:PRK06606   17 PWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAKILRMEiPYSVDELMEAQREVVRK------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 177 dgNG-TSLYVRP-VLIGNEpSLGV---GMVTQALLFVIlcPVGSYFPGDSMTP-----VS---LLADPSF-VRAwiggvg 242
Cdd:PRK06606   90 --NNlKSAYIRPlVFVGDE-GLGVrphGLPTDVAIAAW--PWGAYLGEEALEKgirvkVSswtRHAPNSIpTRA------ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 243 dcKLGGNYGPTVAVQQEAQKKGCEQVLWLyGPDHQLTEVGTMNIFVYwthEDGelELATPPLDGIILPGVVRQSLLDLAR 322
Cdd:PRK06606  159 --KASGNYLNSILAKTEARRNGYDEALLL-DVEGYVSEGSGENIFIV---RDG--VLYTPPLTSSILEGITRDTVITLAK 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958649257 323 TWGeFRVAERKVTMKELKRAleegrvREVFGSGTACQVCPVHQI 366
Cdd:PRK06606  231 DLG-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREV 267
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 110-366 2.99e-16

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: 77.73  E-value: 2.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 110 GLHYSLQLFEGLKAYKGRdkqvrlfRPWLN--MDRMLRSARRLCLPDFDKQELLECIRQLIEVDKdwVPDGngtslYVRp 187
Cdd:cd01559     3 GFAYGDGVFETMRALDGR-------LFLLDahLARLERSARRLGIPEPDLPRLRAALESLLAAND--IDEG-----RIR- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 188 VLIGNEPSlGVGMVTQAllfvilCPVGSYFPGDSMTPVSLLADPsfVRAWIGGVGDCKLGG-------NYGPTVAVQQEA 260
Cdd:cd01559    68 LILSRGPG-GRGYAPSV------CPGPALYVSVIPLPPAWRQDG--VRLITCPVRLGEQPLlaglkhlNYLENVLAKREA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 261 QKKGCEQVLWLYGPDHqLTEVGTMNIFvyWTHeDGELelATPPLDGIILPGVVRQSLLDLARTWGEfRVAERKVTMKELK 340
Cdd:cd01559   139 RDRGADEALFLDTDGR-VIEGTASNLF--FVK-DGEL--VTPSLDRGGLAGITRQRVIELAAAKGY-AVDERPLRLEDLL 211

                         250       260
                  ....*....|....*....|....*.
gi 1958649257 341 RAleegrvREVFGSGTACQVCPVHQI 366
Cdd:cd01559   212 AA------DEAFLTNSLLGVAPVTAI 231
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 98-366 3.96e-12

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 66.54  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257  98 PFQNLTLHPACSGLHYSLQLFEGLKAYKGRdkqvrLFRPWLNMDRMLRSARRLclpDFD----KQELLECIRQLIEVdkd 173
Cdd:PRK07544   19 PWRDAKVHVLTHGLHYASSVFEGERAYGGK-----IFKLREHSERLRRSAELL---DFEipysVAEIDAAKKETLAA--- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 174 wvpdgNG-TSLYVRPVLIGNEPSLGVGMVTQALLFVILC-PVGSYF-PGDSMTPVSL-LA-----DPSF--VRAwiggvg 242
Cdd:PRK07544   88 -----NGlTDAYVRPVAWRGSEMMGVSAQQNKIHLAIAAwEWPSYFdPEAKMKGIRLdIAkwrrpDPETapSAA------ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 243 dcKLGGNYGPTVAVQQEAQKKGCEQVLWLygpDH--QLTEVGTMNIFVYwthEDGELELATPP--LDGIilpgvVRQSLL 318
Cdd:PRK07544  157 --KAAGLYMICTISKHAAEAKGYADALML---DYrgYVAEATGANIFFV---KDGVIHTPTPDcfLDGI-----TRQTVI 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958649257 319 DLARTWGeFRVAERKVTMKELKRAleegrvREVFGSGTACQVCPVHQI 366
Cdd:PRK07544  224 ELAKRRG-IEVVERHIMPEELAGF------SECFLTGTAAEVTPVSEI 264
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 110-366 1.13e-11

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 64.89  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 110 GLHYSLQLFEGLKAYKGRdkqvrLFRPWLNMDRMLRSARRLCL-PDFDKQELLECIRQLIEVDkdwvpdgNGTSLYVRPV 188
Cdd:PRK08320   25 GFLYGDGVFEGIRAYNGR-----VFRLKEHIDRLYDSAKAIMLeIPLSKEEMTEIVLETLRKN-------NLRDAYIRLV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 189 LignepSLGVGMV-------TQALLFVILCPVGSYfPGDsMTPVSLLADPSFVRAWIGGVGDCKLGG-NYGPTVAVQQEA 260
Cdd:PRK08320   93 V-----SRGVGDLgldprkcPKPTVVCIAEPIGLY-PGE-LYEKGLKVITVSTRRNRPDALSPQVKSlNYLNNILAKIEA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 261 QKKGCEQVLWLygpDHQ--LTEVGTMNIFVYwthEDGELelATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKE 338
Cdd:PRK08320  166 NLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGKL--ITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTLHD 236

                         250       260
                  ....*....|....*....|....*...
gi 1958649257 339 LKRAleegrvREVFGSGTACQVCPVHQI 366
Cdd:PRK08320  237 LYTA------DEVFLTGTAAEVIPVVKV 258
PRK07849 PRK07849
aminodeoxychorismate lyase;
118-342 9.35e-07

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 49.96  E-value: 9.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 118 FEGLKAYKGRdkqVRLFRPWLnmDRMLRSARRLCLPDFDKQELLECIRQLIEvdkDWvpDGNGTSLYVRPVLignepSLG 197
Cdd:PRK07849   42 FETLLVRDGR---PCNLEAHL--ERLARSAALLDLPEPDLDRWRRAVELAIE---EW--RAPEDEAALRLVY-----SRG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 198 VGMVTQALLFVILCPVGSYFPGDSMTPVSLLADPsfvRAWIGGVGDCK---LGG----NYGPTVAVQQEAQKKGCEQVLW 270
Cdd:PRK07849  107 RESGGAPTAWVTVSPVPERVARARREGVSVITLD---RGYPSDAAERApwlLAGaktlSYAVNMAALRYAARRGADDVIF 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649257 271 LyGPDHQLTEVGTMNifVYWTHEDgelELATPPLDGIILPGVVRQSLLDLARTWGeFRVAERKVTMKELKRA 342
Cdd:PRK07849  184 T-STDGYVLEGPTST--VVIATDD---RLLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 110-363 9.59e-07

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 50.02  E-value: 9.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 110 GLHYSLQLFEGLKAYKGrdkQVRLFRPwlNMDRMLRSARR--LCLPdFDKQELLECIRQLIEvDKDWVPDGngtSLYVrp 187
Cdd:PRK12400   29 GLQFGDGVYEVIRLYKG---NFHLLDP--HITRLYRSMEEieLTLP-FSKAELITLLYKLIE-NNNFHEDG---TIYL-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 188 vlignEPSLGVGMVTQALLFVILCPVGSYfpgdsmtpVSLLADPSF-----VRA-------WIggvgDCKLGG-NYGPTV 254
Cdd:PRK12400   97 -----QVSRGVQARTHTFSYDVPPTIYAY--------ITKKERPALwieygVRAisepdtrWL----RCDIKSlNLLPNI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 255 AVQQEAQKKGCEQVLWLYgpDHQLTEVGTMNIFVYwthEDGELelATPPLDGIILPGVVRQSLLDLARTWgEFRVAERKV 334
Cdd:PRK12400  160 LAATKAERKGCKEALFVR--NGTVTEGSHSNFFLI---KNGTL--YTHPANHLILNGIIRQYVLSLAKTL-RIPVQEELF 231

                         250       260
                  ....*....|....*....|....*....
gi 1958649257 335 TMKELKRAleegrvREVFGSGTACQVCPV 363
Cdd:PRK12400  232 SVRDVYQA------DECFFTGTTIEILPM 254
PRK07546 PRK07546
hypothetical protein; Provisional
 277-342 5.48e-05

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 43.81  E-value: 5.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649257 277 QLTEVGTMNIFVywthEDGELELATPPLDGIILPGVVRQSLLDlartwgEFRVAERKVTMKELKRA 342
Cdd:PRK07546  136 EVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSA 191
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 249-344 9.72e-05

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 44.24  E-value: 9.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649257 249 NYGPTVAVQQEAQKKGCEQVLWLYGpDHQLTEVGTMNI-FVywTHEDgelELATPPLDGiILPGVVRQSLLDLA---RTW 324
Cdd:PLN02845  188 NYLPNALSQMEAEERGAFAGIWLDE-EGFVAEGPNMNVaFL--TNDG---ELVLPPFDK-ILSGCTARRVLELAprlVSP 260

                          90       100
                  ....*....|....*....|.
gi 1958649257 325 GEFR-VAERKVTMKELKRALE 344
Cdd:PLN02845  261 GDLRgVKQRKISVEEAKAADE 281
 
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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